ARABIDOPSIS CRINKLY4 Function, Internalization, and Turnover Are Dependent on the Extracellular Crinkly Repeat Domainw⃞

ARABIDOPSIS CRINKLY4 Function, Internalization, and Turnover Are Dependent on the Extracellular Crinkly Repeat Domainw⃞
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拟南芥 CRINKLY4 功能、内化和周转取决于细胞外卷曲重复结构域w⃞

DOI:
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发表时间:
2005
期刊:
The Plant Cell Online
影响因子:
--
通讯作者:
G. Ingram
G. Ingram
中科院分区:
--
文献类型:
--
作者:
M. Gifford;Fiona C. Robertson;D. Soares;G. Ingram

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植物中受体激酶信号传导的调节和细胞动力学研究是一个快速发展的领域,有望为信号感知的分子控制提供巨大的见解。在这项研究中,我们分析了拟南芥植物中 L1 特异性受体激酶 ARABIDOPSIS CRINKLY4 (ACR4) 的行为,并表明它存在于细胞内的两个不同的区室中。这些代表蛋白质输出体和内化囊泡群。同时,缺失分析表明,预测的 β-螺旋桨形成胞外结构域对于 ACR4 功能是必需的。该结构域中具有缺失或点突变的非功能性 ACR4 变体与野生型融合蛋白的行为不同,因为它们的内化程度不同。此外,与看似快速更新的功能性ACR4相比,它们是稳定的。因此,对于 ACR4,内化和周转是相关的,并且取决于功能,这表明 ACR4 信号传导可能会通过内化和降解而受到抑制。观察到的 ACR4 的快速周转使其有别于其他最近研究的植物受体激酶。最后,ACR4 激酶活性并不是蛋白质功能所必需的,因此我们通过类比动物系统提出,ACR4 可能在信号传导过程中与激酶活性伴侣发生异源寡聚化。植物和动物受体激酶具有不同的进化起源。然而,通过最近的其他工作,我们的研究表明,用于调节其活动的机制之间存在相当大的趋同进化。
The study of the regulation and cellular dynamics of receptor kinase signaling in plants is a rapidly evolving field that promises to give enormous insights into the molecular control of signal perception. In this study, we have analyzed the behavior of the L1-specific receptor kinase ARABIDOPSIS CRINKLY4 (ACR4) from Arabidopsis thaliana in planta and have shown it to be present in two distinct compartments within cells. These represent protein export bodies and a population of internalized vesicles. In parallel, deletion analysis has shown that a predicted β-propeller–forming extracellular domain is necessary for ACR4 function. Nonfunctional ACR4 variants with deletions or point mutations in this domain behave differently to wild-type fusion protein in that they are not internalized to the same extent. In addition, in contrast with functional ACR4, which appears to be rapidly turned over, they are stabilized. Thus, for ACR4, internalization and turnover are linked and depend on functionality, suggesting that ACR4 signaling may be subject to damping down via internalization and degradation. The observed rapid turnover of ACR4 sets it apart from other recently studied plant receptor kinases. Finally, ACR4 kinase activity is not required for protein function, leading us to propose, by analogy to animal systems, that ACR4 may hetero-oligomerize with a kinase-active partner during signaling. Plant and animal receptor kinases have distinct evolutionary origins. However, with other recent work, our study suggests that there has been considerable convergent evolution between mechanisms used to regulate their activity.
DOI: 10.1104/pp.120.2.559
发表时间: 1999-06
期刊: Plant physiology
影响因子: 7.4
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