1.I.1 The Eukaryotic Nuclear Pore Complex (E-NPC) Family [formerly 1.A.75]

Numerous NPC proteins, called nucleoporins, have been identified and characterized from vertebrates and yeast (Brohawn et al., 2009). Thirty such proteins are recognized constituents of the yeast NPC, and at least 50 nucleopore proteins have been characterized from vertebrates. Many of these proteins have been tabulated for (1) S. cerevisiae and (2) vertebrates by Stoffler et al. (1999) and Tran and Wente (2006). How they function in transport is poorly defined. It is known, however, that nuclear proteins contain short sequences called 'nuclear localization sequences' (NLS) that target them for nuclear import. A nuclear localization sequence receptor and several cytosolic factors appear to play roles in nuclear import of NLS-bearing proteins. Nuclear export signals (NESs) have also been identified. Several different forms of each type of targeting signal have been identified that lack homology to each other and may be recognized by different receptors. NLS and NES receptors (termed importins and exportins, respectively) may all be homologous and are members of the karyopherin-β/importin-βsuperfamily (Sorokin et al., 2008). The many protein constituents of NPCs have been discussed from structural, topological and functional standpoints by Panté and Aebi (1996), Nigg (1997) and Stoffler et al. (1999). Evidence for an involvement of the specific receptors or shuttling vectors, such as the importin-β-family member, Msn5 (spP52918), has been presented (Kaffman et al., 1998). Structural features and functional correlates have been discussed by Talcott and Moore (1999) as well as Gorlich and Kutay (Görlich and Kutay, 1999).The Nuclear Pore Complex (NPC) facilitates molecular trafficking between nucleus and cytoplasm and is an integral feature of the eukaryote cell, and LINC complexes can affect nucleo-cytoplasmic transport through the NPC (Jahed et al. 2016).  The NPC exhibits eight-fold rotational symmetry and is comprised of approximately 30 nucleoporins (Nups) in different stoichiometries. Nups are broadly conserved between yeast, vertebrates and plants, but few have been identified among other major eukaryotic groups.

The Nuclear Pore Complex (NPC) exhibits eight-fold rotational symmetry and is comprised of approximately 30 nucleoporins (Nups) in different stoichiometries. Nups are broadly conserved between yeast, vertebrates and plants. Neumann et al. (Neumann et al., 2010) screened for Nups across 60 eukaryote genomes and reported that 19 Nups (spanning all major protein subcomplexes) are found in all eukaryote supergroups studied (Opisthokonts, Amoebozoa, Viridiplantae, Chromalveolates and Excavates). Based on parsimony, between 23 and 26 of 31 Nups can be placed in the last eukaryotic common ancestor (LECA). Notably, they include central components of the anchoring system (Ndc1 and Gp210) indicating that the anchoring system did not evolve by convergence, as has previously been suggested. These results significantly extend earlier results and, importantly, unambiguously place a fully-fledged NPC in LECA. Vesicle coating complexes share a common evolutionary origin with Nups, and can be traced back to LECA. Surprisingly, only three supergroup-level differences (one gain and two losses) between the constituents of COPI, COPII and Clathrin complexes were formed. The results indicated that all major protein subcomplexes in the Nuclear Pore Complex are traceable to the Last Eukaryotic Common Ancestor (LECA), regardless of the position of the root of the eukaryotic tree (Neumann et al., 2010).

The symmetric core of the nuclear pore complex can be considered as a series of concentric cylinders. A peripheral cylinder coating the pore membrane contains the elongated heptamer that harbors Sec13-Nup145C in its middle section. Sec13-Nup145C crystallizes as a hetero-octamer. Oligomerization of Sec13-Nup145C is due to numerous interacting surfaces in the hetero-octamer, which forms a slightly curved, yet rigid rod of sufficient length to span the entire height of the proposed membrane-adjacent cylinder. In concordance with the dimensions and symmetry of the nuclear pore complex core, Hsia et al. (2007) suggested that the cylinder is constructed of four antiparallel rings, each ring being composed of eight heptamers arranged in a head-to-tail fashion. This model suggests that the hetero-octamer vertically traverses and connects the four stacked rings. See Hsia et al., 2007 for a detailed picture of subcomplexes and thin arrangements in the NPC. Bilokapic and Schwartz (2012) have summarized the state of NPC structural efforts, described the breakthroughs of recent years, and pointed out the existing disputes in the field. Stuwe et al. 2015 have determined the crystal structure of the nuclear pore complex coat (~400 kilodaltons) from Saccharomyces cerevisiae at 7.4Å resolution.  More recently, the architecture of the symmetic core of the nuclear pore has been elucidated (Lin et al. 2016Stuwe et al. 2015; Stuwe et al. 2015). Cell stretching modulates the characteristic time needed for the nuclear import of small inert molecules (García-González et al. 2018).

Members of the importin-β family of transport receptors mediate NPC passage of cargo by interacting with nucleoporins and a small GTPase, Ran. Ran acts as a molecular switch by interconverting between a GTP and GDP binding state, regulated by a nuclear GTP/GDP exchange factor, RCC1, and a cytoplasmic GTPase-activating factor, RanGAP. The asymmetric distribution of these proteins insures that nuclear Ran is primarily in the GTP-bound form, but cytoplasmic Ran is in the GDP-bound form. This gradient of Ran-GTP ensures release of cargo from the transport importin-β receptors which bind NLS-substrate/importin-β complex in the cytoplasm, and this ternary complex dissociates by binding RanGTP to importin-β in the nucleus. While ATP (or GTP) is required for nuclear export of importin-β, it is not required for nuclear import. Smad2/Smad4 heterocomplexes, formed in the cytoplasm, are imported through the nuclear pore complex as entireties, and finally dissociate in the nucleus (Li et al. 2018).

Mediators of import into the nucleus (importins) and export mediators (exportins) interact with RanGTP but respond to the nucleocytoplasmic RanGTP gradient in diametrically opposed ways (Mingot et al., 2004). Importins bind cargo at low RanGTP levels in the cytoplasm and release cargo upon RanGTP binding in the nucleus. In contrast, exportins recruit cargo at high RanGTP concentrations, as ternary cargo/exportin/RanGTP complexes, in the nuclear compartment and release cargo when the Ran-bound GTP molecule is hydrolyzed in the cytoplasm. This active control of cargo binding and release by the RanGTPase system constitutes the sole input of metabolic enegy into these transport cycles and is sufficient to allow importins and exportins to accumulate cargoes actively against gradients of chemical activity.

Transport through the NPC occurs by facilitated diffusion of the soluble carrier proteins or carrier-cargo complexes (Macara, 2001). Vectorality is provided by compartment-specific assembly and disassembly of the carrier-cargo complexes, often mediated by the Ran GTPase as noted above. The carriers recognize localization signals on the cargo and bind to pore proteins (Macara, 2001). While the yeast NPC is complex, those in plants and animals are much more so with hundreds of proteins functioning in various capacities. Many of the yeast NPC constituents can be found in other eukaryotes (e.g., vertebrate centrins function as does Cdc31p of yeast and plays a role in mRNA and protein export) (Resendes et al., 2008). The RNA U small nuclear (sn)RNA export adaptor protein, or the phosphorylated adaptor for RNA export, regulates U snRNA nuclear export to the cytoplasm in metazoa. It is phosphorylated in the nucleus and exported as part of the U snRNA export complex where it is dephosphorylated, causing complex disassembly (Kitao et al., 2008).

Targeting of newly synthesized integral membrane proteins to the appropriate cellular compartment is specified by discrete sequence elements, many of which have been well characterized. An understanding of the signals required to direct integral membrane proteins to the inner nuclear membrane (INM) represent a notable exception. King et al. (2006) have shown that integral INM proteins possess basic sequence motifs that resemble 'classical' nuclear localization signals. These sequences can mediate direct binding to karyopherin-β and are essential for the passage of integral membrane proteins to the INM. Furthermore, karyopherin-β, karyopherin-β1 and the Ran GTPase cycle are required for INM targeting, underscoring parallels between mechanisms governing the targeting of integral INM proteins and soluble nuclear transport. King et al. (2006) provided evidence that specific nuclear pore complex proteins contribute to this process, suggesting a role for signal-mediated alterations in the nuclear pore complex to allow for passage of INM proteins along the pore membrane.

The transport receptor Mex67-Mtr2 functions in mRNA export, and also, using a loop-confined surface on the heterodimer, it binds to and exports pre-60S particles. Mex67-Mtr2, through the same surface that recruits pre-60S particles, interacts with the Nup84 complex, a structural module of the nuclear pore complex devoid of Phe-Gly domains (Yao et al., 2007). In vitro, pre-60S particles and the Nup84 complex compete for an overlapping binding site on the loop-extended Mex67-Mtr2 surface. Nup85 is the subunit in the Nup84 complex that binds to the Mex67 loop, an interaction that is crucial for mRNA export.

NPCs are proteinaceous assemblies of approximately 50 MDa of 456 known constituents that selectively transport cargoes across the nuclear envelope. Half of the NPC is made up of a core scaffold, which is structurally analogous to vesicle-coating complexes. This scaffold forms an interlaced network that coats the entire curved surface of the nuclear envelope membrane within which the NPC is embedded. The selective barrier for transport is formed by large numbers of proteins with disordered regions that line the inner face of the scaffold (Alber et al., 2007). The NPC consists of only a few structural modules that resemble each other in terms of the configuration of their homologous constituents. The most striking of these is a 16-fold repetition of 'columns'.

Trafficking of nucleic acids and large proteins through nuclear pore complexes (NPCs) requires interactions with NPC proteins that harbor FG (phenylalanine-glycine) repeat domains. Specialized transport receptors that recognize cargo and bind FG domains facilitate these interactions. Terry and Wente (2007) generated in S. cerevisiae a set of more minimal pore (mmp) mutants lacking specific FG domains. A comparison of messenger RNA (mRNA) export versus protein import reveals unique subsets of mmp mutants with functional defects in specific transport receptors. Thus, multiple functionally independent NPC translocation routes exist for different transport receptors. mRNA export also requires two NPC substructures-one on the nuclear NPC face and one in the NPC central core.

A novel family of NPC proteins, the FG-nucleoporins (FG-Nups), coordinates and potentially regulates NPC translocation. The extensive repeats of phenylalanine-glycine (FG) in each FG-Nup directly bind to shuttling transport receptors moving through the NPC. In addition, FG-Nups are essential components of the nuclear permeability barrier. Terry & Wente (2009) reviewed the structural features, cellular functions, and evolutionary conservation of the FG-Nups. The normal distribution of nuclear envelope transmembrane proteins (NETs) is disrupted in several human diseases. NETs are synthesized on the endoplasmic reticulum and then transported from the outer nuclear membrane (ONM) to the inner nuclear membrane (INM) (Mudumbi et al. 2016).

Large cargoes require multiple receptors for efficient transport through the nuclear pore complex. The 60S ribosomal subunit in yeast utilizes three different receptors, Crm1, Mex67/Mtr2, and Arx1 which collaborate in its export. However, only Crm1, recruited by the adapter Nmd3, appears to be conserved for 60S ribosomal subunit export in higher eukaryotes. Several receptors can function in export. This helps explain how different export receptors could have evolved. Lo and Johnson (2009) have reviewed the structural features, cellular functions, and evolutionary conservation of the FG-Nups.

Nuclear transport receptors (NTRs) bind cargo molecules and supply nuclei with proteins and the cytoplasm with nuclear products like ribosomes. The facilitated mode of NPC passage reaches a capacity of up to 1,000 translocation events per NPC per second and accommodates objects of up to nearly 40 nm in diameter (Hülsmann et al., 2012). NTRs can utilize an energy input, e.g., from the RanGTPase system to accumulate substrates against steep concentration gradients.

NPCs are built from ∼30 different nucleoporins (Nups) that can be classified into structural Nups and phenylalanine-glycine repeat-containing Nups (FG Nups). The structural Nups form the NPC scaffold and provide binding sites for the nonglobular FG Nups which are critical for the barrier. (Strawn et al., 2004; Frey and Görlich, 2007; Patel et al., 2007). An FG-Nup typically has hundreds of residues with up to 50 FG, FxFG, or GLFG motifs.

FG motifs bind NTRs during facilitated translocation and such interactions render NPCs 100- to >1,000-fold more permeable for NTR⋅cargo complexes than for inert objects of similar size. Molecules that are not bound to an NTR are blocked from NPC passage.

The favored 'selective phase model' (Hülsmann et al., 2012) assumes that the barrier-forming FG domains comprise many cohesive units, which bind each other and thereby mediate multivalent interactions within and between individual FG domains. Such interactions result in a sieve-like FG hydrogel that allows passage of small molecules but suppresses fluxes of larger ones. NTRs overcome this size limit by binding to FG motifs and consequently disengaging FG meshes in their immediate vicinity. This way, NTRs can partition into the FG hydrogel and exit the barrier on the trans side (Hülsmann et al., 2012).

Nuclear export of mRNAs was thought to occur exclusively through nuclear pore complexes. However, Speese et al. (2012) identified an alternate pathway for mRNA export in muscle cells where ribonucleoprotein complexes involved in forming neuromuscular junctions transit the nuclear envelope by fusing with and budding through the nuclear membrane.

Rothballer and Kutay (2013) have discussed the biogenesis of NPCs during interphase of the cell cycle. This process requires a mechanistically enigmatic fusion step between the inner and the outer nuclear membrane. They focus on the principle of membrane pore formation in the nuclear envelope and consider existing paradigms of other cellular membrane remodeling events. The emerging roles of transmembrane proteins and membrane-shaping factors in NPC biogenesis are discussed.

Linker of nucleoskeleton and cytoskeleton (LINC) complexes span the double membrane of the nuclear envelope (NE) and physically connect nuclear structures to cytoskeletal elements (Rothballer et al. 2013). LINC complexes are envisioned as force transducers in the NE, which facilitate processes like nuclear anchorage and migration or chromosome movements. The complexes are built from members of two evolutionary conserved families of transmembrane (TM) proteins, the SUN (Sad1/UNC-84) domain proteins in the inner nuclear membrane (INM) and the KASH (Klarsicht/ANC-1/SYNE homology) domain proteins in the outer nuclear membrane (ONM). In the lumen of the NE, the SUN and KASH domains engage in an intimate assembly to jointly form a NE bridge. Detailed insights into the molecular architecture and atomic structure of LINC complexes have recently revealed the molecular basis of nucleo-cytoskeletal coupling (Rothballer et al., 2013). They bear important implications for LINC complex function and suggest new potential and as yet unexplored roles, which the complexes may play in the cell. 

The majority of nuclear import pathways are mediated by importin-cargo interactions, but not all nuclear proteins interact with importins, necessitating the identification of a general importin-independent nuclear import pathway. Lu et al. 2014 identify a code that determines importin-independent nuclear import of ankyrin repeats (ARs), a structural motif found in over 250 human proteins with diverse functions. AR-containing proteins (ARPs) with a hydrophobic residue at the 13th position of two consecutive ARs bind RanGDP efficiently, and consequently enter the nucleus. This code predicts the nuclear-cytoplasmic localization of over 150 annotated human ARPs with high accuracy, leading to nuclear accumulation. The RaDAR (RanGDP/AR) pathway represents a general importin-independent nuclear import pathway used by AR-containing transcriptional regulators (Lu et al. 2014). 

Stuwe et al. 2015 presented the reconstitution of the ~425-kilodalton inner ring complex (IRC), which forms the central transport channel and diffusion barrier of the NPC, revealing its interaction network and equimolar stoichiometry. The Nsp1•Nup49•Nup57 channel nucleoporin heterotrimer (CNT) attaches to the IRC solely through the adaptor nucleoporin Nic96. The CNT•Nic96 structure reveals that Nic96 functions as an assembly sensor that recognizes the three-dimensional architecture of the CNT, thereby mediating the incorporation of a defined CNT state into the NPC. They proposed that the IRC adopts a relatively rigid scaffold that recruits the CNT to primarily form the diffusion barrier of the NPC, rather than enabling channel dilation (Stuwe et al. 2015). 

NPCs mediate nucleocytoplasmic transport and gain transport selectivity through nucleoporin FG domains. Chug et al. 2015 reported a structural analysis of the frog FG Nup62•58•54 complex. It comprises a ≈13 nanometer-long trimerization interface with an unusual 2W3F coil, a canonical heterotrimeric coiled coil, and a kink that enforces a compact six-helix bundle. Nup54 also contains a ferredoxin-like domain. Chug et al. 2015 further identified a heterotrimeric Nup93-binding module for NPC anchorage. The quaternary structure alternations in the Nup62 complex, which were previously proposed to trigger a general gating of the NPC, are incompatible with the trimer structure. Chug et al. 2015 suggested that the highly elongated Nup62 complex projects barrier-forming FG repeats far into the central NPC channel, supporting a barrier that guards the entire cross section.

Ciliates have two functionally distinct nuclei, a transcriptionally active somatic macronucleus (MAC) and a germline micronucleus (MIC) that develop from daughter nuclei of the last postzygotic division (PZD) during the sexual process of conjugation. Iwamoto et al. 2015 showed, by live-cell imaging of Tetrahymena, that biased assembly of the nuclear pore complex (NPC) occurs immediately after the last PZD, which generates anterior-posterior polarized nuclei: MAC-specific NPCs assemble in anterior presumptive MACs but not in posterior presumptive MICs. MAC-specific NPC assembly in the anterior nuclei occurs much earlier than transport of Twi1p, which is required for MAC genome rearrangement. Addition of new nuclear envelope (NE) precursors occured through the formation of domains of redundant NE, where the outer double membrane contains the newly assembled NPCs. Nocodazole inhibition of the second PZD resulted in assembly of MAC-specific NPCs in the division-failed zygotic nuclei, leading to failure of MIC differentiation. Thus, NPC type switching plays a crucial role in the establishment of nuclear differentiation in ciliates (Iwamoto et al. 2015). 

The NPCs in ciliates consists of about 30 different nucleoporins each. Iwamoto et al. 2017 presented evidence for compositionally distinct NPCs that form within a single cell of Tetrahymena thermophila. Each cell contains both a MAC and a MIC. Iwamoto et al. 2017 identified numerous novel components of MAC and MIC NPCs. Core members of the Nup107-160 scaffold complex were enriched in MIC NPCs. Two paralogs of Nup214 and of Nup153 localized exclusively to either MAC or MIC NPCs, and the transmembrane components, Pom121 and Pom82, localize exclusively to MAC and MIC NPCs, respectively. Thus, functional nuclear dimorphism in ciliates depends on compositional and structural differences. 

A protein known to localize to and be important in the assembly of both the yeast NPC and the spindle pole body, which functions as the microtubule organizing center, is the 6 TMS protein, Ndc1p (NPC1 in humans). The N- and C-termini of Ndc1p are exposed to the cytoplasm (Lau et al. 2006). The paralogous Brr6 and Brl1 are conserved integral membrane proteins of the nuclear envelope (NE). Depletion of Brr6 and Brl1 caused defects in NPC biogenesis, whereas the already assembled NPCs remained unaffected. This NPC biogenesis defect was not accompanied by a change in lipid composition. However, Brl1 interacted with Ndc1 and Nup188 as well as transmembrane and outer and inner ring NPC components, indicating a direct role in NPC biogenesis.Both Brr6 and Brl1 associated with a subpopulation of NPCs and emerging NPC assembly sites. BRL1 overexpression affected NE morphology and suppressed the nuclear pore biogenesis defect of Δnup116 and Δgle2 cells. Possibly Brr6 and Brl1 transiently associate with NPC assembly sites where they promote NPC biogenesis (Zhang et al. 2018).



This family belongs to the Ankyrin Repeat Domain-containing (Ank) Family, found in at least some proteins in the following TC families .

 

References:

Alber, F., S. Dokudovskaya, L.M. Veenhoff, W. Zhang, J. Kipper, D. Devos, A. Suprapto, O. Karni-Schmidt, R. Williams, B.T. Chait, A. Sali, and M.P. Rout. (2007). The molecular architecture of the nuclear pore complex. Nature 450: 695-701.

Bilokapic, S. and T.U. Schwartz. (2012). 3D ultrastructure of the nuclear pore complex. Curr. Opin. Cell Biol. 24: 86-91.

Brohawn, S.G., J.R. Partridge, J.R. Whittle, and T.U. Schwartz. (2009). The nuclear pore complex has entered the atomic age. Structure 17: 1156-1168.

Chug, H., S. Trakhanov, B.B. Hülsmann, T. Pleiner, and D. Görlich. (2015). Crystal structure of the metazoan Nup62•Nup58•Nup54 nucleoporin complex. Science 350: 106-110.

García-González, A., E. Jacchetti, R. Marotta, M. Tunesi, J.F. Rodríguez Matas, and M.T. Raimondi. (2018). The Effect of Cell Morphology on the Permeability of the Nuclear Envelope to Diffusive Factors. Front Physiol 9: 925.

Görlich, D. and U. Kutay. (1999). Transport between the cell nucleus and the cytoplasm. Annu. Rev. Cell Dev. Biol. 15: 607-660.

Hatch, E.M. and M.W. Hetzer. (2012). RNP Export by Nuclear Envelope Budding. Cell 149: 733-735.

Hsia, K.C., P. Stavropoulos, G. Blobel, and A. Hoelz. (2007). Architecture of a coat for the nuclear pore membrane. Cell 131: 1313-1326.

Hülsmann, B.B., A.A. Labokha, and D. Görlich. (2012). The permeability of reconstituted nuclear pores provides direct evidence for the selective phase model. Cell 150: 738-751.

Iwamoto, M., C. Mori, T. Kojidani, F. Bunai, T. Hori, T. Fukagawa, Y. Hiraoka, and T. Haraguchi. (2009). Two distinct repeat sequences of Nup98 nucleoporins characterize dual nuclei in the binucleated ciliate tetrahymena. Curr. Biol. 19: 843-847.

Iwamoto, M., H. Osakada, C. Mori, Y. Fukuda, K. Nagao, C. Obuse, Y. Hiraoka, and T. Haraguchi. (2017). Compositionally distinct nuclear pore complexes of functionally distinct dimorphic nuclei in ciliate Tetrahymena. J Cell Sci. [Epub: Ahead of Print]

Iwamoto, M., T. Koujin, H. Osakada, C. Mori, T. Kojidani, A. Matsuda, H. Asakawa, Y. Hiraoka, and T. Haraguchi. (2015). Biased assembly of the nuclear pore complex is required for somatic and germline nuclear differentiation in Tetrahymena. J Cell Sci 128: 1812-1823.

Jahed, Z., M. Soheilypour, M. Peyro, and M.R. Mofrad. (2016). The LINC and NPC relationship - it''s complicated! J Cell Sci. [Epub: Ahead of Print]

Kaffman, A., N.M. Rank, E.M. O'Neill, L.S. Huang, and E.K. O'Shea. (1998). The receptor Msn5 exports the phosphorylated transcription factor Pho4 out of the nucleus. Nature 396: 482-486.

King, M.C., C.P. Lusk, and G. Blobel. (2006). Karyopherin-mediated import of integral inner nuclear membrane proteins. Nature 442: 1003-1007.

Kitao, S., A. Segref, J. Kast, M. Wilm, I.W. Mattaj, and M. Ohno. (2008). A compartmentalized phosphorylation/dephosphorylation system that regulates U snRNA export from the nucleus. Mol. Cell Biol. 28: 487-497.

Laba, J.K., A. Steen, P. Popken, A. Chernova, B. Poolman, and L.M. Veenhoff. (2015). Active Nuclear Import of Membrane Proteins Revisited. Cells 4: 653-673.

Lau, C.K., V.A. Delmar, and D.J. Forbes. (2006). Topology of yeast Ndc1p: predictions for the human NDC1/NET3 homologue. Anat Rec A Discov Mol. Cell Evol Biol 288: 681-694.

Li, Y., W. Luo, and W. Yang. (2018). Nuclear Transport and Accumulation of Smad Proteins Studied by Single-Molecule Microscopy. Biophys. J. 114: 2243-2251.

Lin, D.H., T. Stuwe, S. Schilbach, E.J. Rundlet, T. Perriches, G. Mobbs, Y. Fan, K. Thierbach, F.M. Huber, L.N. Collins, A.M. Davenport, Y.E. Jeon, and A. Hoelz. (2016). Architecture of the symmetric core of the nuclear pore. Science 352: aaf1015.

Lo, K.Y. and A.W. Johnson. (2009). Reengineering ribosome export. Mol. Biol. Cell 20: 1545-1554.

Lu, M., J. Zak, S. Chen, L. Sanchez-Pulido, D.T. Severson, J. Endicott, C.P. Ponting, C.J. Schofield, and X. Lu. (2014). A Code for RanGDP Binding in Ankyrin Repeats Defines a Nuclear Import Pathway. Cell 157: 1130-1145.

Macara, I.G. (2001). Transport into and out of the nucleus. Microbiol. Mol. Biol. Rev. 65: 570-94, table of contents.

Madrid, A.S., J. Mancuso, W.Z. Cande, and K. Weis. (2006). The role of the integral membrane nucleoporins Ndc1p and Pom152p in nuclear pore complex assembly and function. J. Cell Biol. 173: 361-371.

Malone, C.D., K.A. Falkowska, A.Y. Li, S.E. Galanti, R.C. Kanuru, E.G. LaMont, K.C. Mazzarella, A.J. Micev, M.M. Osman, N.K. Piotrowski, J.W. Suszko, A.C. Timm, M.M. Xu, L. Liu, and D.L. Chalker. (2008). Nucleus-specific importin alpha proteins and nucleoporins regulate protein import and nuclear division in the binucleate Tetrahymena thermophila. Eukaryot. Cell. 7: 1487-1499.

Meinema, A.C., J.K. Laba, R.A. Hapsari, R. Otten, F.A. Mulder, A. Kralt, G. van den Bogaart, C.P. Lusk, B. Poolman, and L.M. Veenhoff. (2011). Long unfolded linkers facilitate membrane protein import through the nuclear pore complex. Science 333: 90-93.

Mingot, J.M., M.T. Bohnsack, U. Jäkle, and D. Görlich. (2004). Exportin 7 defines a novel general nuclear export pathway. EMBO. J. 23: 3227-3236.

Mudumbi, K.C., E.C. Schirmer, and W. Yang. (2016). Single-point single-molecule FRAP distinguishes inner and outer nuclear membrane protein distribution. Nat Commun 7: 12562.

Neumann, N., D. Lundin, and A.M. Poole. (2010). Comparative genomic evidence for a complete nuclear pore complex in the last eukaryotic common ancestor. PLoS One 5: e13241.

Nigg, E.A. (1997). Nucleocytoplasmic transport: signals, mechanisms and regulation. Nature 386: 779-787.

Panté, N. and U. Aebi. (1996). Molecular dissection of the nuclear pore complex. Crit. Rev. Biochem. Mol. Biol. 31: 153-199.

Resendes, K.K., B.A. Rasala, and D.J. Forbes. (2008). Centrin 2 localizes to the vertebrate nuclear pore and plays a role in mRNA and protein export. Mol. Cell Biol. 28: 1755-1769.

Rothballer A. and Kutay U. (2013). Poring over pores: nuclear pore complex insertion into the nuclear envelope. Trends Biochem Sci. 38(6):292-301.

Rothballer, A., T.U. Schwartz, and U. Kutay. (2013). LINCing complex functions at the nuclear envelope: what the molecular architecture of the LINC complex can reveal about its function. Nucleus 4: 29-36.

Schaller, T., L. Bulli, D. Pollpeter, G. Betancor, J. Kutzner, L. Apolonia, N. Herold, R. Burk, and M.H. Malim. (2017). Effects of the inner nuclear membrane proteins SUN1/UNC-84A and SUN2/UNC-84B on the early steps of HIV-1 infection. J. Virol. [Epub: Ahead of Print]

Speese, S.D., J. Ashley, V. Jokhi, J. Nunnari, R. Barria, Y. Li, B. Ataman, A. Koon, Y.T. Chang, Q. Li, M.J. Moore, and V. Budnik. (2012). Nuclear Envelope Budding Enables Large Ribonucleoprotein Particle Export during Synaptic Wnt Signaling. Cell 149: 832-846.

Stoffler, D., B. Fahrenkrog, and U. Aebi. (1999). The nuclear pore complex: from molecular architecture to functional dynamics. Curr. Opin. Cell Biol. 11: 391-401.

Stuwe, T., A.R. Correia, D.H. Lin, M. Paduch, V.T. Lu, A.A. Kossiakoff, and A. Hoelz. (2015). Nuclear pores. Architecture of the nuclear pore complex coat. Science 347: 1148-1152.

Stuwe, T., C.J. Bley, K. Thierbach, S. Petrovic, S. Schilbach, D.J. Mayo, T. Perriches, E.J. Rundlet, Y.E. Jeon, L.N. Collins, F.M. Huber, D.H. Lin, M. Paduch, A. Koide, V. Lu, J. Fischer, E. Hurt, S. Koide, A.A. Kossiakoff, and A. Hoelz. (2015). Architecture of the fungal nuclear pore inner ring complex. Science 350: 56-64.

Talcott, B. and M.S. Moore. (1999). Getting across the nuclear pore complex. Trends Cell Biol. 9: 312-318.

Terry, L.J. and S.R. Wente. (2007). Nuclear mRNA export requires specific FG nucleoporins for translocation through the nuclear pore complex. J. Cell Biol. 178: 1121-1132.

Terry, L.J. and S.R. Wente. (2009). Flexible gates: dynamic topologies and functions for FG nucleoporins in nucleocytoplasmic transport. Eukaryot. Cell. 8: 1814-1827.

Tran, E.J. and S.R. Wente. (2006). Dynamic nuclear pore complexes: life on the edge. Cell 125: 1041-1053.

Yao, W., D. Roser, A. Köhler, B. Bradatsch, J. Bassler, and E. Hurt. (2007). Nuclear export of ribosomal 60S subunits by the general mRNA export receptor Mex67-Mtr2. Mol. Cell 26: 51-62.

Zhang, W., A. Neuner, D. Rüthnick, T. Sachsenheimer, C. Lüchtenborg, B. Brügger, and E. Schiebel. (2018). Brr6 and Brl1 locate to nuclear pore complex assembly sites to promote their biogenesis. J. Cell Biol. [Epub: Ahead of Print]

Examples:

TC#NameOrganismal TypeExample
1.I.1.1.1

NPC (Tran and Wente, 2006).  The structure of the NPC core (400kD) has been determined at 7.4 Å resolution revealing a curved Y-shaped architecture with the coat nucleoporin interactions forming the central ""triskeleton"".  32 copies of the coat neucloporin complex (CNC) structure dock into the cryoelectron tomographic reconstruction of the assembled human NPC, thus accountng for ~16 MDa of it's mass (Stuwe et al. 2015).  Import of integral membrane proteins (mono- and polytopic) into the the inner nuclear membrane occurs by an active, transport factor-dependent process (Laba et al. 2015). Ndc1 and Pom52 are partially redundant NPC components that are essential for proper assembly of the NPC. The absence of Ndc1p and Pom152p results in aberrant pores that have enlarged diameters and lack proteinaceous material, leading to increased diffusion between the cytoplasm and the nucleus (Madrid et al. 2006).

Yeast

Well-characterized nucleoporins of Saccharomyces cerevisiae
CDC31p (161 aa; P06704)
GLE1p (538 aa; Q12315)
GLE2p (365 aa; P40066)
Mex67 r and m RNA export factor (599aas; Q99257)
Mlp1 (1875 aas; Q02455)
Mlp2 (1679 aas; P40457)
Mtr2 r and m RNA export regulator (184aas; P34232)
Ndc1p (655 aa; NP_013681; P32500)
Nic96p (839 aa; NP_116657; P34077)
Nsp1p (823 aa; NP_012494; P14907)
Nup1p (1076 aa; NP_014741; P20676)
Nup2p (720 aa; AAB67259; P32499)
Nup42p (430 aa; P49686)
Nup49p (472 aa; NP_011343; Q02199)
Nup53p (475 aa; NP_013873; Q03790)
Nup57p (541 aa; NP_011634; P48837)
Nup59p (528 aa; Q05166)
Nup60p (539 aa; P39705)
Nup82p (713 aa; NP_012474; P40368)
Nup84p (726 aa; P52891)
Nup85p (744 aa; P46673)
Nup100p (959 aa; NP_012855; Q02629)
Nup116p (1113 aa; NP_013762; Q02630)
Nup120p (Rat2p) (1037 aa; NP_012866; P35729)
Nup133p (Rat3p) (1157 aa; CAA56372; P36161)
Nup145p (1317 aa; CAA54057; P49687)
Nup157p (1391 aa; NP_011031; P40064)
Nup159p (Rat7p) (1460 aa; NP_012151; P40477)
Nup170p (1502 aa; NP_009474; P38181)
Nup188p (1655 aa; NP_013604; P52593)
Nup192p (1683 aa; P47054)
Pom34p (299 aa; Q12445)
Pom152p (1337 aa; CAA88554; P39685)
Rip1p (215 aa; NP_010890; P08067)
Seh1p (349 aa; P53011)
Snl1p (159 aa; NP_012248; P40548)
U snRNA export adaptor protein (Q63068)

 
1.I.1.1.2

Fungal Nuclear Pore Complex (NPC) with 29 components.  Stuwe et al. 2015 presented the reconstitution of the ~425-kilodalton inner ring complex (IRC), which forms the central transport channel and diffusion barrier of the NPC, revealing its interaction network and equimolar stoichiometry. The Nsp1•Nup49•Nup57 channel nucleoporin heterotrimer (CNT) attaches to the IRC solely through the adaptor nucleoporin Nic96. The CNT•Nic96 structure reveals that Nic96 functions as an assembly sensor that recognizes the three-dimensional architecture of the CNT, thereby mediating the incorporation of a defined CNT state into the NPC. They proposed that the IRC adopts a relatively rigid scaffold that recruits the CNT to primarily form the diffusion barrier of the NPC, rather than enabling channel dilation (Stuwe et al. 2015).

NPC of Chaetomium thermophilum

Nucleoporin NUP192 (Nuclear pore protein NUP192); 1756aa; G0S4T0
Nucleoporin NUP145 (EC 3.4.21.-) (Nuclear pore protein NUP145) [Cleaved into: Nucleoporin NUP145N (N-NUP145); Nucleoporin NUP145C (C-NUP145)]; 1793aa; G0SAK3
Nucleoporin SEH1 (Nuclear pore protein SEH1); 538aa; G0S450
Nucleoporin GLE1 (Nuclear pore protein GLE1) (RNA export factor GLE1); 529aa; G0S7F3
Nucleoporin GLE2 (Nuclear pore protein GLE2); 357aa; G0SEA3
Nucleoporin NDC1 (Nuclear pore protein NDC1); 646aa; G0S235
Nucleoporin NUP82 (Nuclear pore protein NUP82); 882aa; G0S4F3
Nucleoporin POM152 (Nuclear pore protein POM152) (Pore membrane protein POM152); 1270aa; G0SB44
Protein transport protein SEC13; 308aa; G0SA60
Nucleoporin AMO1 (Nuclear pore protein AMO1); 557aa; G0S381
Nucleoporin NSP1 (Nuclear pore protein NSP1) (Nucleoskeletal-like protein); 678aa; G0SBQ3
Nucleoporin NUP152 (Nuclear pore protein NUP152); 1463aa; G0SDP9
Nucleoporin NUP159 (Nuclear pore protein NUP159); 1481aa; G0SBS8
Nucleoporin NUP53 (Nuclear pore protein NUP53); 426aa; G0S156
Nucleoporin NUP49 (Nuclear pore protein NUP49); 470aa; G0S4X2
Nucleoporin NUP57 (Nuclear pore protein NUP57); 326aa; G0S0R2
Nucleoporin NUP56 (Nuclear pore protein NUP56); 524aa; G0S8I1
Protein ELYS; 299aa; G0S2G1
Nucleoporin NIC96 (Nuclear pore protein NIC96); 1112aa; G0S024
Nucleoporin NUP120 (Nuclear pore protein NUP120); 1262aa; G0S0E7
Nucleoporin NUP133 (Nuclear pore protein NUP133); 1364aa; G0S9A7
Nucleoporin NUP170 (Nuclear pore protein NUP170); 1416aa; G0S7B6
Nucleoporin NUP188 (Nuclear pore protein NUP188); 1858aa; G0SFH5
Nucleoporin NUP84 (Nuclear pore protein NUP84); 948aa; G0SER9
Nucleoporin NUP85 (Nuclear pore protein NUP85); 1169aa; G0SDQ4
Nucleoporin NUP37 (Nuclear pore protein NUP37); 751aa; G0S2X1
Nucleoporin POM33 (Nuclear pore protein POM33) (Pore membrane protein of 33 kDa); 287aa; G0S6T0
Nucleoporin POM34 (Nuclear pore protein POM34) (Pore membrane protein of 34 kDa); 326aa; G0S7R3
Protein MLP1 homologue; 2085aa; G0SA56

 
1.I.1.1.3

Nuclear Pore Complex, NPC with 86 protein components.  NPCs mediate nucleocytoplasmic transport and gain transport selectivity through nucleoporin FG domains. Chug et al. 2015 reported a structural analysis of the frog FG Nup62•58•54 complex. It comprises a ≈13 nanometer-long trimerization interface with an unusual 2W3F coil, a canonical heterotrimeric coiled coil, and a kink that enforces a compact six-helix bundle. Nup54 also contains a ferredoxin-like domain. Chug et al. 2015 further identified a heterotrimeric Nup93-binding module for NPC anchorage. The quaternary structure alternations in the Nup62 complex, which were previously proposed to trigger a general gating of the NPC, are incompatible with the trimer structure. Chug et al. 2015 suggested that the highly elongated Nup62 complex projects barrier-forming FG repeats far into the central NPC channel, supporting a barrier that guards the entire cross section. The Sun1/UNC84A protein and Sun2/UNC84B may function redundantly in early HIV-1 infection steps and therefore influence HIV-1 replication and pathogenesis (Schaller et al. 2017).

NPC of Homo sapiens

Nuclear pore complex protein Nup98-Nup96 [Cleaved into: Nuclear pore complex protein Nup98 (98 kDa nucleoporin) (Nucleoporin Nup98) (Nup98); Nuclear pore complex protein Nup96 (96 kDa nucleoporin) (Nucleoporin Nup96) (Nup96)]; 1817aa; P52948
Nuclear pore membrane glycoprotein 210 (Nuclear pore protein gp210) (Nuclear envelope pore membrane protein POM 210) (POM210) (Nucleoporin Nup210) (Pore membrane protein of 210 kDa); 1887aa; Q8TEM1
Nuclear pore complex protein Nup50 (50 kDa nucleoporin) (Nuclear pore-associated protein 60 kDa-like) (Nucleoporin Nup50); 468aa; Q9UKX7
Nuclear envelope pore membrane protein POM 121 (Nuclear envelope pore membrane protein POM 121A) (Nucleoporin Nup121) (Pore membrane protein of 121 kDa); 1249aa; Q96HA1
Nuclear envelope pore membrane protein POM 121C (Nuclear pore membrane protein 121-2) (POM121-2) (Pore membrane protein of 121 kDa C); 1229aa; A8CG34
Nuclear pore complex-interacting protein family member A1 (Nuclear pore complex-interacting protein) (NPIP); 350aa; Q9UND3
Nuclear pore complex protein Nup107 (107 kDa nucleoporin) (Nucleoporin Nup107); 925aa; P57740
Nuclear pore complex protein Nup153 (153 kDa nucleoporin) (Nucleoporin Nup153); 1475aa; P49790
Nuclear pore complex protein Nup93 (93 kDa nucleoporin) (Nucleoporin Nup93); 819aa; Q8N1F7
Nuclear pore complex protein Nup205 (205 kDa nucleoporin) (Nucleoporin Nup205); 2012aa; Q92621
Nuclear pore complex protein Nup85 (85 kDa nucleoporin) (FROUNT) (Nucleoporin Nup75) (Nucleoporin Nup85) (Pericentrin-1); 656aa; Q9BW27
Nuclear pore complex protein Nup155 (155 kDa nucleoporin) (Nucleoporin Nup155); 1391aa; O75694
Nucleoporin NUP53 (35 kDa nucleoporin) (Mitotic phosphoprotein 44) (MP-44) (Nuclear pore complex protein Nup53) (Nucleoporin Nup35); 326aa; Q8NFH5
Nuclear pore complex protein Nup88 (88 kDa nucleoporin) (Nucleoporin Nup88); 741aa; Q99567
Nuclear pore complex protein Nup133 (133 kDa nucleoporin) (Nucleoporin Nup133); 1156aa; Q8WUM0
Nuclear pore complex protein Nup160 (160 kDa nucleoporin) (Nucleoporin Nup160); 1436aa; Q12769
Importin subunit beta-1 (Importin-90) (Karyopherin subunit beta-1) (Nuclear factor p97) (Pore targeting complex 97 kDa subunit) (PTAC97); 876aa; Q14974
E3 SUMO-protein ligase RanBP2 (EC 6.3.2.-) (358 kDa nucleoporin) (Nuclear pore complex protein Nup358) (Nucleoporin Nup358) (Ran-binding protein 2) (RanBP2) (p270); 3224aa; P49792
Nuclear pore complex protein Nup214 (214 kDa nucleoporin) (Nucleoporin Nup214) (Protein CAN); 2090aa; P35658
Nucleoprotein TPR (Megator) (NPC-associated intranuclear protein) (Translocated promoter region protein); 2363aa; P12270
Nuclear pore glycoprotein p62 (62 kDa nucleoporin) (Nucleoporin Nup62); 522aa; P37198
Nuclear pore-associated protein 1; 1156aa; Q9NZP6
Putative nuclear envelope pore membrane protein POM 121B; 834aa; A6NF01
Germinal-center associated nuclear protein (GANP) (80 kDa MCM3-associated protein) (MCM3 acetylating protein) (MCM3AP) (EC 2.3.1.-) (MCM3 acetyltransferase); 1980aa; O60318
Protein ELYS (Embryonic large molecule derived from yolk sac) (Protein MEL-28) (Putative AT-hook-containing transcription factor 1); 2266aa; Q8WYP5
Nucleoporin NDC1 (hNDC1; TMEM48;Transmembrane protein 48); 674aa and 5 TMSs; Q9BTX1
Nucleoporin Nup43 (Nup107-160 subcomplex subunit Nup43) (p42); 380aa; Q8NFH3
Nucleoporin-like protein 2 (NLP-1) (NUP42 homologue) (Nucleoporin hCG1); 423aa; O15504
Protein SEC13 homologue (SEC13-like protein 1) (SEC13-related protein); 322aa; P55735
Nucleoporin GLE1 (hGLE1) (GLE1-like protein); 698aa; Q53GS7
Importin subunit alpha-5 (Karyopherin subunit alpha-1) (Nucleoprotein interactor 1) (NPI-1) (RAG cohort protein 2) (SRP1-beta) [Cleaved into: Importin subunit alpha-5, N-terminally processed]; 538aa; P52294
Nucleoporin NUP188 homologue (hNup188); 1749aa; Q5SRE5
Transportin-1 (Importin beta-2) (Karyopherin beta-2) (M9 region interaction protein) (MIP); 898aa; Q92973
Importin-7 (Imp7) (Ran-binding protein 7) (RanBP7); 1038aa; O95373
Importin-5 (Imp5) (Importin subunit beta-3) (Karyopherin beta-3) (Ran-binding protein 5) (RanBP5); 1097aa; O00410
Importin subunit alpha-4 (Importin alpha Q2) (Qip2) (Karyopherin subunit alpha-3) (SRP1-gamma); 521aa; O00505
Ran GTPase-activating protein 1 (RanGAP1); 587aa; P46060
SUN domain-containing protein 1 (Protein unc-84 homologue A) (Sad1/unc-84 protein-like 1); 812aa; O94901
Major vault protein (MVP) (Lung resistance-related protein); 893aa; Q14764
Importin-4 (Imp4) (Importin-4b) (Imp4b) (Ran-binding protein 4) (RanBP4); 1081aa; Q8TEX9
Importin subunit alpha-3 (Importin alpha Q1) (Qip1) (Karyopherin subunit alpha-4); 521aa; O00629
Importin-13 (Imp13) (Karyopherin-13) (Kap13) (Ran-binding protein 13) (RanBP13); 963aa; O94829
Sentrin-specific protease 2 (EC 3.4.22.68) (Axam2) (SMT3-specific isopeptidase 2) (Smt3ip2) (Sentrin/SUMO-specific protease SENP2); 589aa; Q9HC62
Exportin-T (Exportin(tRNA)) (tRNA exportin); 962aa; O43592
ATP-dependent RNA helicase DDX19B (EC 3.6.4.13) (DEAD box RNA helicase DEAD5) (DEAD box protein 19B); 479aa; Q9UMR2
Importin-9 (Imp9) (Ran-binding protein 9) (RanBP9); 1041aa; Q96P70
Tankyrase-1 (TANK1) (EC 2.4.2.30) (ADP-ribosyltransferase diphtheria toxin-like 5) (ARTD5) (Poly [ADP-ribose] polymerase 5A) (TNKS-1) (TRF1-interacting ankyrin-related ADP-ribose polymerase) (Tankyrase I); 1327aa; O95271
Importin subunit alpha-7 (Karyopherin subunit alpha-6); 536aa; O60684
Exportin-1 (Exp1) (Chromosome region maintenance 1 protein homologue); 1071aa; O14980
Nucleoporin Nup37 (p37) (Nup107-160 subcomplex subunit Nup37); 326aa; Q8NFH4
Interferon-induced GTP-binding protein Mx2 (Interferon-regulated resistance GTP-binding protein MxB) (Myxovirus resistance protein 2) (p78-related protein); 715aa; P20592
Exportin-5 (Exp5) (Ran-binding protein 21); 1204aa; Q9HAV4
Aladin (Adracalin); 546aa; Q9NRG9
Importin subunit alpha-1 (Karyopherin subunit alpha-2) (RAG cohort protein 1) (SRP1-alpha); 529aa; P52292
Exportin-4 (Exp4); 1151aa; Q9C0E2
mRNA export factor (Rae1 protein homologue) (mRNA-associated protein mrnp 41); 368aa; P78406
G2/mitotic-specific cyclin-B1; 433aa; P14635
Exportin-2 (Exp2) (Cellular apoptosis susceptibility protein) (Chromosome segregation 1-like protein) (Importin-alpha re-exporter); 971aa; P55060
Potassium voltage-gated channel subfamily H member 1 (Ether-a-go-go potassium channel 1) (EAG channel 1) (h-eag) (hEAG1) (Voltage-gated potassium channel subunit Kv10.1); 989aa; O95259
Unconventional myosin-Ic (Myosin I beta) (MMI-beta) (MMIb); 1063aa; O00159
CBP80/20-dependent translation initiation factor; 598aa; O43310
Serine/threonine-protein kinase Nek9 (EC 2.7.11.1) (Nercc1 kinase) (Never in mitosis A-related kinase 9) (NimA-related protein kinase 9) (NimA-related kinase 8) (Nek8); 979aa; Q8TD19
Eukaryotic translation initiation factor 5A-1 (eIF-5A-1) (eIF-5A1) (Eukaryotic initiation factor 5A isoform 1) (eIF-5A) (Rev-binding factor) (eIF-4D); 154aa; P63241
Nucleoporin SEH1 (Nup107-160 subcomplex subunit SEH1) (SEC13-like protein); 360aa; Q96EE3
Serine/threonine-protein kinase Nek7 (EC 2.7.11.1) (Never in mitosis A-related kinase 7) (NimA-related protein kinase 7); 302aa; Q8TDX7
Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homologue) (Cell division protein kinase 1) (p34 protein kinase); 297aa; P06493
Serine/threonine-protein kinase Nek6 (EC 2.7.11.1) (Never in mitosis A-related kinase 6) (NimA-related protein kinase 6) (Protein kinase SID6-1512); 313aa; Q9HC98
Exportin-7 (Exp7) (Ran-binding protein 16); 1087aa; Q9UIA9
ATP-dependent RNA helicase DDX3X (EC 3.6.4.13) (DEAD box protein 3, X-chromosomal) (DEAD box, X isoform) (Helicase-like protein 2) (HLP2); 662aa; O00571
Transportin-2 (Karyopherin beta-2b); 897aa; O14787
Transcription and mRNA export factor ENY2 (Enhancer of yellow 2 transcription factor homologue); 101aa; Q9NPA8
Nucleoporin p58/p45 (Nucleoporin-like protein 1); 599aa; Q9BVL2
Nucleoporin p54 (54 kDa nucleoporin); 507aa; Q7Z3B4
Importin subunit alpha-6 (Karyopherin subunit alpha-5); 536aa; O15131
Importin-11 (Imp11) (Ran-binding protein 11) (RanBP11); 975aa; Q9UI26
Importin-8 (Imp8) (Ran-binding protein 8) (RanBP8); 1037aa; O15397
ATP-dependent RNA helicase DDX19A (EC 3.6.4.13) (DDX19-like protein) (DEAD box protein 19A); 478aa; Q9NUU7
Double homeobox protein 4 (Double homeobox protein 10); 424aa; Q9UBX2
Eukaryotic translation initiation factor 5A-2 (eIF-5A-2) (eIF-5A2) (Eukaryotic initiation factor 5A isoform 2); 153aa; Q9GZV4
G2/mitotic-specific cyclin-B2; 398aa; O95067
Double homeobox protein 1; 170aa; O43812
Ran-binding protein 17; 1088aa; Q9H2T7
Eukaryotic translation initiation factor 5A-1-like (eIF-5A-1-like) (eIF-5A1-like) (Eukaryotic initiation factor 5A isoform 1-like); 154aa; Q6IS14
Transcription and mRNA export factor ENY2 (Enhancer of yellow 2 transcription factor homologue); 100aa; E5RHX8
Transcription and mRNA export factor ENY2 (Enhancer of yellow 2 transcription factor homologue); 101aa; A0A024R9D9
Nucleoporin NUP53; 326aa; A8K3Z5

 
1.I.1.1.4

Ciliate nucleopore complex, NPC.  Regulates protein import and nuclear division (Malone et al. 2008). The NPC contributes to nucleus-selective transport in ciliates (Iwamoto et al. 2009).  The transmembrane components, Pom121 and Pom82, localize exclusively to the macro (MAC)- and micro (MIC)-nuclear NPCs, respectively. Functional nuclear dimorphism in ciliates is likely to depend on compositional and structural specificity of the NPCs (Iwamoto et al. 2017).

NPC of Tetrahymena thermophila

Nucleoporins gp210 of 1927 aas,
Nup155 of 2039 aas,
MicNup98A (Nup4) of 942 aas,
Nup50 (Nup1) of 414 aas,
MacNup98A (Nup2) of 1105 aas,
MacNup98B (Nup3) of 815 aas,
MacNup98B-Nup96 (Nup5) of 2003 aas,
Seh (Seh1) of 365 aas,
Nup93 of 962 aas,
Nup308 of 2,675 aas,
Nup54 of 322 aas.