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.



Gene Ontology Annotations    Click to see Annotation Detail View

Cellular Component

  

Objects Annotated

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


Additional Information