9.B.392.  The Golgi Apparatus Golgin (Golgin) Family

These proteins are involved in maintaining the Golgi structure, stimulating the formation of Golgi stacks and ribbons (Diao et al. 2003), and in intra-Golgi retrograde transport. Coiled-coil proteins of the golgin family have been implicated in intra-Golgi transport through tethering coat protein complex I (COPI) vesicles. The p115-golgin tether is the best studied. Malsam et al. 2005 characterized the golgin-84-CASP tether. The vesicles bound by this tether were strikingly different from those bound by the p115-golgin tether in that they lacked members of the p24 family of putative cargo receptors and contained enzymes instead of anterograde cargo. Microinjected golgin-84 or CASP inhibited Golgi-enzyme transport to the endoplasmic reticulum, further implicating this tether in retrograde transport. These and other golgins may modulate the flow patterns within the Golgi stack (Malsam et al. 2005).

The plant Golgi apparatus is responsible for the processing of proteins received from the ER, and their distribution to multiple destinations within the cell. Golgi matrix components, such as golgins, are tethering factors that mediate the physical connections between Golgi bodies and the ER. Golgins are  anchored to the Golgi membrane by the C-terminus either throughTMSs or interaction with small regulatory GTPases. The golgin N-terminus contains long coiled-coil domains which consist of a number of alpha-helices wrapped around each other to form a structure similar to a rope being made from several strands, reaching into the cytoplasm. In animal cells golgins are implicated in specific recognition of cargo. The plant golgin Atgolgin-84A is a tethering factor at the ER-Golgi interface.  Without it, transport between the ER and Golgi bodies is impaired, and cargo proteins are redirected to the vacuole (Vieira et al. 2020). Both O- and N-glycans appear to function as generic Golgi export signals at the trans-Golgi to promote exocytic trafficking (Sun et al. 2020).

 


 

References:

Cao, H., X. Li, Z. Wang, M. Ding, Y. Sun, F. Dong, F. Chen, L. Liu, J. Doughty, Y. Li, and Y.X. Liu. (2015). Histone H2B Monoubiquitination Mediated by HISTONE MONOUBIQUITINATION1 and HISTONE MONOUBIQUITINATION2 Is Involved in Anther Development by Regulating Tapetum Degradation-Related Genes in Rice. Plant Physiol. 168: 1389-1405.
Diao, A., D. Rahman, D.J. Pappin, J. Lucocq, and M. Lowe. (2003). The coiled-coil membrane protein golgin-84 is a novel rab effector required for Golgi ribbon formation. J. Cell Biol. 160: 201-212.
Du, Y., W. He, C. Deng, X. Chen, L. Gou, F. Zhu, W. Guo, J. Zhang, and T. Wang. (2016). Flowering-Related RING Protein 1 (FRRP1) Regulates Flowering Time and Yield Potential by Affecting Histone H2B Monoubiquitination in Rice (Oryza Sativa). PLoS One 11: e0150458.
Kim, J.H., S.D. Lim, K.H. Jung, and C.S. Jang. (2023). Overexpression of a C3HC4-type E3-ubiquitin ligase contributes to salinity tolerance by modulating Na homeostasis in rice. Physiol Plant 175: e14075.
Kovacs, M.T., M. Vallette, P. Wiertsema, F. Dingli, D. Loew, G.P.F. Nader, M. Piel, and R. Ceccaldi. (2023). DNA damage induces nuclear envelope rupture through ATR-mediated phosphorylation of lamin A/C. Mol. Cell 83: 3659-3668.e10.
Malsam, J., A. Satoh, L. Pelletier, and G. Warren. (2005). Golgin tethers define subpopulations of COPI vesicles. Science 307: 1095-1098.
Shi, M., N. Zhou, M. Xiu, X. Li, F. Shan, W. Chen, W. Li, C.M. Chiang, X. Wu, Y. Zhang, A. Li, and J. Cao. (2024). Identification of host proteins that interact with African swine fever virus pE301R. Eng Microbiol 4: 100149.
Sun, X., H.C. Tie, B. Chen, and L. Lu. (2020). Glycans function as a Golgi export signal to promote the constitutive exocytic trafficking. J. Biol. Chem. 295: 14750-14762.
Vieira, V., C. Pain, S. Wojcik, T.S. Rossi, J. Denecke, A. Osterrieder, C. Hawes, and V. Kriechbaumer. (2020). Living on the edge: the role of Atgolgin-84A at the plant ER-Golgi interface. J Microsc. [Epub: Ahead of Print]
Examples:

TC#NameOrganismal TypeExample
9.B.392.1.1

Golgin of 731 aas and 1 C-terminal TMS.

Golgin of Homo sapiens

 
9.B.392.1.2

Golgin-84 of 516 aas and one C-terminal TMS

Golgin-84 of Drosophila melanogaster (fruit fly)

 
9.B.392.1.3

Uncharacterized protein of 554 aas and one C-terminal TMS.

UP of Acanthamoeba castellanii

 
9.B.392.1.4

Uncharacterized protein of 757 aas and one C-terminal TMS.

UP of Thecamonas trahens

 
9.B.392.1.5

Uncharacterized protein of 542 aas and 1 C-terminal TMS

UP of Saprolegnia parasitica

 
Examples:

TC#NameOrganismal TypeExample
9.B.392.2.1

Golgin-84 of 853 aas and one C-terminal TMS.

Golgin-84 of Porphyridium purpureum

 
9.B.392.2.2

Golgin of 707 aas and one C-terminal TMS. It is a golgi matrix protein, playing a role in tethering of vesicles to Golgi membranes and in maintaining the overall structure of the Golgi apparatus.

Golgin of Arabidopsis thaliana (Mouse-ear cress)

 
9.B.392.2.3

Uncharacterized protein of 603 aas

UP of Exophiala dermatitidis

 
Examples:

TC#NameOrganismal TypeExample
9.B.392.3.1

CASP C terminal putative protein of 687 aas and one C-terminal TMS.

Putative protein of Oryza sativa

 
9.B.392.3.2

Coy1p of 679 aas and one C-terminal TMS.

Coy1p of Saccharomyces cerevisiae

 
9.B.392.3.3

Putative golgi membrane protein of 765 aas and 2 C-terminal TMSs.

Membrane protein of Eutypa lata

 
Examples:

TC#NameOrganismal TypeExample
9.B.392.4.1

Uncharacterized protein of 542 aas and one C-terminal TMS.

UP of Ostreococcus tauri

 
9.B.392.4.2

Uncharacterized protein of 878 aas with one C-terminal TMS.

UP of Micromonas pusilla

 
9.B.392.4.3

Uncharacterized protein of 1104 aas and one C-terminal TMS

UP of Trebouxia sp. A1-2

 
9.B.392.4.4

E3 ubiquitin-protein ligase (HUB2 of 844 aas) monoubiquitinates H2B to form H2BK143ub1 which gives a specific tag for epigenetic transcriptional activation and is a prerequisite for H3 Lys-4 methylation (H3K4me). It thereby plays a central role in histone code and gene regulation (Cao et al. 2015, Du et al. 2016).  Overexpression of this C3HC4-type E3-ubiquitin ligase contributes to salinity tolerance by modulating Na+ homeostasis in rice (Kim et al. 2023).

E3 ubiquitinase of Oryza sativa subsp. japonica (Rice)

 

 
9.B.392.4.5

Vimentin (VIM) poptosis-inducing factor of 466 aas and 1 TMS near the N-terminus.  It interacts with African swine fever virus pE301R as does another protein, AIFM1 (UP acc # O95831) of 613 aas with one N-terminal TMS (Shi et al. 2024).

Vimentin of Homo sapiens

 
9.B.392.4.6

Pre-lamin-A/C of 664 aas and 1 TMS.  Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (Kovacs et al. 2023).

Pre-lamin-A/C of Homo sapiens