Abstract
Vesicle trafficking at multiple stages of the secretory pathway depends on a family of soluble proteins related to yeast Sec1p. In yeast, this family consists of four members: the late-acting Sec1p 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 Sly1p 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 Sec1p homologue (n-sec1/Munc-18) binds the plasma membrane protein syntaxin and may regulate synaptic vesicle docking. The Sec1p family of proteins is essential for vesicle trafficking in both regulated and constitutive trafficking pathways, and n-sec1 is critical in the regulated release of neurotransmitter from the nerve terminal.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 89-95 |
| Number of pages | 7 |
| Journal | Journal of neuroscience research |
| Volume | 45 |
| Issue number | 2 |
| DOIs | |
| State | Published - 1996 |
Keywords
- neurotransmission
- secretion
- synaptic vesicles
ASJC Scopus subject areas
- Cellular and Molecular Neuroscience