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1 December 2000 A Novel N-Terminal Domain Directs Membrane Localization of Mouse Testis-Specific Calpastatin
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Abstract

Multiple isoforms of calpastatin have been identified with unique N-terminal regions followed by identical calpain inhibitory domains (II–IV). In many instances the isoforms are cell-type specific, although the precise functional differences among these N-terminal regions are largely unknown. Here we report a germ cell-specific isoform of calpastatin (tCAST) that consists of a novel N-terminal peptide of 40 amino acids (domain T) followed by domains II to IV of somatic calpastatin (sCAST). Domain T is responsible for membrane association of tCAST through a protein modification by myristylation. Mutation of the myristylation site eliminates membrane targeting. Unlike most of the isoforms of calpastatin that are generated through alternative RNA splicing or post-translational proteolysis, the testis-specific isoform is transcribed from an intronic promoter in haploid germ cells of the testis. The intronic promoter directs specific expression of a reporter transgene in developing germ cells of the mouse testis.

Siming Li and Erwin Goldberg "A Novel N-Terminal Domain Directs Membrane Localization of Mouse Testis-Specific Calpastatin," Biology of Reproduction 63(6), 1594-1600, (1 December 2000). https://doi.org/10.1095/biolreprod63.6.1594
Received: 5 May 2000; Accepted: 1 July 2000; Published: 1 December 2000
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