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CYFIP1 — RAC1
Pathways - manually collected, often from reviews:
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
-
IRef Dip Interaction:
Complex of ABI2-RAC1-BRK1-CYFIP1-WASF1-NCKAP1
(pull down)
Ismail et al., Nature structural & molecular biology 2009
-
IRef Dip Interaction:
Complex of RAC1-RAC1-CYFIP1-CYFIP1-NCKAP1-NCKAP1
(pull down)
Ismail et al., Nature structural & molecular biology 2009
-
IRef Dip Interaction:
RAC1
—
CYFIP1
(physical association, pull down)
Chen et al., Nature 2010*
-
IRef Dip Interaction:
RAC1
—
CYFIP1
(physical association, pull down)
Ismail et al., Nature structural & molecular biology 2009
-
IRef Hprd Interaction:
CYFIP1
—
RAC1
(in vivo)
Kobayashi et al., J Biol Chem 1998*
-
IRef Hprd Interaction:
CYFIP1
—
RAC1
(in vitro)
Kobayashi et al., J Biol Chem 1998*
-
IRef Ophid Interaction:
RAC1
—
CYFIP1
(aggregation, interologs mapping)
Brown et al., Bioinformatics 2005
Text-mined interactions from Literome
Miki et al., Biochem Biophys Res Commun 2002
:
Interestingly, the intramolecular interaction is interrupted by the binding of WAVE2 and full-length IRSp53 associates with
Rac in the
presence of
WAVE2
Oikawa et al., Nat Cell Biol 2004
:
Production of PtdIns ( 3,4,5 ) P ( 3 ) at the cell membrane by myristoylated phosphatidylinositol-3-OH kinase ( PI(3)K ) is sufficient to recruit
WAVE2 in the
presence of dominant negative
Rac and latrunculin, demonstrating that PtdIns ( 3,4,5 ) P ( 3 ) alone is able to recruit WAVE2
Suetsugu et al., J Cell Biol 2006
:
Purified
WAVE2 and purified WAVE2 complex were activated by IRSp53 in a
Rac dependent manner with PIP ( 3 ) -containing liposomes ... Therefore, IRSp53 optimizes the activity of the
WAVE2 complex in the
presence of activated
Rac and PIP ( 3 )
Harmon et al., PLoS Pathog 2010
(Astrocytoma...) :
Rac and the tyrosine kinase Abl then
activate the
Wave2 complex and promote Arp2/3 dependent actin polymerization
Kobayashi et al., J Biol Chem 1998
:
These results suggest that
Sra-1 is a novel and specific
target for
Rac1