Interaction of calmodulin and other calcium-modulated proteins with mammalian and arthropod junctional membrane proteins

Linda J. Van Eldik, Elliot L. Hertzberg, Robert C. Berdan, Norton B. Gilula

Research output: Contribution to journalArticlepeer-review

57 Scopus citations

Abstract

Calmodulin and other calcium-modulated proteins bind in vitro to purified junctional polypeptides from rat liver gap junctions, bovine lens fiber junctions, a chymotryptic fragment from bovine lens junctions, and crayfish hepatopancreas gap junctions. The potential biological relevance of the interaction of calmodulin with junctional proteins is suggested by immunocytochemical localization of endogenous calmodulin in cortical regions of the cell where gap junctions exist. These observations provide a molecular basis for understanding the potential regulatory role of calmodulin on cell-cell communication channels in vivo. In addition, the calmodulin binding represents the first molecular homology that has been found for junctional channel proteins from mammalian and arthropod tissues.

Original languageEnglish
Pages (from-to)825-832
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume126
Issue number2
DOIs
StatePublished - Jan 31 1985

Bibliographical note

Funding Information:
Supported in part by American Cancer Society institutional grant IN-25V and National Science Foundation grant PCM-8302912 (to L.V.E.) and National Institutes of Health grants HL28446 (to N.B.G.) and GM30667 (to E.L.H.). thank D.M. Watterson and W.H. Burgess for critical comments and helpful discussions, and K.G. Waymire for her superb technical assistance.

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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