University at Buffalo - The State University of New York
Skip to Content
A trimeric protein complex functions as a synaptic chaperone machine. - PubMed - NCBI

Send to

Choose Destination
See comment in PubMed Commons below
Neuron. 2001 Sep 27;31(6):987-99.

A trimeric protein complex functions as a synaptic chaperone machine.

Author information

Max-Planck-Institute for Experimental Medicine, 37075 Göttingen, Germany.


We identify a chaperone complex composed of (1) the synaptic vesicle cysteine string protein (CSP), thought to function in neurotransmitter release, (2) the ubiquitous heat-shock protein cognate Hsc70, and (3) the SGT protein containing three tandem tetratricopeptide repeats. These three proteins interact with each other to form a stable trimeric complex that is located on the synaptic vesicle surface, and is disrupted in CSP knockout mice. The CSP/SGT/Hsc70 complex functions as an ATP-dependent chaperone that reactivates a denatured substrate. SGT overexpression in cultured neurons inhibits neurotransmitter release, suggesting that the CSP/SGT/Hsc70 complex is important for maintenance of a normal synapse. Taken together, our results identify a novel trimeric complex that functions as a synapse-specific chaperone machine.

[Indexed for MEDLINE]
Free full text
PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Support Center