Two distinct domains in hsc70 are essential for the interaction with the synaptic vesicle cysteine string protein
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Cited by (33)
Comprehensive review on the HSC70 functions, interactions with related molecules and involvement in clinical diseases and therapeutic potential
2012, Pharmacology and TherapeuticsCitation Excerpt :The interaction of Csp with HSC70 can stimulate the ATPase activity of HSC70 and cause a conformational change in HSC70. Interestingly, Csp can only interact with HSC70 and HSP70, but not with other heat shock proteins, such as HSP60 and HSP90 (Chamberlain & Burgoyne, 1997; Stahl et al., 1999). Small glutamine-rich TPR-containing protein (SGT) is a Csp partner which was originally identified because its interaction with envelope proteins of viruses.
The CSPα/G protein complex in PC12 cells
2007, Biochemical and Biophysical Research CommunicationsInteraction between constitutively expressed heat shock protein, Hsc 70, and cysteine string protein is important for cortical granule exocytosis in Xenopus oocytes
2005, Journal of Biological ChemistryCitation Excerpt :First, by itself, overexpression of the J-domain of csp significantly blunts cortical granule exocytosis. Because the J-domain underlies the interaction of csp with members of the Hsp/Hsc 70 family of proteins (34–38), this result supports a role for csp-Hsp/Hsc 70 interaction in cortical granule exocytosis. Second, mutation of the J-domain of csp (to produce constructs that have been shown not to associate with Hsp/Hsc 70; see Refs. 35, 40, and 41) significantly reduces the inhibitory effect of these constructs on cortical granule exocytosis.
Characterization of the Gα<inf>s</inf> regulator cysteine string protein
2005, Journal of Biological ChemistryCysteine String Protein (CSP) Inhibition of N-type Calcium Channels Is Blocked by Mutant Huntingtin
2003, Journal of Biological ChemistryA brain-specific isoform of small glutamine-rich tetratricopeptide repeat-containing protein binds to Hsc70 and the cysteine string protein
2003, Journal of Biological Chemistry
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Dr. Bernd Stahl, Max-Planck-Institute for Experimental Medicine, Hermann-Rein-Str. 3, D-37075 Göttingen/Germany, Fax: ++5513899753.