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

S. Li, E. Goldberg*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)1594-1600
Number of pages7
JournalBiology of reproduction
Issue number6
StatePublished - 2000


  • Gene regulation
  • Spermatid
  • Spermatogenesis
  • Testes

ASJC Scopus subject areas

  • Reproductive Medicine
  • Cell Biology


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