A hydrophobie domain of Ca2+-modulating cyclophilin ligand modulates calcium influx signaling in T lymphocytes

Michael P. Holloway, Richard J. Bram

Research output: Contribution to journalArticle

30 Scopus citations

Abstract

Ca2+-modulating cyclophilin ligand (CAML) was originally described as a cyclophilin B-binding protein whose overexpression in T cells causes a rise in intracellular calcium, thus activating transcription factors responsible for the early immune response. As reported here, structure-function analysis of the CAML gene in Jurkat T cells indicates that two of CAML's putative membrane-spanning domains are necessary and sufficient for the modulation of intracellular calcium. We propose that the hydrophobic C-terminal tail of CAML forms its effector domain, thus implicating the N-terminal hydrophilic domain in a regulatory role. These findings define a novel protein motif that functions in intracellular calcium signaling.

Original languageEnglish (US)
Pages (from-to)8549-8552
Number of pages4
JournalJournal of Biological Chemistry
Volume271
Issue number15
DOIs
StatePublished - Apr 12 1996

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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