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The role of Sec1p-related proteins in vesicle trafficking in the nerve terminal

✍ Scribed by J. Pevsner

Publisher
John Wiley and Sons
Year
1996
Tongue
English
Weight
675 KB
Volume
45
Category
Article
ISSN
0360-4012

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✦ Synopsis

Vesicle trafficking at multiple stages of the secretory pathway depends on a family of soluble proteins related to yeast Seclp. In yeast, this family consists of four members: the late-acting Seclp that is required for vesicular transport between the Golgi apparatus and the cell surface; Vps33p and Vps45p which are required for trafficking between the Golgi complex and the lysosome-like vacuole; and Slylp that is essential for trafficking between the endoplasmic reticulum and the Golgi apparatus. In mammalian systems, homologues of these proteins have been identified. In particular, a neural-specific Seclp homologue (n-secl/Munc-lS) binds the plasma membrane protein syntaxin and may regulate synaptic vesicle docking. The Seclp family of proteins is essential for vesicle trafficking in both regulated and constitutive trafficking pathways, and n-secl is critical in the regulated release of neurotransmitter from the nerve terminal.

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