TY - JOUR
T1 - The role of calcium-binding proteins in the control of transcription
T2 - Structure to function
AU - Ikura, Mitsuhiko
AU - Osawa, Masanori
AU - Ames, James B.
N1 - Copyright:
Copyright 2008 Elsevier B.V., All rights reserved.
PY - 2002
Y1 - 2002
N2 - Transcriptional regulation is coupled with numerous intracellular signaling processes often mediated by second messengers. Now, growing evidence points to the importance of Ca2+, one of the most versatile second messengers, in activating or inhibiting gene transcription through actions frequently mediated by members of the EF-hand superfamily of Ca2+-binding proteins. Calmodulin and calcineurin, representative members of this EF-hand superfamily, indirectly regulate transcription through phosphorylation/dephosphorylation of transcription factors in response to a Ca2+ increase in the cell. Recently, a novel EF-hand Ca2+-binding protein called DREAM has been found to interact with regulatory sequences of DNA, thereby acting as a direct regulator of transcription. Finally, S100B, a dimeric EF-hand Ca2+ binding protein, interacts with the tumor suppressor p53 and controls its transcriptional activity. In light of the structural studies reported to date, this review provides an overview of the structural basis of EF-hand Ca2+ binding proteins linked with transcriptional regulation.
AB - Transcriptional regulation is coupled with numerous intracellular signaling processes often mediated by second messengers. Now, growing evidence points to the importance of Ca2+, one of the most versatile second messengers, in activating or inhibiting gene transcription through actions frequently mediated by members of the EF-hand superfamily of Ca2+-binding proteins. Calmodulin and calcineurin, representative members of this EF-hand superfamily, indirectly regulate transcription through phosphorylation/dephosphorylation of transcription factors in response to a Ca2+ increase in the cell. Recently, a novel EF-hand Ca2+-binding protein called DREAM has been found to interact with regulatory sequences of DNA, thereby acting as a direct regulator of transcription. Finally, S100B, a dimeric EF-hand Ca2+ binding protein, interacts with the tumor suppressor p53 and controls its transcriptional activity. In light of the structural studies reported to date, this review provides an overview of the structural basis of EF-hand Ca2+ binding proteins linked with transcriptional regulation.
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U2 - 10.1002/bies.10105
DO - 10.1002/bies.10105
M3 - Review article
C2 - 12111723
AN - SCOPUS:0035996798
VL - 24
SP - 625
EP - 636
JO - BioEssays
JF - BioEssays
SN - 0265-9247
IS - 7
ER -