8.A.137.  The Clathrin (Clathrin) Family 

Clathrin impacts Wnt/beta-catenin signaling by controlling exocytosis of transmembrane proteins including cadherins and Wnt co-receptors that together control the membrane-bound and soluble pools of beta-catenin. Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network. It acts as a component of the TACC3/ch-TOG/clathrin complex, proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as an inter-microtubule bridge (Royle et al. 2005, Royle and Lagnado 2006, Booth et al. 2011). The TACC3/ch-TOG/clathrin complex is required for the maintenance of kinetochore fiber tension (Cheeseman et al. 2013). It also plays a role in early autophagosome formation (Ravikumar et al. 2010).


 

References:

Booth, D.G., F.E. Hood, I.A. Prior, and S.J. Royle. (2011). A TACC3/ch-TOG/clathrin complex stabilises kinetochore fibres by inter-microtubule bridging. EMBO. J. 30: 906-919.
Cheeseman, L.P., E.F. Harry, A.D. McAinsh, I.A. Prior, and S.J. Royle. (2013). Specific removal of TACC3-ch-TOG-clathrin at metaphase deregulates kinetochore fiber tension. J Cell Sci 126: 2102-2113.
Kalthoff, C., S. Groos, R. Kohl, S. Mahrhold, and E.J. Ungewickell. (2002). Clint: a novel clathrin-binding ENTH-domain protein at the Golgi. Mol. Biol. Cell 13: 4060-4073.
Mills, I.G., G.J. Praefcke, Y. Vallis, B.J. Peter, L.E. Olesen, J.L. Gallop, P.J. Butler, P.R. Evans, and H.T. McMahon. (2003). EpsinR: an AP1/clathrin interacting protein involved in vesicle trafficking. J. Cell Biol. 160: 213-222.
Munthe, E., C. Raiborg, H. Stenmark, and E.M. Wenzel. (2020). Clathrin regulates Wnt/β-catenin signaling by affecting Golgi to plasma membrane transport of transmembrane proteins. J Cell Sci. [Epub: Ahead of Print]
Ravikumar, B., K. Moreau, L. Jahreiss, C. Puri, and D.C. Rubinsztein. (2010). Plasma membrane contributes to the formation of pre-autophagosomal structures. Nat. Cell Biol. 12: 747-757.
Royle, S.J. and L. Lagnado. (2006). Trimerisation is important for the function of clathrin at the mitotic spindle. J Cell Sci 119: 4071-4078.
Royle, S.J., N.A. Bright, and L. Lagnado. (2005). Clathrin is required for the function of the mitotic spindle. Nature 434: 1152-1157.
Examples:

TC#NameOrganismal TypeExample
8.A.137.1.1

Clathrin heavy chain 1 of 1675 aas, CLTC CLH17, CLTCL2 + clathrin light chain A of 248 aas, CCLTA. Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. It acts as a component of the TACC3/ch-TOG/clathrin complex, proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as an inter-microtubule bridge (Royle et al. 2005, Booth et al. 2011). The clathrin interactor 1 protein, CLTCL1, binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and may have a role in transport via clathrin-coated vesicles from the trans-Golgi network to endosomes It also stimulates clathrin assembly (Kalthoff et al. 2002; Mills et al. 2003).

Clathrin HC1/LCA with CLTCL1 of Homo sapiens

 
8.A.137.1.2

Clathrin heavy chain 2 of 1625 aas, CLTCL1 CLH22, CLTCL, CLTD plus the sclathrin light chain B, CLCB. It impacts on Wnt/beta-catenin signaling by controlling exocytosis of transmembrane proteins including cadherins and Wnt co-receptors that together control the membrane-bound and soluble pools of beta-catenin (Munthe et al. 2020).

Clathrin HC2 of Homo sapiens

 
8.A.137.1.3

Uncharacterized protein of 630 aas.

UP of Capitella teleta

 
8.A.137.1.4

Clathrin heavy chain linker domain-containing protein 1 of 585 aa

Clathrin HC1 of Sphaeramia orbicularis

 
8.A.137.1.5

Clathrin heavy chain of 2180 aa

Clathrin HC of Nannochloropsis gaditana

 
8.A.137.1.6

Uncharacterized protein of 995 aas

UP of Candida auris

 
Examples:

TC#NameOrganismal TypeExample