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

29 Citations (Scopus)

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
StatePublished - Apr 12 1996
Externally publishedYes

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Cyclophilins
Calcium Signaling
T-cells
Ligands
Calcium
T-Lymphocytes
Activating Transcription Factors
Amino Acid Motifs
Jurkat Cells
Carrier Proteins
Genes
Modulation
Membranes
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

A hydrophobie domain of Ca2+-modulating cyclophilin ligand modulates calcium influx signaling in T lymphocytes. / Holloway, Michael P.; Bram, Richard J.

In: Journal of Biological Chemistry, Vol. 271, No. 15, 12.04.1996, p. 8549-8552.

Research output: Contribution to journalArticle

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