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ESR1 — PAK1
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
-
IRef Biogrid Interaction:
ESR1
—
PAK1
(physical association, affinity chromatography technology)
Rayala et al., Cancer Res 2006*
-
IRef Biogrid Interaction:
ESR1
—
PAK1
(direct interaction, enzymatic study)
Wang et al., EMBO J 2002*
-
IRef Biogrid Interaction:
ESR1
—
PAK1
(physical association, affinity chromatography technology)
Wang et al., EMBO J 2002*
-
IRef Biogrid Interaction:
ESR1
—
PAK1
(direct interaction, pull down)
Wang et al., EMBO J 2002*
-
IRef Hprd Interaction:
PAK1
—
ESR1
(in vivo)
Wang et al., EMBO J 2002*
-
IRef Hprd Interaction:
PAK1
—
ESR1
(in vitro)
Wang et al., EMBO J 2002*
Text-mined interactions from Literome
Wang et al., EMBO J 2002
(Hyperplasia) :
Here, we show that inhibition of
Pak1 kinase activity by a dominant negative fragment or by short interference RNA markedly
reduced the
estrogen receptor-alpha ( ER ) transactivation functions
Holm et al., J Natl Cancer Inst 2006
(Breast Neoplasms) :
Our data support a
role for
Pak1 , particular Pak1 localized to the nucleus, in
ERalpha signaling and in tamoxifen resistance
Zhao et al., Proc Natl Acad Sci U S A 2009
:
To determine whether rapid induction of
PAK phosphorylation by E ( 2 ) is
mediated by nonclassical [ estrogen response element ( ERE ) -independent ]
ERalpha signaling, we used female ERalpha null ( ERalpha ( -/- ) ) mice possessing an ER knock-in mutation ( E207A/G208A ; AA ), in which the mutant ERalpha is incapable of binding DNA and can signal only through membrane initiated or ERE independent genotropic pathways ( ERalpha ( -/AA ) mice )