Journal
BIOCHEMISTRY AND CELL BIOLOGY
Volume 88, Issue 2, Pages 157-165Publisher
CANADIAN SCIENCE PUBLISHING, NRC RESEARCH PRESS
DOI: 10.1139/O09-124
Keywords
CSP alpha; J protein; DnaJ protein; J domain; Hsp40; chaperone
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Cysteine string protein (CSP alpha, also called DnaJC5) is unique among J proteins. Similar to other J proteins, CSP alpha interacts with and activates the ATPase of Hsc70s (heat shock proteins of 70 kDa), thereby harnessing the ATPase activity for conformational work on client proteins. In contrast to other J proteins, CSP alpha is anchored to synaptic vesicles, as well as to exocrine, endocrine and neuroendocrine secretory granules, and has been shown to have an essential anti-neurodegenerative role. CSP alpha-null organisms exhibit progressive neurodegeneration, behavioural deficits, and premature death, most likely due to the progressive misfolding of one or more client proteins. Here we highlight recent advances in our understanding of the critical role that CSP alpha plays in governing exocytotic secretory functions.
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