14-3-3 λ protein interacts with ADF1 to regulate actin cytoskeleton dynamics in Arabidopsis
被引:14
作者:
Zhao ShuangShuang
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机构:
Shandong Normal Univ, Life Sci Coll, Key Lab Plant Stress, Jinan 250014, Peoples R China
China Agr Univ, Coll Biol Sci, State Key Lab Plant Physiol & Biochem, Beijing 100193, Peoples R ChinaShandong Normal Univ, Life Sci Coll, Key Lab Plant Stress, Jinan 250014, Peoples R China
Zhao ShuangShuang
[1
,2
]
Zhao YanXiu
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机构:
Shandong Normal Univ, Life Sci Coll, Key Lab Plant Stress, Jinan 250014, Peoples R ChinaShandong Normal Univ, Life Sci Coll, Key Lab Plant Stress, Jinan 250014, Peoples R China
Zhao YanXiu
[1
]
Guo Yan
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机构:
China Agr Univ, Coll Biol Sci, State Key Lab Plant Physiol & Biochem, Beijing 100193, Peoples R ChinaShandong Normal Univ, Life Sci Coll, Key Lab Plant Stress, Jinan 250014, Peoples R China
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
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.