The complexity of Raf-1 regulation

https://doi.org/10.1016/S0955-0674(97)80060-9Get rights and content

Abstract

The activation of the serine/threonine kinase Raf-1 is proving to be an intricate multistep process. Recent advances in elucidating how Raf-1 becomes activated in response to signaling events have emphasized the role of phosphorylation emerging is that Raf-1 activity can be regulated by multiple mechanisms.

References (62)

  • M Wartmann et al.

    The native structure of the activated Raf protein kinases is a membrane-bound multi-subunit complex

    J Biol Chem

    (1994)
  • TW Schulte et al.

    Disruption of the Raf-1-Hsp90 molecular complex results in destabilization of Raf-1 and loss of Raf-1-Ras association

    J Biol Chem

    (1995)
  • M Therrien et al.

    KSR modulates signal propagation within the MAPK cascade

    Genes Dev

    (1996)
  • W Kolch et al.

    Protein kinase Cα activates Raf-1 by direct phosphorylation

    Nature

    (1993)
  • Y Ueda et al.

    Protein kinase C δ activates the MEK-ERK pathway in a manner independent of Ras and dependent on Raf

    J Biol Chem

    (1996)
  • ML Samuels et al.

    Conditional transformation of cells and rapid activation of the mitogen-activated protein kinase cascade by an estradiol-dependent human Raf-1 protein kinase

    Mol Cell Biol

    (1993)
  • G Daum et al.

    The ins and outs of Raf kinases

    Trends Biochem Sci

    (1994)
  • G Heidecker et al.

    Mutational activation of c-raf-1 and definition of the minimal transforming sequence

    Mol Cell Biol

    (1990)
  • VP Stanton et al.

    Definition of the human raf amino-terminal regulatory region by deletion mutagenesis

    Mol Cell Biol

    (1989)
  • D Stokoe et al.

    Activation of Raf as a result of recruitment to the plasma membrane

    Science

    (1994)
  • SJ Leevers et al.

    Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane

    Nature

    (1994)
  • AB Vojitek et al.

    Mammalian Ras interacts directly with the serine/threonine kinase Raf

    Cell

    (1993)
  • N Nassar et al.

    The 2.2 Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue

    Nature

    (1995)
  • C Gorman et al.

    Equilibrium and kinetic measurements reveal rapidly reversible binding of Ras to Raf

    J Biol Chem

    (1996)
  • TR Brtva et al.

    Two distinct Raf domains mediate interaction with Ras

    J Biol Chem

    (1995)
  • JK Drugan et al.

    Ras interaction with two distinct binding domains in Raf-1 may be required for Ras transformation

    J Biol Chem

    (1996)
  • C Hu et al.

    Cysteine-rich region of Raf-1 interacts with activator domain of post-translationally modified Ha-Ras

    J Biol Chem

    (1995)
  • S Ghosh et al.

    The cysteine-rich region of Raf-1 kinase contains zinc, translocates to liposomes and is adjacent to a segment that bind GTP-Ras

    J Biol Chem

    (1994)
  • EC Lerner et al.

    Ras CAAX peptidomimetic FTI-277 selectively blocks oncogenic Ras signaling by inducing cytoplasmic accumulation of inactive Ras—Raf complexes

    J Biol Chem

    (1995)
  • T Okada et al.

    Post-translational modification of H-Ras is required for activation of, but not for association with, B-Raf

    J Biol Chem

    (1996)
  • GJ Clark et al.

    Peptides containing a consensus Ras binding sequence from Raf-1 and the GTPase activating protein NF1 inhibit Ras function

    Proc Natl Acad Sci USA

    (1996)
  • Cited by (0)

    View full text