Clathrin

Clathrin (Bos taurus) bound to NAD
clathrin, light polypeptide (Lca)
Identifiers
Symbol	CLTA
Entrez	1211
HUGO	2090
OMIM	118960
RefSeq	NM_007096
UniProt	P09496
Other data
Locus	Chr. 12 q23-q24

clathrin, light polypeptide (Lcb)
Identifiers
Symbol	CLTB
Entrez	1212
HUGO	2091
OMIM	118970
RefSeq	NM_001834
UniProt	P09497
Other data
Locus	Chr. 4 q

clathrin, heavy polypeptide (Hc)
Identifiers
Symbol	CLTC
Alt. Symbols	CLTCL2
Entrez	1213
HUGO	2092
OMIM	118955
RefSeq	NM_004859
UniProt	Q00610
Other data
Locus	Chr. 17 q11-qter

clathrin, heavy polypeptide-like 1
Identifiers
Symbol	CLTCL1
Alt. Symbols	CLTCL
Entrez	8218
HUGO	2093
OMIM	601273
RefSeq	NM_001835
UniProt	P53675
Other data
Locus	Chr. 22 q11.2

Clathrin is a protein that is the major constituent of the 'coat' of the clathrin-coated pits and coated vesicles formed during endocytosis of materials at the surface of cells.

Clathrin molecules are recruited with the aid of adaptor proteins to a membrane segment that is destined to be incorporated into a vesicle. In synaptic vesicle formation, one such adaptor protein is AP180 (see here for micrographs of clathrin assembly). This protein both recruits clathrin to membranes and also promotes its polymerisation in a localized polyhedral lattice on the plasma membrane. Epsin can also recruit clathrin to membranes and promote its polymerisation, and, in this case, the epsin helps deform the membrane and thus clathrin coated vesicles can bud (see here for micrographs of vesicle budding). After vesicle scission, the coat quickly falls off and may then be reused to form fresh-coated pits and vesicles. The un-coated vesicle then fuses with endosomes, delivering its contents to them; this membrane is ultimately returned to the cell surface.

A similar process also buds membrane segments from intracellular organelles, such as in the formation of vesicles from the trans-Golgi network.

Clathrin was first isolated and named by Barbara Pearse in 1975.^[1]

See also

• AP180
• Cap formation
• Cell migration
• Endocytic cycle
• Epsin
• Synaptic vesicle
• Adaptin

External links

• Clathrin structure
• Membrane Dynamics

References

1. ^ Pearse, B.M.F. (Apr 1976). "Clathrin: a unique protein associated with intracellular transfer of membrane by coated vesicles". Proc. Natl. Acad. Sci. USA 73 (4): 1255-9. PMID 1063406. 

• Ford MG; Pearse BM, Higgins MK, Vallis Y, Owen DJ, Gibson A, Hopkins CR, Evans PR, McMahon HT. (Feb 2001). "Simultaneous binding of PtdIns(4,5)P2 and clathrin by AP180 in the nucleation of clathrin lattices on membranes". Science 291 (5506): 1051-5. doi:10.1126/science.291.5506.1051. PMID 11161218. 
• Wakeham DE; Chen CY, Greene B, Hwang PK, Brodsky FM (Oct 2003). "Clathrin self-assembly involves coordinated weak interactions favorable for cellular regulation". EMBO J. 22 (19): 4980-90.. doi:10.1093/emboj/cdg511. PMID 14517237. 
• Ford MG; Mills IG, Peter BJ, Vallis Y, Praefcke GJ, Evans PR, McMahon HT. (Sep 2002). "Curvature of clathrin-coated pits driven by epsin.". Nature 419 (6905): 361-6. doi:10.1038/nature01020. PMID 12353027. 

• Fotin A; Cheng Y, Sliz P, Grigorieff N, Harrison S, Kirchhausten T, Walz T (Dec 2004). "Molecular model for a complete clathrin lattice from electron cryomicroscopy". Nature 432: 573-9.. 

• Berg T; S Mousavi, Malerod L, Kjeken R (2004). "Clathrin-dependent endocytosis". Biochem J 377: 1-16.. 
• Smith CJ; Grigorieff N, Pearse BMF. (Sep 1998). "Clathrin coats at 21 Å resolution: a cellular assembly designed to recycle multiple membrane receptors". The EMBO Journal 17 (17): 4943-53. doi:10.1093/emboj/17.17.4943. PMID 9724631.  (Model of Clathrin assembly)
• Pérez-Gómez J; Moore I. (Mar 2007). "Plant Endocytosis: It Is Clathrin after All". Curr Biol. 17 (6): 217-9. doi:10.1016/j.cub.2007.01.045. PMID 17371763.  (Review on involvement of clathrin in plant endocytosis - prooven recently)

Membrane protein: vesicular transport proteins
Archain - Clathrin - Caveolin - Dynamin - Lysosomal trafficking regulator - SNARE (SNAP-25, Syntaxin, Synaptobrevin) - Synaptotagmin