Specific binding of CAP-50 to calcyclin

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

Research output: Contribution to journalArticlepeer-review


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
Issue number3
Publication statusPublished - Jul 6 1992
Externally publishedYes


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

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


Dive into the research topics of 'Specific binding of CAP-50 to calcyclin'. Together they form a unique fingerprint.

Cite this