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XB-ART-15593
Cell Growth Differ 1998 Jan 01;91:41-8.
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The immunophilin FKBP65 forms an association with the serine/threonine kinase c-Raf-1.

Coss MC , Stephens RM , Morrison DK , Winterstein D , Smith LM , Simek SL .


Abstract
FKBP65 is a member of the FK506-binding protein class of immunophilins and is the only member reported to contain four peptidylprolyl cis-trans isomerase domains and an unrelated COOH-terminal domain. In this report, we show that the heat shock protein hsp90 and the serine/threonine protein kinase c-Raf-1 are components of FKBP65 immune complexes. The NH2-terminal regulatory domain of c-Raf-1 appears to be required for its interaction with FKBP65. Using GST-FKBP65 fusion protein and purified Raf proteins, we show that full-length FKBP65 can interact with c-Raf-1 but not B-Raf. The activation kinetics of c-Raf-1 after v-H-RasV12 injection of Xenopus oocytes appear to correlate with FKBP65/c-Raf-1 interaction, suggesting that FKBP65 may preferentially associate with forms of c-Raf-1 that are more posttranslationally modified. The interaction of FKBP65 with the c-Raf-heat shock protein 90 heterocomplex implicates this immunophilin in signal-transduction processes.

PubMed ID: 9438387
Article link: Cell Growth Differ


Species referenced: Xenopus laevis
Genes referenced: braf hsp90aa1.1 raf1 snrpe