Journal
FEBS LETTERS
Volume 580, Issue 27, Pages 6405-6412Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2006.10.054
Keywords
Raf kinase inhibitory protein; Raf-1; kinetic binding analysis; surface plasmon resonance
Funding
- NIGMS NIH HHS [R01 GM64767, R01 GM057959, R01 GM064767] Funding Source: Medline
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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-I in the later phase of mitogen stimulation. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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