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A Novel N-Terminal Domain Directs Membrane Localization of Mouse Testis-Specific Calpastatin¹

^a Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208

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.

FOOTNOTES

First decision: 15 June 2000.

¹ This work was supported by NIH Sub-5-U54-HD29099, by P30HD28048, and by NIH HD05863.

² Correspondence: Erwin Goldberg, Department of Biochemistry, Molecular Biology and Cell Biology, 2153 N. Campus Dr., Northwestern University, Evanston, IL 60208. FAX: 847 467 1380; erv{at}nwu.edu

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