◀ Back to RAF1
PAK3 — RAF1
Pathways - manually collected, often from reviews:
-
KEGG Focal adhesion:
PAK1/PAK2/PAK3/PAK4/PAK6/PAK7
→
RAF1
(protein-protein, phosphorylation)
-
WikiPathways Focal Adhesion:
PAK1/PAK3/PAK2/PAK4/PAK7/PAK6
→
ARAF/BRAF/RAF1
(activation)
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
-
IRef Hprd Interaction:
RAF1
—
PAK3
(in vivo)
Mason et al., EMBO J 1999, Zang et al., J Biol Chem 2002*, Diaz et al., Mol Cell Biol 1997*, King et al., Nature 1998*
-
IRef Hprd Interaction:
RAF1
—
PAK3
(in vitro)
Mason et al., EMBO J 1999, Zang et al., J Biol Chem 2002*, Diaz et al., Mol Cell Biol 1997*, King et al., Nature 1998*
Text-mined interactions from Literome
Sun et al., Curr Biol 2000
:
Thus, Raf-1 activation by Ras is achieved through a combination of both physical interaction and indirect mechanisms involving the activation of a second Ras effector, PI 3-kinase, which directs
Pak mediated regulatory phosphorylation of
Raf-1
Chiloeches et al., Mol Cell Biol 2001
:
S338 phosphorylation of
Raf-1 is
independent of phosphatidylinositol 3-kinase and
Pak3 ... The recent suggestion that
Pak3 could
stimulate Raf-1 activity by directly phosphorylating S338 through a Ras/phosphatidylinositol 3-kinase ( Pl3-K ) /-Cdc42 dependent pathway has attracted much attention
King et al., FEBS Lett 2001
:
Phosphorylation site specificity of the
Pak mediated regulation of
Raf-1 and cooperativity with Src
Beeser et al., J Biol Chem 2005
:
Inhibition of
Pak reduced the Ser ( 338 ) phosphorylation of
c-Raf in response to both PDGF and EGF ; however, in the case of EGF, the reduction in Ser ( 338 ) phosphorylation was not accompanied by a significant decrease in c-Raf activity
King et al., Nature 1998
:
The protein kinase
Pak3 positively
regulates Raf-1 activity through phosphorylation of serine 338