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Inositol 1,4,5‐trisphosphate receptor (type 1) phosphorylation and modulation by Cdc2
Author(s) -
Malathi Krishnamurthy,
Kohyama Shinya,
Ho Michael,
Soghoian Damien,
Li Xiaogui,
Silane Michael,
Berenstein Alejandro,
Jayaraman Thottala
Publication year - 2003
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.10720
Subject(s) - cyclin dependent kinase 1 , phosphorylation , microbiology and biotechnology , inositol trisphosphate receptor , inositol , endoplasmic reticulum , intracellular , cyclin dependent kinase , kinase , biology , receptor , cell cycle , biochemistry , cell
Abstract Calcium (Ca 2+ ) release from the endoplasmic reticulum (ER) controls numerous cellular functions including proliferation, and is regulated in part by inositol 1,4,5‐trisphosphate receptors (IP3Rs). IP3Rs are ubiquitously expressed intracellular Ca 2+ ‐release channels found in many cell types. Although IP3R‐mediated Ca 2+ release has been implicated in cellular proliferation, the biochemical pathways that modulate intracellular Ca 2+ release during cell cycle progression are not known. Sequence analysis of IP3R1 reveals the presence of two putative phosphorylation sites for cyclin‐dependent kinases (cdks). In the present study, we show that cdc2/CyB, a critical regulator of eukaryotic cell cycle progression, phosphorylates IP3R1 in vitro and in vivo at both Ser 421 and Thr 799 and that this phosphorylation increases IP3 binding. Taken together, these results indicate that IP3R1 may be a specific target for cdc2/CyB during cell cycle progression. © 2003 Wiley‐Liss, Inc.