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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

Additional recommended knowledge

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

  • 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)


 
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Clathrin". A list of authors is available in Wikipedia.
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