Li Xiang, MacLeod Ruth, Dunlop Allan J, Edwards Helen V, Advant Noopur, Gibson Lucien C D, Devine Nicola M, Brown Kim M, Adams David R, Houslay Miles D, Baillie George S
Neuroscience and Molecular Pharmacology, Faculty of Biomedical and Life Sciences, Wolfson Building, Glasgow University, Glasgow G12 8QQ, United Kingdom.
FEBS Lett. 2009 Oct 20;583(20):3310-6. doi: 10.1016/j.febslet.2009.09.035. Epub 2009 Sep 24.
Beta arrestins are molecular scaffolds that can bring together three-component mitogen-activated protein kinase signalling modules to promote signal compartmentalisation. We use peptide array technology to define novel interfaces between components within the c-Jun N-terminal kinase (JNK)/beta arrestin signalling complex. We show that beta arrestin 1 and beta arrestin 2 associate with JNK3 via the kinase N-terminal domain in a region that, surprisingly, does not harbour a known 'common docking' motif. In the N-domain and C-terminus of beta arrestin 1 and beta arrestin 2 we identify two novel apoptosis signal-regulating kinase 1 binding sites and in the N-domain of the beta arrestin 1 and beta arrestin 2 we identify a novel MKK4 docking site.
β抑制蛋白是一种分子支架,它能够将三组分丝裂原活化蛋白激酶信号模块聚集在一起,以促进信号的区室化。我们利用肽阵列技术来确定c-Jun氨基末端激酶(JNK)/β抑制蛋白信号复合物中各组分之间的新型相互作用界面。我们发现,β抑制蛋白1和β抑制蛋白2通过激酶的N末端结构域与JNK3结合,令人惊讶的是,该区域并没有已知的“通用对接”基序。在β抑制蛋白1和β抑制蛋白2的N结构域和C末端,我们鉴定出两个新型凋亡信号调节激酶1结合位点,在β抑制蛋白1和β抑制蛋白2的N结构域中,我们鉴定出一个新型MKK4对接位点。