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Regulation of RKIP binding to the N‐region of the Raf‐1 kinase
Author(s) -
Park Sungdae,
Rath Oliver,
Beach Sandy,
Xiang Xiaoqin,
Kelly Sharon M.,
Luo Zhijun,
Kolch Walter,
Yeung Kam C.
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.10.054
Subject(s) - kinase , phosphorylation , surface plasmon resonance , chemistry , mapk/erk pathway , protein kinase a , binding site , protein kinase domain , peptide , linker , microbiology and biotechnology , mitogen activated protein kinase , biochemistry , biology , gene , mutant , materials science , nanotechnology , nanoparticle , computer science , operating system
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.