University at Buffalo - The State University of New York
Skip to Content
Molecular chaperones and the regulation of neurotransmitter exocytosis. - PubMed - NCBI
Format

Send to

Choose Destination
See comment in PubMed Commons below
Biochem Pharmacol. 2001 Jul 1;62(1):1-11.

Molecular chaperones and the regulation of neurotransmitter exocytosis.

Author information

1
Department of Neuroscience, 234d Stemmler Hall, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6974, USA. zinsmaie@mail.med.upenn.edu

Abstract

Regulated neurotransmitter release depends on a precise sequence of events that lead to repeated cycles of exocytosis and endocytosis. These events are mediated by a series of molecular interactions among vesicular, plasma membrane, and cytosolic proteins. An emerging theme has been that molecular chaperones may guide the sequential restructuring of stable or transient protein complexes to promote a temporal and spatial regulation of the endo- and exocytotic machinery and to ensure a vectorial passage through the vesicle cycle. Chaperones, specialized for a few substrates, are ideally suited to participate in regulatory processes that require some molecular dexterity to rearrange conformational or oligomeric protein structures. This article emphasizes the significance of three molecular chaperone systems in regulated neurotransmitter release: the regulation of soluble NSF attachment protein receptor (SNARE) complexes by N-ethylmaleimide-sensitive factor (NSF) and the soluble NSF attachment protein (SNAP), the uncoating of clathrin-coated vesicles by the 70 kDa heat-shock cognate protein (Hsc70), and the regulation of SNARE complex-associated protein interactions by cysteine-string protein and Hsc70.

PMID:
11377391
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Support Center