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A trimeric protein complex functions as a synaptic chaperone machine

By:Tobaben, S (Tobaben, S); Thakur, P (Thakur, P); Fernandez-Chacon, R (Fernandez-Chacon, R); Sudhof, TC (Sudhof, TC); Rettig, J (Rettig, J); Stahl, B (Stahl, B)

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Volume: 31

Issue: 6

Pages: 987-999

DOI: 10.1016/S0896-6273(01)00427-5

Published: SEP 27 2001


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.

Author Information

Reprint Address: Stahl, B (reprint author)

Max Planck Inst Expt Med, Hermann Rein Str 3, D-37075 Gottingen, Germany.


[ 1 ] Max Planck Inst Expt Med, D-37075 Gottingen, Germany
[ 2 ] Max Planck Inst Biophys Chem, D-37077 Gottingen, Germany
[ 3 ] Univ Saarland, Inst Physiol, D-66421 Homburg, Germany
[ 4 ] Univ Texas, SW Med Ctr, Dept Mol Genet, Dallas, TX 75235 USA
[ 5 ] Univ Texas, SW Med Ctr, Ctr Bas Neurosci, Howard Hughes Med Inst, Dallas, TX 75235 USA



Categories / Classification

Research Areas:Neurosciences & Neurology

Web of Science Categories:Neurosciences

Document Information

Document Type:Article


Accession Number: WOS:000171281300013

PubMed ID: 11580898

ISSN: 0896-6273

Other Information

IDS Number: 477JW

Cited References in Web of Science Core Collection: 50

Times Cited in Web of Science Core Collection: 144

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