Nuclear protein phosphatases with Kelch-repeat domains modulate the response to bras sino steroids in Arabidopsis
Nuclear protein phosphatases with Kelch-repeat domains modulate the response to bras sino steroids in Arabidopsis
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DOI：
10.1101/gad.1174204
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发表时间：
2004-02-15
影响因子：
10.5
通讯作者：
Chory, J
中科院分区：
文献类型：
--
作者：
Mora-García, S;Vert, G;Chory, J
通过膜相关受体激酶BRI 1感知植物类固醇激素油菜素（BL），触发转录调节因子BES 1和BZR 1在细胞核中的去磷酸化和积累。我们确定bsu 1 -1D作为一个显性抑制剂的bri 1在拟南芥。BSU 1编码一个位于核内的丝氨酸-苏氨酸蛋白磷酸酶，其N-末端具有Kelch重复结构域，并优先在伸长细胞中表达。BSU 1能够调节BES 1的磷酸化状态，抵消糖原合成酶激酶-3 BIN 2的作用，并导致去磷酸化BES 1的稳态水平增加。BSU 1属于一个小的基因家族;功能丧失分析揭示了家族成员之间的功能重叠程度，并证实了这些磷酸酶在BL控制细胞伸长中的作用。我们的数据表明，BES 1是受拮抗磷酸化和去磷酸化反应在细胞核中，微调的幅度的BL的反应。
Perception of the plant steroid hormone brassinolide (BL) by the membrane-associated receptor kinase BRI1 triggers the dephosphorylation and accumulation in the nucleus of the transcriptional modulators BES1 and BZR1. We identified bsu1-1D as a dominant suppressor of bri1 in Arabidopsis. BSU1 encodes a nuclear-localized serine-threonine protein phosphatase with an N-terminal Kelch-repeat domain, and is preferentially expressed in elongating cells. BSU1 is able to modulate the phosphorylation state of BES1, counteracting the action of the glycogen synthase kinase-3 BIN2, and leading to increased steady-state levels of dephosphorylated BES1. BSU1 belongs to a small gene family; loss-of-function analyses unravel the extent of functional overlap among members of the family and confirm the role of these phosphatases in the control of cell elongation by BL. Our data indicate that BES1 is subject to antagonistic phosphorylation and dephosphorylation reactions in the nucleus, which fine-tune the amplitude of the response to BL.