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Regulation of MAP kinase signaling modules by scaffold proteins in mammals.
Annual Review of Cell and Developmental Biology ( IF 11.4 ) Pub Date : 2003-10-23 , DOI: 10.1146/annurev.cellbio.19.111401.091942
Deborah K Morrison 1 , Roger J Davis
Affiliation  

The mitogen-activated protein kinase (MAPK) group of serine/threonine protein kinases mediates the response of cells to many extracellular stimuli such as cytokines and growth factors. These protein kinases include the extracellular signal-regulated protein kinases (ERK) and two stress-activated protein kinases (SAPK), the c-Jun N-terminal kinases (JNK), and the p38 MAPK. The enzymes are evolutionarily conserved and are activated by a common mechanism that involves a protein kinase cascade. Scaffold proteins have been proposed to interact with MAPK pathway components to create a functional signaling module and to control the specificity of signal transduction. Here we critically evaluate the evidence that supports a physiologically relevant role of MAPK scaffold proteins in mammals.

中文翻译:

哺乳动物中支架蛋白对MAP激酶信号传导模块的调节。

丝氨酸/苏氨酸蛋白激酶的促分裂原活化蛋白激酶(MAPK)组介导细胞对许多细胞外刺激物(例如细胞因子和生长因子)的反应。这些蛋白激酶包括细胞外信号调节蛋白激酶(ERK)和两个应激激活蛋白激酶(SAPK),c-Jun N端激酶(JNK)和p38 MAPK。这些酶在进化上是保守的,并通过涉及蛋白激酶级联的常见机制激活。已经提出支架蛋白与MAPK途径组分相互作用以产生功能性信号传导模块并控制信号转导的特异性。在这里,我们严格评估支持MAPK支架蛋白在哺乳动物中生理相关作用的证据。
更新日期:2019-11-01
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