Clathrin

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Clathrin (Bos taurus) bound to NAD
clathrin, light polypeptide (Lca)
Identifiers
Symbol CLTA
HUGO 2090
Entrez 1211
OMIM 118960
RefSeq NM_007096
UniProt P09496
Other data
Locus Chr. 12 q23-q24
clathrin, light polypeptide (Lcb)
Identifiers
Symbol CLTB
HUGO 2091
Entrez 1212
OMIM 118970
RefSeq NM_001834
UniProt P09497
Other data
Locus Chr. 4 q
clathrin, heavy polypeptide (Hc)
Identifiers
Symbol CLTC CLTCL2
HUGO 2092
Entrez 1213
OMIM 118955
RefSeq NM_004859
UniProt Q00610
Other data
Locus Chr. 17 q11-qter
clathrin, heavy polypeptide-like 1
Identifiers
Symbol CLTCL1 CLTCL
HUGO 2093
Entrez 8218
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.

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