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Cysteine-String Protein’s Role at Synapses

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Folding for the Synapse
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Abstract

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).

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Acknowledgements

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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Zinsmaier, K.E., Imad, M. (2011). Cysteine-String Protein’s Role at Synapses. In: Wyttenbach, A., O'Connor, V. (eds) Folding for the Synapse. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-7061-9_8

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