Control of meristem development by CLAVATA1 receptor kinase and kinase-associated protein phosphatase interactions
Control of meristem development by CLAVATA1 receptor kinase and kinase-associated protein phosphatase interactions
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DOI：
10.1104/pp.117.4.1217
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发表时间：
1998-08-01
期刊：
影响因子：
7.4
通讯作者：
Clark, SE
中科院分区：
文献类型：
--
作者：
Stone, JM;Trotochaud, AE;Clark, SE
CLAVATA1（CLV1）基因编码一种假定的受体激酶，这种激酶是拟南芥茎和花分生组织中细胞增殖和分化之间的适当平衡所必需的。受损的CLV1信号传导导致在芽和花分生组织处的大量未分化细胞。虽然许多推定的受体激酶已被确定在植物中，植物受体样激酶介导的信号转导机制在很大程度上是未知的。受体激酶信号传导的一个潜在效应子是激酶相关蛋白磷酸酶（KAPP），它是一种以磷酸化依赖性方式与多种植物受体样激酶结合的蛋白质。为了研究KAPP在CLV 1依赖的植物发育中的可能作用，在体外和体内研究了CLV 1和KAPP的相互作用。KAPP在体外直接与自磷酸化的CLV1结合，并与来自分生组织的植物提取物中的CLV1共免疫沉淀。在中间clv1突变体中KAPP转录物积累的减少抑制了突变体表型，并且抑制程度与KAPP mRNA水平呈负相关。这些数据表明KAPP在植物发育中作为CLV 1信号传导的负调节剂起作用。这可能代表了KAPP与受体激酶相互作用的一般模型。
The CLAVATA1 (CLV1) gene encodes a putative receptor kinase required for the proper balance between cell proliferation and differentiation in Arabidopsis shoot and flower meristems. impaired CLV1 signaling results in masses of undifferentiated cells at the shoot and floral meristems. Although many putative receptor kinases have been identified in plants, the mechanism of signal transduction mediated by plant receptor-like kinases is largely unknown. One potential effector of receptor kinase signaling ic; kinase-associated protein phosphatase (KAPP), a protein that binds to multiple plant receptor-like kinases in a phosphorylation-dependent manner. To examine a possible role for KAPP in CLV1-dependent plant development, the interaction of CLV1 and KAPP was investigated in vitro and in vivo. KAPP binds directly to autophosphorylated CLV1 in vitro and co-immunoprecipitates with CLV1 in plant extracts derived from meristematic tissue. Reduction of KAPP transcript accumulation in an intermediate clv1 mutant suppresses the mutant phenotype, and the degree of suppression is inversely correlated with KAPP mRNA levels. These data suggest that KAPP functions as a negative regulator of CLV1 signaling in plant development. This may represent a general model for the interaction of KAPP with receptor kinases.