Inhibition of PP2A activity by phosphorylation of the catalytic subunit at tyrosine Y307

Stable Identifier
R-HSA-8857925
Type
Reaction [transition]
Species
Homo sapiens
Compartment
cytosol, plasma membrane
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Inhibition of PP2A activity by phosphorylation of the catalytic subunit at tyrosine Y307
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SRC family tyrosine kinases, such as SRC and LCK, as well as receptor tyrosine kinases, such as EGFR and insulin receptor, can phosphorylate the catalytic subunit of serine/threonine protein phosphatase PP2A at tyrosine residue Y307. Phosphorylation at Y307 inhibits the catalytic activity of PP2A. Phosphatidylinositol-5-phosphate (PI5P) positively regulates phosphorylation of the catalytic subunit of PP2A at Y307.

Literature References
PubMed ID Title Journal Year
19576174 PtdIns5P protects Akt from dephosphorylation through PP2A inhibition

Ramel, D, Lagarrigue, F, Dupuis-Coronas, S, Chicanne, G, Leslie, N, Gaits-Iacovoni, F, Payrastre, B, Tronchère, H

Biochem. Biophys. Res. Commun. 2009
1325671 Regulation of protein serine-threonine phosphatase type-2A by tyrosine phosphorylation

Chen, J, Martin, BL, Brautigan, DL

Science 1992
Participants
Input
Output
Participant Of
hasEvent
Catalyst Activity
Catalyst Activity
Title
protein tyrosine kinase activity of Activated SRC,LCK,EGFR,INSR [plasma membrane]
Physical Entity
Activated SRC,LCK,EGFR,INSR [plasma membrane]
Activity
protein tyrosine kinase activity (0004713)
This event is regulated
Positively by
Orthologous Events
Inhibition of PP2A activity by phosphorylation of the catalytic subunit at tyrosine Y307 (Caenorhabditis elegans)
Inhibition of PP2A activity by phosphorylation of the catalytic subunit at tyrosine Y307 (Danio rerio)
Inhibition of PP2A activity by phosphorylation of the catalytic subunit at tyrosine Y307 (Mus musculus)
Inhibition of PP2A activity by phosphorylation of the catalytic subunit at tyrosine Y307 (Rattus norvegicus)
Inhibition of PP2A activity by phosphorylation of the catalytic subunit at tyrosine Y307 (Xenopus tropicalis)
Authored
Orlic-Milacic, M  (2016-02-17)
Reviewed
Porteu, F  (2016-02-08)
Created
Orlic-Milacic, M  (2016-02-17)
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