Inositol 1,4,5-trisphosphate receptor (type 1) phosphorylation and modulation by Cdc2
| Autor: | Krishnamurthy Malathi, Shinya Kohyama, Michael Ho, Damien Soghoian, Xiaogui Li, Michael Silane, Alejandro Berenstein, Thottala Jayaraman |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
Threonine
Receptors Cytoplasmic and Nuclear Inositol 1 4 5-Trisphosphate Biology Biochemistry Calcium in biology Jurkat Cells chemistry.chemical_compound CDC2 Protein Kinase Serine Animals Humans Inositol 1 4 5-Trisphosphate Receptors Inositol Amino Acid Sequence Phosphorylation Receptor Molecular Biology Mitotic catastrophe Cyclin-dependent kinase 1 Cell Cycle Cell Biology humanities Cell biology chemistry Apoptosis Inositol 1 4 5 triphosphate receptor Calcium Calcium Channels Antibodies Phospho-Specific |
| Zdroj: | Journal of Cellular Biochemistry. 90:1186-1196 |
| ISSN: | 1097-4644 0730-2312 |
| DOI: | 10.1002/jcb.10720 |
| Popis: | Calcium (Ca2+) 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 Ca2+-release channels found in many cell types. Although IP3R-mediated Ca2+ release has been implicated in cellular proliferation, the biochemical pathways that modulate intracellular Ca2+ 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. |
| Databáze: | OpenAIRE |
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