Regulation of RKIP binding to the N-region of the Raf-1 kinase |
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Authors: | Park Sungdae Rath Oliver Beach Sandy Xiang Xiaoqin Kelly Sharon M Luo Zhijun Kolch Walter Yeung Kam C |
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Affiliation: | Medical University of Ohio, Department of Biochemistry and Cancer Biology, 3035 Arlington Avenue, Toledo, OH 43614-5804, USA. |
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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. |
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Keywords: | Raf kinase inhibitory protein Raf-1 Kinetic binding analysis Surface plasmon resonance |
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