| First Author | Bai GR | Year | 2006 |
| Journal | Biochem Biophys Res Commun | Volume | 348 |
| Issue | 4 | Pages | 1319-27 |
| PubMed ID | 16925983 | Mgi Jnum | J:112584 |
| Mgi Id | MGI:3662805 | Doi | 10.1016/j.bbrc.2006.07.208 |
| Citation | Bai GR, et al. (2006) Inositol 1,4,5-trisphosphate receptor type 1 phosphorylation and regulation by extracellular signal-regulated kinase. Biochem Biophys Res Commun 348(4):1319-27 |
| abstractText | 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. |
