Abstract

Cysteine-string protein (CSP), a member of the DnaJ/Hsp40 family of cochaperones, is critical for maintaining neurotransmitter release and preventing neurodegeneration. CSP likely forms a chaperone complex on synaptic vesicles together with the 70-kDa heat shock cognate (Hsc70) and the small glutamine-rich tetratricopeptide repeat (TPR)-containing protein (SGT) that may control or protect the assembly and activity of SNARE proteins and various other protein substrates. Here, the author summarizes studies that elucidated CSP's neuroprotective role.

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