RGD Reference Report - A trimeric protein complex functions as a synaptic chaperone machine. - Rat Genome Database

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A trimeric protein complex functions as a synaptic chaperone machine.

Authors: Tobaben, S  Thakur, P  Fernández-Chacón, R  Südhof, T C  Rettig, J  Stahl, B 
Citation: Tobaben S, etal., Neuron. 2001 Sep 27;31(6):987-99.
RGD ID: 13702369
Pubmed: PMID:11580898   (View Abstract at PubMed)

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.




Cellular Component

  


Genes (Rattus norvegicus)
Dnajc5  (DnaJ heat shock protein family (Hsp40) member C5) Sgta  (small glutamine rich tetratricopeptide repeat co-chaperone alpha)