TY - JOUR
T1 - A hydrophobie domain of Ca2+-modulating cyclophilin ligand modulates calcium influx signaling in T lymphocytes
AU - Holloway, Michael P.
AU - Bram, Richard J.
PY - 1996/4/12
Y1 - 1996/4/12
N2 - 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.
AB - 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.
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U2 - 10.1074/jbc.271.15.8549
DO - 10.1074/jbc.271.15.8549
M3 - Article
C2 - 8621480
AN - SCOPUS:0029664622
SN - 0021-9258
VL - 271
SP - 8549
EP - 8552
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 15
ER -