Cysteine-string protein's neuroprotective role.
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.
Zinsmaier
Konrad E
KE
Department of Neuroscience and Department of Molecular and Cellular Biology, University of Arizona, Tucson, Arizona 85721-0077, USA. kez4@email.arizona.edu
D000818:Animals; D001921:Brain / Q000166:cytology / Q000473:pathology / Q000502:physiology; D019610:Cytoprotection / Q000502:physiology*; D004331:Drosophila melanogaster; D050956:HSP40 Heat-Shock Proteins / Q000502:physiology*; D020271:Heredodegenerative Disorders, Nervous System / Q000378:metabolism / Q000473:pathology / Q000517:prevention & control*; D006801:Humans; D008565:Membrane Proteins / Q000502:physiology*; D018377:Neurotransmitter Agents / Q000378:metabolism*
D050956:HSP40 Heat-Shock Proteins; D008565:Membrane Proteins; D018377:Neurotransmitter Agents; C088460:cysteine string protein