14‐3‐3 proteins: regulation of signal‐induced events

信号转导 磷酸化 功能(生物学) 生物 拟南芥 转导(生物物理学) 蛋白质磷酸化 细胞生物学 14-3-3蛋白质 计算生物学 遗传学 生物化学 突变体 基因 蛋白激酶A
作者
Robert J. Ferl
出处
期刊:Physiologia Plantarum [Wiley]
卷期号:120 (2): 173-178 被引量:96
标识
DOI:10.1111/j.0031-9317.2004.0239.x
摘要

The field of signal transduction has experienced a significant paradigm shift as a result of an increased understanding of the roles of 14-3-3 proteins. There are many cases where signal-induced phosphorylation itself may cause a change in protein function. This simple modification is, in fact, the primary basis of signal transduction events in many systems. There are a large and growing number of cases, however, where simple phosphorylation is not enough to effect a change in protein function. In these cases, the 14-3-3 proteins can be required to complete the change in function. Therefore signal transduction can be either the relatively simple process where phosphorylation alters target activity, or it can be a more complex, multistep process with the 14-3-3 proteins playing the major role of bringing the signal transduction event to completion. This makes 14-3-3-modulated signal transduction a more complicated process with additional avenues for regulation and variety. Adding further complexity to the process is the fact that 14-3-3 proteins are present as multigene families in most organisms (Aitken et al. Trends Biochem Sci 17: 498-501, 1992; Ferl Annu Rev Plant Physiol Plant Molecular Biology 47: 49-73, 1996), with each member of the family being differentially expressed in various tissues and with potentially differential affinity for various target proteins. This review focuses on the 14-3-3 family of Arabidopsis as a model for further developing understanding of the roles of the 14-3-3 proteins as modulators of signal transduction events in plants. The primary approaches to these questions are not unlike the approaches that would be used in the functional dissection of any multigene family, but the interpretation of these data will have wide implications since the 14-3-3 s physically interact with other protein families.
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