RKIP与Raf-1激酶N区域结合的调控。
Regulation of RKIP binding to the N-region of the Raf-1 kinase.
作者信息
Park Sungdae, Rath Oliver, Beach Sandy, Xiang Xiaoqin, Kelly Sharon M, Luo Zhijun, Kolch Walter, Yeung Kam C
机构信息
Medical University of Ohio, Department of Biochemistry and Cancer Biology, 3035 Arlington Avenue, Toledo, OH 43614-5804, USA.
出版信息
FEBS Lett. 2006 Nov 27;580(27):6405-12. doi: 10.1016/j.febslet.2006.10.054. Epub 2006 Nov 3.
Abstract
The Raf kinase inhibitory protein (RKIP) binds to Raf-1 interfering with binding of the MEK substrate and potentially also Raf-1 activation. In response to mitogen stimulation RKIP dissociates from Raf-1 and later re-associates. Here, using a combination of mutational approaches, biochemical studies, peptide arrays and plasmon surface resonance (BIAcore), we fine map and characterize a minimal 24 amino acid long RKIP binding domain in the Raf-1 N-region, which consists of constitutive elements at both flanks and a center element that is regulated by phosphorylation and enhances the re-binding of RKIP to Raf-1 in the later phase of mitogen stimulation.
摘要
Raf激酶抑制蛋白（RKIP）与Raf-1结合，干扰MEK底物的结合，也可能干扰Raf-1的激活。响应有丝分裂原刺激时，RKIP从Raf-1上解离，随后重新结合。在此，我们结合突变方法、生化研究、肽阵列和表面等离子体共振（BIAcore），对Raf-1 N区域中一个最小的24个氨基酸长的RKIP结合域进行精细定位和表征，该区域由两侧的组成元件和一个中心元件组成，中心元件受磷酸化调节，并在有丝分裂原刺激后期增强RKIP与Raf-1的重新结合。
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