Cysteine-string protein alpha (CSP alpha) is a DnaJ chaperone that is associated with secretory vesicles in diverse cell types. The cysteine-string region is the signature domain of CSP alpha and contains 14 closely spaced cysteines, the majority of which are palmitoylated; this post-translational modification mediates stable membrane attachment. CSP alpha has been proposed to function in regulated exocytosis pathways throughout the body and has an additional neuroprotective function. Two novel CSP isoforms, beta and gamma, were identified recently, although the expression profile, properties, and functions of these proteins are not clear and in some cases are subject to debate. Here, we report that CSP beta is enriched in rat testis and was not detected in any other tissue that was examined. including brain. Although the cysteine-string domain of CSP beta is distinct from that found in CSP alpha, the endogenous beta isoform expressed in testis is membrane-associated and palmitoylated. However, in agreement with earlier work, we find that the palmitoylation efficiency or CSP beta is reduced compared with that of CSP alpha. Subsequent analysis of chimeric proteins reveals that regions upstream of the cysteine-string domains of CSP alpha and CSP beta underlie this difference in palmitoylation efficiency between the two isoforms.
|Number of pages||6|
|Publication status||Published - Jun 2010|