Cysteine-String Protein’s Role at Synapses
Accumulating evidence illustrates the significance of chaperone systems for the regulation and maintenance of neuronal and synaptic function. The significance of synaptic chaperones is best illustrated by cysteine-string protein (CSP), a member of the DnaJ/Hsp40 family of Hsp70/Hsc70 co-chaperones. CSP recruits the ubiquitous chaperone Hsc70 to synaptic vesicles forming a chaperone complex that maintains synaptic function and prevents neurodegeneration. Here, we summarize studies that demonstrate CSP’s neuroprotective role for synaptic function and discuss insights into its possible clientele (the proteins whose function it facilitates).
KeywordsSynaptic Vesicle Synaptic Function Chaperone Activity Client Protein Snare Protein
This work has been supported by grants to K.E.Z. from NINDS (R03 NS057215–01, R21 NS055202–02) and a PERT fellowship to M.I. (K12 GM000708).
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