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Publication : A novel N-terminal domain directs membrane localization of mouse testis-specific calpastatin.

First Author  Li S Year  2000
Journal  Biol Reprod Volume  63
Issue  6 Pages  1594-600
PubMed ID  11090425 Mgi Jnum  J:65896
Mgi Id  MGI:1927428 Doi  10.1095/biolreprod63.6.1594
Citation  Li S, et al. (2000) A novel N-terminal domain directs membrane localization of mouse testis-specific calpastatin. Biol Reprod 63(6):1594-600
abstractText  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.
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