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CRK — PIK3R1
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 Biogrid Interaction:
CRK
—
PIK3R1
(physical association, affinity chromatography technology)
Gelkop et al., J Biol Chem 2001*
-
IRef Biogrid Interaction:
CRK
—
PIK3R1
(physical association, affinity chromatography technology)
Garcia-Guzman et al., Oncogene 2000*
-
IRef Biogrid Interaction:
CRK
—
PIK3R1
(physical association, affinity chromatography technology)
Brehme et al., Proc Natl Acad Sci U S A 2009
-
MIPS CORUM CIN85 complex (CIN85, CRK, BCAR1, CBL, PIK3R1, GRB2, SOS1):
CIN85 complex (CIN85, CRK, BCAR1, CBL, PIK3R1, GRB2, SOS1) complex (BCAR1-CBL-CRK-GRB2-PIK3R1-SH3KBP1-SOS1)
Watanabe et al., Biochem Biophys Res Commun 2000
-
IRef Corum Interaction:
Complex of SH3KBP1-SOS1-PIK3R1-GRB2-CBL-BCAR1-CRK
(association, coimmunoprecipitation)
Watanabe et al., Biochem Biophys Res Commun 2000
-
IRef Hprd Interaction:
CRK
—
PIK3R1
(in vivo)
Lennartsson et al., Exp Cell Res 2003
-
IRef Hprd Interaction:
Complex of 50 proteins
(in vivo)
Watanabe et al., Biochem Biophys Res Commun 2000
-
IRef Intact Interaction:
Complex of 12 proteins
(association, pull down)
Stephanowitz et al., J Proteome Res 2012
-
IRef Intact Interaction:
Complex of 28 proteins
(association, tandem affinity purification)
Brehme et al., Proc Natl Acad Sci U S A 2009
-
IRef Intact Interaction:
Complex of 29 proteins
(association, tandem affinity purification)
Brehme et al., Proc Natl Acad Sci U S A 2009
-
IRef Intact Interaction:
Complex of 17 proteins
(association, anti bait coimmunoprecipitation)
Brehme et al., Proc Natl Acad Sci U S A 2009
-
IRef Intact Interaction:
Complex of 12 proteins
(association, tandem affinity purification)
Brehme et al., Proc Natl Acad Sci U S A 2009
Text-mined interactions from Literome
Take et al., Biochem Biophys Res Commun 2000
:
Our results suggest that
CIN85 may
play a specific role in the
EGF receptor mediated signaling cascade via its interaction with c-Cbl
Petrelli et al., Nature 2002
:
Cbl, in turn, binds and ubiquitinates activated
HGF receptor , and by recruiting the
endophilin-CIN85 complex , it
regulates receptor internalization
Iijima et al., Circulation 2002
:
To elucidate the signaling mechanism underlying the RWP effects, we investigated the effects of RWPs on the activity of
PI3K and the phosphorylation of MAPK pathways in PDGF-BB stimulated SMCs. RWPs
inhibited the PI3K activity and
p38 ( MAPK ) phosphorylation, but not ERK1/2 phosphorylation, in a concentration dependent manner
Kowanetz et al., J Biol Chem 2003
:
Identification of a novel proline-arginine motif involved in
CIN85 dependent clustering of Cbl and down-regulation of
epidermal growth factor receptors
Strassheim et al., J Immunol 2004
(Inflammation) :
Inhibition of
PI3-K also
prevented activation of
p38 mitogen activated protein kinase and extracellular receptor activated kinase 1/2 in TLR2 stimulated neutrophils
Badr et al., J Immunol 2005
(HIV Infections) :
Unlike CXCL12, gp120 did not
induce the activation of phospholipase Cbeta3 and
PI3K downstream from CXCR4, whereas
p38 MAPK activation was observed
Park et al., Toxicol Appl Pharmacol 2006
(Lymphoma) :
In contrast, the enhanced AP-1 DNA binding activities and
p38 MAPK phosphorylation were significantly
suppressed by specific inhibitors for PKC and p38 MAPK, but not by
PI3-K inhibitors
Hagiwara et al., Nephrol Dial Transplant 2006
(Diabetes Mellitus, Type 2...) :
EPA and specific inhibitors of ERK1/2, JNK and
PI3K decreased levels of MCP-1 in MMCs. EPA
suppressed phosphorylation of ERK1/2 and
p38 in MMCs, and decreased p-ERK positive cells in glomeruli of KKAy/Ta mice
Peruzzi et al., J Immunol 2007
(Calcium Signaling) :
We found that
CIN85 overexpression
inhibits the FcepsilonRI induced tyrosine phosphorylation of
phospholipase Cgamma , thus altering calcium mobilization ... Altogether, our findings support a new
role for
CIN85 in regulating
Syk protein levels in RBL-2H3 cells through the activation of the ubiquitin-proteasome pathway and provide a mechanism for this regulation involving c-Cbl ligase activity
Bouchard et al., Apoptosis 2008
:
Hence, beta1 integrin/Fak/Src signaling translates into integrated mediating functions of
p38beta activation and
regulation of Bcl-2 homologs by
PI3-K/Akt-1 and MEK/Erk, consequently determining their requirement ( or not ) for survival
Wadhone et al., J Immunol 2009
(Leishmaniasis, Visceral) :
Miltefosine induced protein kinase C-dependent and
PI3K dependent
p38MAP kinase phosphorylation and anti-leishmanial function
Wakasaki et al., Neoplasia (New York, N.Y.) 2010
(Carcinoma, Squamous Cell...) :
Little is known, however, about a
role of
CIN85 in
EGFR signaling as well as its relevance to tumor development and progression of HNSCC
Bros et al., Gene 2011
:
Both Cacnb3 isoforms, similar to Fscn1, required JNK and
p38 kinase activity for stimulation associated upregulation, and this process was
inhibited by ERK and
PI(3)K
Marois et al., J Biol Chem 2011
:
Silencing the expression of
CIN85 by siRNA in dibutyryl cyclic AMP differentiated PLB 985 cells
prevented Fc?RIIa degradation and increased IgG mediated phagocytosis
Wang et al., J Cell Mol Med 2012
(Carcinoma, Hepatocellular...) :
Tumour necrosis factor-a (TNF-a) significantly induced phosphorylation of p38 MAPK, ERK, Akt and production of IL-8 from HCC cells, which were prevented by SB203580 (
p38 MAPK inhibitor ), PD98059 ( ERK inhibitor ), LY294002 and Wortmannin (
PI3K inhibitor ) and SB328437 ( CCR3 inhibitor )
Tossidou et al., Mol Cell Biol 2012
:
Our results indicate a novel
role for
CD2AP in regulating posttranslational modification of
CIN85
Yang et al., Biosci Rep 2012
(Insulin Resistance) :
In contrast, saturated fatty acid exposure caused insulin resistance, reducing
PI3K ( phosphoinositide 3-kinase ) and ERK ( extracellular-signal regulated kinase )
activation while increasing activation of stress kinases JNK ( c-Jun N-terminal kinase ) and
p38
Samoylenko et al., Carcinogenesis 2012
(Adenocarcinoma...) :
Thereby, Ruk ( l )
/CIN85 led to a more rapid and prolonged epidermal growth factor dependent activation of
Src , Akt and ERK1/2 and treatment with the Src inhibitor PP2 and the PI3K inhibitor LY294002 abolished the Ruk ( l ) /CIN85 dependent changes in cell motility ... Thereby, Ruk ( l )
/CIN85 led to a more rapid and prolonged epidermal growth factor dependent activation of Src, Akt and
ERK1/2 and treatment with the Src inhibitor PP2 and the PI3K inhibitor LY294002 abolished the Ruk ( l ) /CIN85 dependent changes in cell motility ... Thereby, Ruk ( l )
/CIN85 led to a more rapid and prolonged epidermal growth factor dependent activation of Src,
Akt and ERK1/2 and treatment with the Src inhibitor PP2 and the PI3K inhibitor LY294002 abolished the Ruk ( l ) /CIN85 dependent changes in cell motility
Schroeder et al., Mol Biol Cell 2012
:
In this study we show that
EGFR activation
leads to a pronounced src mediated tyrosine phosphorylation of
CIN85 that subsequently influences EGFR ubiquitination
Bior et al., FEBS Lett 2013
:
Dab1 stabilizes its interaction with
Cin85 by suppressing Cin85 phosphorylation at serine 587 ... Furthermore a
Cin85 Ser587 phosphomimetic
disrupts the
Dab1-Cin85 complex without affecting the Cin85-CapZ complex
Fuchigami et al., Genes Cells 2013
:
We reported previously that
Cdk5-p35 phosphorylates Dab1 at Ser400 and Ser491 and the phosphorylation
regulates its binding to
CIN85 , which is an SH3 containing multiadaptor protein involved in endocytic downregulation of receptor-tyrosine kinases ... We reported previously that
Cdk5-p35 phosphorylates Dab1 at Ser400 and Ser491 and the phosphorylation
regulates its binding to
CIN85 , which is an SH3 containing multiadaptor protein involved in endocytic downregulation of receptor-tyrosine kinases ... We reported previously that Cdk5-p35 phosphorylates
Dab1 at Ser400 and Ser491 and the phosphorylation
regulates its binding to
CIN85 , which is an SH3 containing multiadaptor protein involved in endocytic downregulation of receptor-tyrosine kinases