Inositol 1,4,5-trisphosphate receptor type 1 phosphorylation and regulation by extracellular signal-regulated kinase
| Autor: | Xiu-Ying Huang, Fang-Zhen Sun, Ling-Hai Yang, Gui-Rong Bai |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
MAPK/ERK pathway
Molecular Sequence Data Biophysics Receptors Cytoplasmic and Nuclear Biochemistry MAP2K7 Phosphorylation cascade Mice chemistry.chemical_compound Microsomes Serine Animals Inositol 1 4 5-Trisphosphate Receptors Inositol Amino Acid Sequence Phosphorylation Extracellular Signal-Regulated MAP Kinases Molecular Biology Binding Sites biology Kinase Cyclin-dependent kinase 2 Cell Biology Molecular biology Protein Structure Tertiary Cell biology chemistry biology.protein Calcium Calcium Channels Intracellular |
| Zdroj: | Biochemical and Biophysical Research Communications. 348:1319-1327 |
| ISSN: | 0006-291X |
| Popis: | Type 1 inositol 1,4,5-trisphosphate receptor (IP(3)R1) is a widely expressed intracellular calcium-release channel found in many cell types. The operation of IP(3)R1 is regulated through phosphorylation by multiple protein kinases. Extracellular signal-regulated kinase (ERK) has been found involved in calcium signaling in distinct cell types, but the underlying mechanisms remain unclear. Here, we present evidence that ERK1/2 and IP(3)R1 bind together through an ERK binding motif in mouse cerebellum in vivo as well as in vitro. ERK-phosphorylating serines (Ser 436) was identified in mouse IP(3)R1 and Ser 436 phosphorylation had a suppressive effect on IP(3) binding to the recombinant N-terminal 604-amino acid residues (N604). Moreover, phosphorylation of Ser 436 in R(224-604) evidently enhance its interaction with the N-terminal "suppressor" region (N223). At last, our data showed that Ser 436 phosphorylation in IP(3)R1 decreased Ca(2+) releasing through IP(3)R1 channels. |
| Databáze: | OpenAIRE |
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