4.1N binding regions of inositol 1,4,5-trisphosphate receptor type 1

被引：24

作者：

Fukatsu, K ^{[1
]}

Bannai, H ^{[1
]}

Inoue, T ^{[1
]}

Mikoshiba, K ^{[1
]}

机构：

[1] Univ Tokyo, Inst Med Sci, Div Mol Neurobiol, Tokyo 1088639, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2006年 / 342卷 / 02期

关键词：

inositol 1,4,5-trisphosphate receptor type 1; 4.1N; CTT14aa; CTM1; immunoprecipitation; diffusion;

D O I：

10.1016/j.bbrc.2006.02.010

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

Zhang et al. and Maximov et al. [S. Zhang, A. Mizutani, C. Hisatsune, T. Higo, H. Bannai, T. Nakayama, M. Hattori, and K. Mikoshiba, Protein 4.1 N is required for translocation of inositol 1,4,5-trisphosphate receptor type I to the basolateral membrane domain in polarized Madin-Darby canine kidney cells, J. Biol. Chem. 278 (2003) 4048-4056; A. Maximov, T. S. Tang. and I. Bezprozvanny, Association of the type I inositol (1,4,5)-trisphosphate receptor with 4.1 N protein in neurons, Mol. Cell. Neurosci. 22 (2003) 271-283.] reported that 4. 1 N is a binding partner of inositol 1,4,5-trisphosphate receptor type I (IP(3)R1), however the binding site of IP(3)R1 differed: the former determined the C-terminal 14 amino acids of the cytoplasmic tail (CTT14aa) as the binding site.. while the latter assigned another segment, cytoplasmic tail middle 1 (CTM1). To solve this discrepancy, we performed immunoprecipitation and found that both the segments had binding activity to 4.1N. Both segments also interfered the 4.1N-regulated IP3R1 diffusion in neuronal dendrites. However, IP(3)R1 lacking the CTT14aa (IP(3)R1-ACTT14aa) does not bind to 4. 1 N [S. Zhang, A. Mizutani, C. Hisatsune, T. Higo, H. Bannai, T. Nakayama, M. Hattori, and K. Mikoshiba, Protein 4. IN is required for translocation of inositol 1,4,5-trisphosphate receptor type I to the basolateral. membrane domain in polarized Madin-Darby canine kidney cells, J. Biol. Chem. 2 78 (2003) 4048-4056.] and its diffusion constant is larger than that of IP(3)R1 full-length in neuronal dendrites [K. Fukatsu, H. Bannai.. S. Zhang, H. Nakamura, T. Inoue, and K. Mikoshiba, Lateral diffusion of inositol 1,4,5-trisphosphate receptor type I is regulated by actin filaments and 4. 1 N in neuronal dendrites, J. Biol. Chem. 279 (2004) 48976-48982.]. We conclude that both the CTT14aa and CTM1 sequences can bind to 4.1N in peptide fragment forms. However, we propose that the responsible binding site for 4.1 N binding in full-length tetramer form of IP(3)R1 is CTT14aa. (c) 2006 Elsevier Inc. All rights reserved.

引用

页码：573 / 576

页数：4

共 19 条

[1]

Calcium signalling: Dynamics, homeostasis and remodelling [J].