2.7.1.153: phosphatidylinositol-4,5-bisphosphate 3-kinase
This is an abbreviated version!
For detailed information about phosphatidylinositol-4,5-bisphosphate 3-kinase, go to the full flat file.
Word Map on EC 2.7.1.153
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2.7.1.153
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wortmannin
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pten
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mapks
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mtor
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rapamycin
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endothelial
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erk
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colorectal
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signal-regulated
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subtypes
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insulin-like
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pkc
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tumour
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adenocarcinoma
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phospholipase
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akt1
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insulin-stimulated
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irs-1
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erbb2
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mitogen
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adipocytes
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integrins
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tensin
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insulin-induced
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3-kinases
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dominant-negative
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platelet-derived
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hotspot
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pi3k-akt
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progression-free
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substrate-1
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igf-i
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sh2
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ctnnb1
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tyrosine-phosphorylated
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phosphatidylinositol-3
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pleckstrin
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cdkn2a
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rac1
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pi3k-dependent
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her2-negative
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cetuximab
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phosphatidylinositol-3-kinase
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everolimus
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anti-egfr
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pdgfra
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trastuzumab
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her2-positive
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phospho-akt
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endometrioid
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medicine
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pharmacology
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analysis
- 2.7.1.153
- wortmannin
- pten
- mapks
- mtor
- rapamycin
- endothelial
- erk
- colorectal
-
signal-regulated
- subtypes
-
insulin-like
- pkc
- tumour
- adenocarcinoma
- phospholipase
- akt1
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insulin-stimulated
- irs-1
- erbb2
-
mitogen
- adipocytes
- integrins
-
tensin
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insulin-induced
- 3-kinases
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dominant-negative
-
platelet-derived
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hotspot
-
pi3k-akt
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progression-free
- substrate-1
- igf-i
- sh2
-
ctnnb1
-
tyrosine-phosphorylated
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phosphatidylinositol-3
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pleckstrin
-
cdkn2a
- rac1
-
pi3k-dependent
-
her2-negative
- cetuximab
-
phosphatidylinositol-3-kinase
-
everolimus
-
anti-egfr
-
pdgfra
- trastuzumab
-
her2-positive
-
phospho-akt
-
endometrioid
- medicine
- pharmacology
- analysis
Reaction
Synonyms
class I phosphoinositide 3-kinase, class I PI3K, class IA phosphatidylinositol 3-kinase, class IA phosphatidylinositol-4,5-bisphosphate 3-kinase, CXCR2/phosphatidylinositol 3-kinase gamma, kinase (phosphorylating), phosphatidylinositol 4,5-diphosphate 3-, More, p101-PI3K, p110alpha, p110beta, p110delta, p110delta PI 3-kinase, p110gamma/p101, P120-PI3K, phosphatidyl-inositol-3-kinase, phosphatidylinositol (4,5)-bisphosphate 3-hydroxykinase, phosphatidylinositol 3'-kinase, phosphatidylinositol 3-hydroxyl kinase, phosphatidylinositol 3-kinase alpha, phosphatidylinositol 3-kinase gamma, phosphatidylinositol-4,5-bisphosphate 3-kinase, phosphoinositide 3-kinase, phosphoinositide 3-kinase p110delta, phosphoinositol 3-kinase, PI 3-K, PI 3-kinase, PI-3K, PI3-K, PI3-kinase, PI3K, PI3K p110delta, PI3Kalpha, PI3Kbeta, PI3Kdelta, PI3Kgamma, PI3Kp110delta, PIK3, PIK3CA, Pik3r1, PtdIns(4,5)P2 3-OH kinase, PtdIns-3-kinase p101, PtdIns-3-kinase p110, PtdInsP 3-OH-kinase, type I phosphoinositide 3-kinase
ECTree
2.7.1.153 phosphatidylinositol-4,5-bisphosphate 3-kinaseAdvanced search results
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results (Activating Compound
Activating Compound on EC 2.7.1.153 - phosphatidylinositol-4,5-bisphosphate 3-kinase
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ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
cAMP
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PI 3-kinase is activated in response to cAMP or IGF-I, the PI 3-kinase activity bound to its p85 regulatory subunit increases by 1.7fold. cAMP-dependent PI 3-kinase activation plays an important role in the increase in cyclin D1 translation. In contrast, IGF-I-dependent PI 3-kinase activation is required for the increase in cyclin D1 mRNA levels and degradation of p27Kip1
G-protein beta,gamma
in vivo, activation of enzyme by a mechanism assigning specific roles for both enzyme subunits, membrane recruitment via the noncatalytic p101 subunit, and direct stimulation of p110gamma
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G-protein beta,gamma subunit
purified from bovine brain, 16fold activitation at 0.016 mM
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G-protein beta,gamma subunits
significant stimulation of enzyme beta and gamma isoforms in the presence as well as in the absence of non-catalytic subunits such as p85alpha or p101, stimulation of autophosphorylation of the catalytic subunit of enzyme
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guanosine 5'-3-O-(thio)triphosphate
up to 3fold increase in activity, activation is blocked by high concentrations of guanosine-5-2-O-(thio)diphosphate
IGF-I
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PI 3-kinase is activated in response to cAMP or IGF-I. cAMP-dependent PI 3-kinase activation plays an important role in the increase in cyclin D1 translation. In contrast, IGF-I-dependent PI 3-kinase activation is required for the increase in cyclin D1 mRNA levels and degradation of p27Kip1
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interleukin-13
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treatment of tracheal tissue is associated with an early activation of phosphoinositide 3-kinase
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monocyte chemotactic peptide-1
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i.e. MCP-1, stimulation can be inhibited by pertussis toxin, but not by wortmannin
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Pasteurella multocida toxin
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mediated by G protein betagamma-subunits and G protein alpha-subunit, EC 3.6.5.1
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platelet-derived growth factor
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stimulates synthesis of 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
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RAS-GTP
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regulatory domain p85 interacts with RAS-GTP. RAS binding is essential for oncogenic transformation by helical domain mutants of p110alpha
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thrombin
activation of enzyme in intact cells, blocked by pertussis toxin
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thyroid receptor
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i.e. PV, nongenomic activation of phosphatidylinositol 3-kinase signaling by thyroid hormone receptors, overview. PI3Kactivation through thyroid recptor via proteinprotein interaction, i.e. binding to regulatory subunit p85alpha. The thyroid receptorbeta mutant physically interacts with the regulatory p85alpha subunit of PI3K to activate the downstream AKT-mammalian target of rapamycin and p70S6K and PI3K-integrin-linked kinase-matrix metalloproteinase-2 signaling pathways. PI3K activation results in increased cell proliferation, motility, migration, and metastasis. Nuclear receptor corepressor, NCoR, is a regulator of thyroid receptor-activated PI3K signaling
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influenza A virus NS1 protein
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influenza A virus infection activates the PI3K/Akt pathway by binding influenza A virus NS1 protein to Val573 of the inter-SH2 domain of the p85beta, but not the p85alpha, regulatory subunit of PI3K. NS1-p85-p110 forms a complex in the cells. The interaction is mediated by the interaction interface between the NS1 SH3 binding motif 1, amino acids 164-167, p85beta Val573, and amino acids 137-142 of NS1, molecular modeling and mechanism, overview. Mutant virus PR8-NS1-141/142 is not able to activate Akt phosphorylation
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influenza A virus NS1 protein
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influenza A virus infection activates the PI3K/Akt pathway by binding influenza A virus NS1 protein to Val573 of the inter-SH2 domain of the p85beta, but not the p85alpha, regulatory subunit of PI3K. NS1-p85-p110 forms a complex in the cells. The interaction is mediated by the interaction interface between the NS1 SH3 binding motif 1, amino acids 164-167, p85beta Val573, and amino acids 137-142 of NS1, molecular modeling and mechanism, overview. Mutant virus PR8-NS1-141/142 is not able to activate Akt phosphorylation
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additional information
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the enzyme is activated and associated to E-cadherin complexes, the assembly is mediated by docking proteins, e.g. beta-catenin, gamma-catenin, and Dlg, and involves c-SRC. Cell-cell adhesion induces c-SRC recruitment and E-cadherin complex assembly as well as activity of PI3K, regulatory and molecular mechanism, overview. Interaction of docking proteins via the p85 subunit of PI3K
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additional information
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stimulation of almost every receptor that induces tyrosine kinase activity also leads to class IA phosphatidylinositol-4,5-bisphosphate 3-kinase activation
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additional information
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activated receptor tyrosine kinases recruit the PI3 kinase complex to the membrane via the p85 regulatory subunit either directly or via insulin receptor substrate adapter proteins, activating the catalytic subunit p110
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additional information
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activation of phosphatidylinositol 3-kinase by membrane localization of subunit p110alpha
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additional information
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class IA are activated by cell surface expressed receptor tyrosine kinases, such as growth factors, insulin and cytokines, while class IB are activated by G-protein coupled receptors. The single class 1B catalytic isoform p110gamma binds to either p101 or p84/p87 adaptors, which function to potentiate activation by betagamma-subunits of heterotrimeric GTP-binding proteins which facilitate intracellular signalling from G-protein coupled receptors
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additional information
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the enzyme is activated and associated to E-cadherin complexes, the assembly is mediated by docking proteins, e.g. beta-catenin, gamma-catenin, and Dlg, and involves c-SRC. Cell-cell adhesion induces c-SRC recruitment and E-cadherin complex assembly as well as activity of PI3K, regulatory and molecular mechanism, overview. Interaction of docking proteins via the p85 subunit of PI3K
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additional information
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the PI3K/Akt pathway is directly activated through loss or inactivation of PTEN, a tumor suppressor. Inhibition of mTor has the ability to activate PI3K signaling either by feedback to growth factor receptors, or by promoting the formation of an alternative mTor complex with rictor, that may serve to phosphorylate Akt, seen in both cell models and clinical samples
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additional information
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virulent Legionella pneumophila infection activates PI3K 10fold in vivo, the avirulent bacteria strain Lp-14 activates 4fold in vivo
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additional information
physiological activation of PI3Kalpha is triggered by binding of phosphorylated tyrosine kinase receptors RTK or their accessory proteins, such as the insulin receptor substrate 1, IRS-1, that bridge the interaction between RTK and PI3Kalpha
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additional information
physiological concentrations of cytokine in the picomolar range were sufficient for activating the protein kinase activity of PI3K leading to Ser585 phosphorylation and hemopoietic cell survival but did not activate PI3K lipid kinase signaling or promote proliferation
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additional information
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physiological concentrations of cytokine in the picomolar range were sufficient for activating the protein kinase activity of PI3K leading to Ser585 phosphorylation and hemopoietic cell survival but did not activate PI3K lipid kinase signaling or promote proliferation
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additional information
receptor tyrosine kinases (RTKs) or G protein-coupled receptors (GPCRs) selectively activates PIK3CB/p110beta (but not PIK3CA/p110alpha or PIK3CD/p110delta), leading to production of phosphatidylinositol-3,4,5-triphosphate (PIP3) and subsequent phosphorylation of AKT
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additional information
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activation of phosphatidylinositol 3-kinase by membrane localization of subunit p110alpha
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additional information
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class IA are activated by cell surface expressed receptor tyrosine kinases, such as growth factors, insulin and cytokines, while class IB are activated by G-protein coupled receptors. The single class 1B catalytic isoform p110gamma binds to either p101 or p84/p87 adaptors, which function to potentiate activation by betagamma-subunits of heterotrimeric GTP-binding proteins which facilitate intracellular signalling from G-protein coupled receptors
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additional information
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Rac1 acts upstream of PI3K to activate downstream Akt and finally induce NF-kappaB activation and NO production, overview
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additional information
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the p110gamma isoform of PI3K is activated by G protein-coupled receptors and regulates neutrophil and macrophage chemotaxis
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