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Regulation of RKIP binding to the N-region of the Raf-1 kinase.


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.

SUBMITTER: Park S 

PROVIDER: S-EPMC1892598 | biostudies-literature | 2006 Nov

REPOSITORIES: biostudies-literature

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Regulation of RKIP binding to the N-region of the Raf-1 kinase.

Park Sungdae S   Rath Oliver O   Beach Sandy S   Xiang Xiaoqin X   Kelly Sharon M SM   Luo Zhijun Z   Kolch Walter W   Yeung Kam C KC  

FEBS letters 20061103 27


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 a  ...[more]

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