Binding of IRBIT to the IP3 receptor:: Determinants and functional effects

被引：35

作者：

Devogelaere, B

Kasri, NN

Derua, R

Waelkens, E

Callewaert, G

Missiaen, L

Parys, JB

De Smedt, H

机构：

[1] Katholieke Univ Leuven, Fysiol Lab, Louvain, Belgium

[2] Katholieke Univ Leuven, Biochem Lab, Louvain, Belgium

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2006年 / 343卷 / 01期

关键词：

IRBIT; PEST motif; PDZ-ligand; inositol 1,4,5-trisphosphate receptor; IP3-induced Ca2+ release; point-mutation;

D O I：

10.1016/j.bbrc.2006.02.119

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

IRBIT has previously been shown to interact with the inositol 1,4,5-tiispliosphate (IP3) receptor (IP3R) in an IP3-sensitive way. So far it remained to be elucidated whether this interaction was direct or indirect, and whether it was functionally relevant. We now show that IRBIT can directly interact with the IP3R, and that both the suppressor domain and the IP3-binding core of the IP3R are essential for a strong interaction. Moreover, we identified a PEST motif and a PDZ-ligand on IRBIT which were critical for the interaction with the IP3R. Furthermore, we identified Asp-73 as a critical residue for this interaction. Finally, we demonstrated that this interaction functionally affects the IP3R: IRBIT inhibits both IP3 binding and IP3-induced Ca2+ release. (c) 2006 Elsevier Inc. All rights reserved.

引用

页码：49 / 56

页数：8

共 24 条

[1] IRBIT, a novel inositol 1,4,5-trisphosphate (IP3) receptor-binding protein, is released from the IP3 receptor upon IP3 binding to the receptor [J].