Interaction specificity of Arabidopsis 14-3-3 proteins with phototropin receptor kinases

被引：77
作者：
Sullivan, Stuart [1 ]
Thomson, Catriona E. [1 ]
Kaiserli, Eirini [1 ]
Christie, John M. [1 ]
机构：
[1] Univ Glasgow, Fac Biomed & Life Sci, Plant Sci Grp, Div Mol & Cellular Biol, Glasgow G12 8QQ, Lanark, Scotland
来源：
FEBS LETTERS | 2009年 / 583卷 / 13期
基金：
英国生物技术与生命科学研究理事会;
关键词：
14-3-3; Protein; Signalling; Protein phosphorylation; Photoreceptor; Kinase activity; Protein-protein interaction; Arabidopsis thaliana; MEMBRANE H+-ATPASE; BLUE-LIGHT; PHOSPHORYLATION SITE; VOLTAGE DOMAINS; PHOTORECEPTOR; BINDING; NPH1; 14-3-3-PROTEIN; LOCALIZATION; ASSOCIATION;
D O I：
10.1016/j.febslet.2009.06.011
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：
Phototropin receptor kinases play an important role in optimising plant growth in response to blue light. Much is known regarding their photochemical reactivity, yet little progress has been made to identify downstream signalling components. Here, we isolated several interacting proteins for Arabidopsis phototropin 1 (phot1) by yeast two-hybrid screening. These include members of the NPH3/RPT2 (NRL) protein family, proteins associated with vesicle traf. cking, and the 14-3-3 lambda (k) isoform from Arabidopsis. 14-3-3 lambda and phot1 were found to colocalise and interact in vivo. Moreover, 14-3-3 binding to phot1 was limited to non-epsilon 14-3-3 isoforms and was dependent on key sites of receptor autophosphorylation. No 14-3-3 binding was detected for Arabidopsis phot2, suggesting that 14-3-3 proteins are specific to phot1 signalling. Structured summary: MINT-7146953: PHOT1 (uniprotkb: O48963) physically interacts (MI: 0915) with ARF7 (uniprotkb: Q9LFJ7) by two hybrid (MI: 0018) MINT-7147335: PHOT1 (uniprotkb: O48963) physically interacts (MI: 0914) with 14-3-3 phi (uniprotkb: P46077) by far Western blotting (MI: 0047) MINT-7146854: PHOT1 (uniprotkb: O48963) physically interacts (MI: 0915) with RPT2 (uniprotkb: Q682S0) by two hybrid (MI: 0018) MINT-7147215: PHOT1 (uniprotkb: O48963) physically interacts (MI: 0914) with 14-3-3 lambda (uniprotkb: P48349) by anti tag coimmunoprecipitation (MI: 0007) MINT-7147044, MINT-7147185, MINT-7147200, MINT-7147413: PHOT1 (uniprotkb: O48963) physically interacts (MI: 0914) with 14-3-3 lambda (uniprotkb: P48349) by far Western blotting (MI: 0047) MINT-7146983: PHOT1 (uniprotkb: O48963) physically interacts (MI: 0915) with 14-3-3 lambda (uniprotkb: P48349) by two hybrid (MI: 0018) MINT-7146871: PHOT1 (uniprotkb: O48963) physically interacts (MI: 0915) with NPH3-like (uniprotkb: Q9S9Q9) by two hybrid (MI: 0018) MINT-7146905: PHOT1 (uniprotkb: O48963) physically interacts (MI: 0915) with ARF2 (uniprotkb: Q9M1P5) by two hybrid (MI: 0018) MINT-7147364: PHOT1 (uniprotkb: O48963) physically interacts (MI: 0914) with 14-3-3 upsilon (uniprotkb: P42645) by far Western blotting (MI: 0047) MINT-7147234: PHOT1 (uniprotkb: O48963) physically interacts (MI: 0914) with 14-3-3 kappa (uniprotkb: P48348) by far Western blotting (MI: 0047) (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
引用
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页码：2187 / 2193
页数：7
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