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Literature summary for 2.7.1.153 extracted from

  • Fukushima, T.; Nedachi, T.; Akizawa, H.; Akahori, M.; Hakuno, F.; Takahashi, S.
    Distinct modes of activation of phosphatidylinositol 3-kinase in response to cyclic adenosine 3',5'-monophosphate or insulin-like growth factor I play different roles in regulation of cyclin D1 and p27Kip1 in FRTL-5 cells (2008), Endocrinology, 149, 3729-3742.
    View publication on PubMed
Search for more literature for 2.7.1.153

Activating Compound

Activating Compound Comment Organism Structure
cAMP 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 Rattus norvegicus
IGF-I 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 Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
LY294002
-
 Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
FRTL-5 cell thyroid follicular cell line Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
 Rattus norvegicus ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
-
 ?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
-
 Rattus norvegicus ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
-
 ?
additional information a p110alpha/beta-subunit binds to a p85 regulatory subunit, and this heterodimer is recruited to the membrane through the association with phosphotyrosyl proteins, leading to production of phosphatidylinositol 3,4,5-triphosphate, PIP3, followed by activation of downstream signal pathway(s) Rattus norvegicus ?
-
 ?

Subunits

Subunits Comment Organism
heterodimer a p110alpha/beta-subunit binds to a p85 regulatory subunit, and this heterodimer is recruited to the membrane through the association with phosphotyrosyl proteins, leading to production of phosphatidylinositol 3,4,5-triphosphate, PIP3, followed by activation of downstream signal pathway(s) Rattus norvegicus

Synonyms

Synonyms Comment Organism
PI 3-kinase
-
 Rattus norvegicus
PI3K
-
 Rattus norvegicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Rattus norvegicus

General Information

General Information Comment Organism
physiological function PI 3-kinase activated in response to cAMP or IGF-I stimulus plays important roles in increasing the translation rate or mRNA levels of cyclin D1, respectively. Activation of PI 3-kinase in response to cAMP or IGF-I are essential for marked increases in G1 CDK activities and DNA synthesis. 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 Rattus norvegicus