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CBFA2T2 — PIK3R1
Text-mined interactions from Literome
Gentili et al., Biochim Biophys Acta 2003
:
Intracellular Ca ( 2+ ) chelation ( BAPTA-AM, 5 microM ) affected the tyrosine phosphorylation of
p85alpha and
inhibited PTH dependent
PI3K activation by 75 % in young rats and completely abolished the enzyme activity in aged animals, demonstrating that Ca ( 2+ ) is required for full activation of PI3K in enterocytes stimulated with PTH
Isenovic et al., Metabolism 2003
:
Exposure to IGF-1 for 30 minutes or E2 for 20 minutes increased insulin receptor substrate-1 (IRS-1) association with the regulatory (
p85 ) subunit of PI3K, enhanced tyrosine phosphorylation of p85, and
increased PI3K activity
Luo et al., Cell cycle (Georgetown, Tex.) 2005
(Neoplasms) :
Here we discuss some recent studies identifying the mechanisms by which
p85 , the regulatory subunit of PI3K, negatively
regulates PI3K signaling
Komori et al., Clinical calcium 2006
:
Phosphoinositide 3-kinase
(PI3K)-Akt signaling enhances DNA binding of Runx2 and Runx2 dependent transcription, and Runx2
upregulates PI3K subunits (
p85 and p110 beta ) and Akt
Bousquet et al., EMBO J 2006
(Neoplasms, Experimental) :
Mutating sst2-Y71 disabled sst2 to interact with
p85 and somatostatin to
inhibit PI3K , consequently abrogating sst2 's ability to suppress cell survival and tumor growth
Geering et al., Proc Natl Acad Sci U S A 2007
:
These results argue against a
role of free
p85 in
PI3K signaling and provide insights into the nonredundant functions of the different class IA PI3K isoforms
Zhao et al., J Cell Biochem 2008
(Calcium Signaling...) :
Our results showed that YSL decreased the mRNA level and protein expression of CaM,
inhibited the activity of
PI3K , and reduced the mRNA level and protein expression of the PI3K regulatory subunit
p85 and mRNA level of PI3K catalytic subunits p110alpha and p110gamma
Beauséjour et al., Apoptosis 2012
:
We report that : ( 1 ) the predominant
PI3-K complexes expressed by HIEC cells are p110a/p85ß and p110a/p55? ; ( 2 ) the inhibition and/or siRNA mediated expression silencing of p110a, but not that of p110ß, ? or d, results in Akt-1 down-activation and consequent apoptosis ; ( 3 ) the expression silencing of
p85ß or p55?, but not that of p85a, likewise
induces Akt-1 down-activation and apoptosis ; however, the impact of a loss of p55? on both Akt-1 activation and cell survival is significantly greater than that from the loss of p85ß ; and ( 4 ) both the p110a/p85ß and p110a/p55? complexes are engaged by ß1 integrin/Fak/Src signaling ; however, the engagement of p110a/p85ß is primarily Src dependent, whereas that of p110a/p55? is primarily Fak dependent ( but Src independent )
Yin et al., Nature 1998
:
We report here that the protein
p85 , a regulator of the signalling protein phosphatidyl-3-OH kinase ( PI(3)K ), participates in the cell death process that is induced in response to oxidative stress and that this role of p85 in apoptosis does not
involve PI(3)K