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Int J Biochem Cell Biol. 2002 Oct;34(10):1173-7.

Endophilin-1: a multifunctional protein.

Author information

1
Centre for Child Health Research and the Western Australian Institute for Medical Research, The University of WA, Telethon Institute for Child Health Research, 100 Roberts Road, WA 6008, Subiaco, Australia. areutens@ichr.uwa.edu.au

Abstract

Endophilin-1, a cytoplasmic Src homology 3 (SH3) domain-containing protein, localises in brain presynaptic nerve termini. Endophilin dimerises through its N-terminus, and participates at multiple stages in clathrin-coated endocytosis, from early membrane invagination to synaptic vesicle uncoating. Both its C-terminal SH3 domain and N-terminus are required for endocytosis. Through its SH3 domain, endophilin bound to proline-rich domains (PRDs) in other endocytic proteins, including synaptojanin and dynamin. The N-terminal region possesses unique functions affecting lipid membrane curvature, through lysophosphatidic acid acyl transferase (LPAAT) activity and direct binding and tubulating activity. In addition to synaptic vesicle formation, endophilin-1 complexes with signalling molecules, including cell surface receptors, metalloprotease disintegrins and germinal centre kinase-like kinase (GLK). Therefore, endophilin-1 may serve to couple vesicle biogenesis with intracellular signalling cascades.

PMID:
12127567
[Indexed for MEDLINE]

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