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“位置,位置,还是位置”:G蛋白偶联受体对丝裂原活化蛋白激酶的激活与靶向作用

'Location, location, location': activation and targeting of MAP kinases by G protein-coupled receptors.

作者信息

Luttrell L M

机构信息

Department of Medicine, Duke University Medical Center, Durham, North Carolina 27710, USA.

出版信息

J Mol Endocrinol. 2003 Apr;30(2):117-26. doi: 10.1677/jme.0.0300117.

Abstract

A growing body of data supports the conclusion that G protein-coupled receptors can regulate cellular growth and differentiation by controlling the activity of MAP kinases. The activation of heterotrimeric G protein pools initiates a complex network of signals leading to MAP kinase activation that frequently involves cross-talk between G protein-coupled receptors and receptor tyrosine kinases or focal adhesions. The dominant mechanism of MAP kinase activation varies significantly between receptor and cell type. Moreover, the mechanism of MAP kinase activation has a substantial impact on MAP kinase function. Some signals lead to the targeting of activated MAP kinase to specific extranuclear locations, while others activate a MAP kinase pool that is free to translocate to the nucleus and contribute to a mitogenic response.

摘要

越来越多的数据支持这样的结论

G蛋白偶联受体可通过控制丝裂原活化蛋白激酶(MAP激酶)的活性来调节细胞生长和分化。异源三聚体G蛋白池的激活引发了一个复杂的信号网络,导致MAP激酶激活,这通常涉及G蛋白偶联受体与受体酪氨酸激酶或粘着斑之间的相互作用。MAP激酶激活的主要机制在不同的受体和细胞类型之间有很大差异。此外,MAP激酶激活机制对MAP激酶功能有重大影响。一些信号导致活化的MAP激酶靶向特定的核外位置,而其他信号则激活一个可自由转运到细胞核并促成有丝分裂反应的MAP激酶池。

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