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PIK3R1 — PLCG1
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 *
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MIPS CORUM LAT-PLC-gamma-1-p85-GRB2-CBL-VAV-SLP-76 signaling complex, C305 activated:
LAT-PLC-gamma-1-p85-GRB2-CBL-VAV-SLP-76 signaling complex, C305 activated complex (CBL-GRB2-LAT-LCP2-PIK3R1-PLCG1-VAV1)
Zhang et al., Cell 1998
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MIPS CORUM PDGFRA-PLC-gamma-1-PI3K-SHP-2 complex, PDGF stimulated:
PDGFRA-PLC-gamma-1-PI3K-SHP-2 complex, PDGF stimulated complex (PDGFRA-PIK3R1-PLCG1-PTPN11)
Bazenet et al., Mol Cell Biol 1996*
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MIPS CORUM LAT-PLC-gamma-1-p85-GRB2-SOS signaling complex, C305 activated:
LAT-PLC-gamma-1-p85-GRB2-SOS signaling complex, C305 activated complex (GRB2-LAT-PIK3R1-PLCG1-SOS1)
Zhang et al., Cell 1998
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IRef Corum Interaction:
Complex of LAT-PLCG1-PIK3R1-GRB2-SOS1
(association, coimmunoprecipitation)
Zhang et al., Cell 1998
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IRef Corum Interaction:
Complex of PDGFRA-PLCG1-PIK3R1-PTPN11
(association, coimmunoprecipitation)
Bazenet et al., Mol Cell Biol 1996*
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IRef Corum Interaction:
Complex of LCP2-GRB2-PIK3R1-CBL-LAT-PLCG1-VAV1
(association, coimmunoprecipitation)
Zhang et al., Cell 1998
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IRef Hprd Interaction:
Complex of 26 proteins
(in vivo)
Zhang et al., Cell 1998
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IRef Intact Interaction:
Complex of 12 proteins
(association, pull down)
Stephanowitz et al., J Proteome Res 2012
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IRef Intact Interaction:
PIK3R1
—
PLCG1
(physical association, pull down)
Emlet et al., J Biol Chem 1997*
Text-mined interactions from Literome
Islam et al., Invest Ophthalmol Vis Sci 2001
:
The data also show that
PLCgamma1 activation and cell proliferation were
inhibited by
PI3K inhibitors, suggesting a role for PI3K in EGF stimulated proliferation of corneal epithelial cells
Piccolo et al., Oncogene 2002
(Breast Neoplasms) :
In an effort to understand the signalling pathway that involves PI 3-K regulation of PLCgamma, we found that EGF induces a
PI 3-K dependent translocation of
PLCgamma1 at the leading edge of migrating cells in a wound healing assay
Wang et al., Traffic 2003
:
We provided original evidence demonstrating that : ( i ) endogenous
phospholipase C-gamma1 , similar to YFP tagged phospholipase C-gamma1, translocated to endosomes following its initial translocation from cytosol to the plasma membrane in response to epidermal growth factor ; ( ii ) phospholipase C-gamma1 remained phosphorylated in endosomes, but phospholipase C-gamma1 activity is not required for its translocation, which suggests a signaling role for phospholipase C-gamma1 in endosomes ; ( iii ) the PH domain was not required for the initial translocation of phospholipase C-gamma1 from cytosol to the plasma membrane, but it stabilizes phospholipase C-gamma1 in the membrane at a later time ; ( iv ) the function of the phospholipase C-gamma1 PH domain in stabilizing phospholipase C-gamma1 membrane association is very important in maintaining the activity of phospholipase C-gamma1 ; and ( v ) the role of the PH domain in phospholipase C-gamma1 membrane association and activation is
dependent on
PI3K activity
Sukumaran et al., J Biol Chem 2003
:
Taken together, these results suggest that E. coli infection of HBMEC induces
PLC-gamma1 activation in a
PI3K dependent manner to increase Ca2+ levels in HBMEC
Xie et al., Mol Biol Cell 2005
:
PI3K inhibitors
blocked calcium activation of
PLC-gamma1 as well as the induction of keratinocyte differentiation markers involucrin and transglutaminase
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
Maffucci et al., PloS one 2009
:
PI3K activity is
required for FGF-2 induced
PLCgamma1 activation and the PI3K/PLCgamma1 pathway is involved in FGF-2 dependent cell migration, determined using Transwell assay, and in FGF-2 induced capillary tube formation ( tubulogenesis assays in vitro ) ... Finally we show that
PI3K dependent
PLCgamma1 activation regulates FGF-2 mediated phosphorylation of Akt at its residue Ser473, determined by Western blotting analysis
Coso et al., PloS one 2012
:
Furthermore, activation of
PI3K/Akt by VEGF-C/VEGFR-3
resulted in phosphorylation of P70S6K, eNOS,
PLC?1 , and Erk1/2