14-3-3 and FHA Domains Mediate Phosphoprotein Interactions

被引：134

作者：

Chevalier, David ^{[1
,2
,3
]}

Morris, Erin R. ^{[1
,2
,4
]}

Walker, John C. ^{[1
,2
]}

机构：

[1] Univ Missouri, Div Biol Sci, Columbia, MO 65211 USA

[2] Univ Missouri, Bond Life Sci Ctr, Columbia, MO 65211 USA

[3] Mississippi State Univ, Dept Biol Sci, Mississippi State, MS 39762 USA

[4] Baker Univ, Dept Biol, Baldwin City, KS 66006 USA

来源：

ANNUAL REVIEW OF PLANT BIOLOGY | 2009年 / 60卷

基金：

美国国家科学基金会;

关键词：

signal transduction; protein interactions; phosphorylation; metabolism; transcription; miRNA; MEMBRANE H+-ATPASE; DEPENDENT PROTEIN-KINASE; PHOSPHORYLATED NITRATE REDUCTASE; SUCROSE-PHOSPHATE SYNTHASE; FORKHEAD-ASSOCIATED DOMAIN; C-TERMINAL REGION; RECEPTOR KINASE; ARABIDOPSIS-THALIANA; SIGNAL-TRANSDUCTION; GENE-EXPRESSION;

D O I：

10.1146/annurev.arplant.59.032607.092844

中图分类号：

Q94 [植物学];

学科分类号：

071001 ;

摘要：

Many aspects of plant growth and development require specific protein interactions to carry out biochemical and Cellular functions. Several proteins mediate these interactions, two of which specifically recognize phosophoproteins: 14-3-3 proteins and proteins with FHA domains. These are the only phosphobinding domains identified in plants. Both domains are present in animals and plants, and are used by plant proteins to regulate metabolic, developmental, and signaling pathways. 14-3-3s regulate sugar metabolism, proton gradients, and control transcription factor localization. FHA domains are Modular domains often found in multidomain proteins that are involved in signal transduction and plant development.

引用

页码：67 / 91

页数：25

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