14-3-3 λ protein interacts with ADF1 to regulate actin cytoskeleton dynamics in Arabidopsis

被引:14
作者
Zhao ShuangShuang [1 ,2 ]
Zhao YanXiu [1 ]
Guo Yan [2 ]
机构
[1] Shandong Normal Univ, Life Sci Coll, Key Lab Plant Stress, Jinan 250014, Peoples R China
[2] China Agr Univ, Coll Biol Sci, State Key Lab Plant Physiol & Biochem, Beijing 100193, Peoples R China
基金
中国国家自然科学基金;
关键词
Arabidopsis; 14-3-3; ADF; phosphorylation; actin cytoskeleton dynamics; DEPOLYMERIZING FACTOR; STOMATAL MOVEMENT; ORGANIZATION; FILAMENTS; COFILIN; COMPLEX; KINASE; GROWTH; PHOSPHORYLATION; LOCALIZATION;
D O I
10.1007/s11427-015-4897-1
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
Actin cytoskeleton dynamics is critical for variety of cellular events including cell elongation, division and morphogenesis, and is tightly regulated by numerous groups of actin binding proteins. However it is not well understood how these actin binding proteins are modulated in a physiological condition by their interaction proteins. In this study, we describe that Arabidopsis 14-3-3 lambda protein interacted with actin depolymerizing factor 1 (ADF1) in plant to regulate F-actin stability and dynamics. Loss of 14-3-3 lambda in Arabidopsis resulted in longer etiolated hypocotyls in dark and changed actin cytoskeleton architecture in hypocotyl cells. Overexpression of ADF1 repressed 14-3-3 lambda mutant hypocotyl elongation and actin dynamic phenotype. In addition, the phosphorylation level of ADF1 was increased and the subcellular localization of ADF1 was altered in 14-3-3 lambda mutant. Consistent with these observations, the actin filaments were more stable in 14-3-3 lambda mutant. Our results indicate that 14-3-3 lambda protein mediates F-actin dynamics possibly through inhibiting ADF1 phosphorylation in vivo.
引用
收藏
页码:1142 / 1150
页数:9
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