Specific binding of CAP-50 to calcyclin

Hiroyuki Minami, Hiroshi Tokumitsu, Akihiro Mizutani, Yasuo Watanabe, Masato Watanabe, Hiroyoshi Hidaka

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Abstract

CAP-50, a calcyclin-associated protein with an apparent molecular mass or 50 kDa, was purified and proved to be a novel annexin [Tokumitsu, H. et al. (1992) J. Biol. Chem. 267, 8919-8924]. We examined the binding of CAP-50 to other Ca2+-binding proteins which have two or four EF-hand structures, by a co-precipitation assay with phospholipid (phosphatidylserine). Among nine Ca2+-binding proteins (calcyclin, S-100 proteins, p11, calgizzarin, calvasculin, calmodulin and troponin C) examined, only calcyclin interacted with CAP-50. These results clearly show that the interaction of CAP-50 to calcyclin is specific, i.e. other Ca2+-binding proteins with the EF-hand structure could not substitute for calcyclin, thereby suggesting the possible role in specific regulation of the function of CAP-50 by Ca2+/calcyclin.

Original languageEnglish
Pages (from-to)217-219
Number of pages3
JournalFEBS Letters
Volume305
Issue number3
DOIs
Publication statusPublished - Jul 6 1992
Externally publishedYes

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Keywords

  • Annexin
  • CAP-50
  • EF-hand protein, Calcyclin

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Minami, H., Tokumitsu, H., Mizutani, A., Watanabe, Y., Watanabe, M., & Hidaka, H. (1992). Specific binding of CAP-50 to calcyclin. FEBS Letters, 305(3), 217-219. https://doi.org/10.1016/0014-5793(92)80671-3