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Literature summary for 2.7.11.1 extracted from

  • Kanan, Y.; Matsumoto, H.; Song, H.; Sokolov, M.; Anderson, R.; Rajala, R.
    Serine/threonine kinase Akt activation regulates the activity of retinal serine/threonine phosphatases, PHLPP and PHLPPL (2010), J. Neurochem., 113, 477-488.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
Insulin
-
Rattus norvegicus

Cloned(Commentary)

Cloned (Comment) Organism
PH domain of Akt-1 isoform Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
photoreceptor inner segment mainly Rattus norvegicus 1917
-
photoreceptor outer segment membrane rod photoreceptors express all three Akt isoforms Rattus norvegicus 42622
-

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein Akt is activated by phosphorylation at Ser473, inhibition of basal level of Akt phosphorylation in phosphoinositide 3-kinase inhibitor-treated ex vivo cultures. PHLPP selectively dephosphorylates Akt2 and Akt3 and PHLPPL selectively dephosphorylates Akt1 and Akt3 Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
eye
-
Rattus norvegicus
-
retina
-
Rattus norvegicus
-

Synonyms

Synonyms Comment Organism
AKT
-
Rattus norvegicus
AKT1
-
Rattus norvegicus
AKT2
-
Rattus norvegicus
Akt3
-
Rattus norvegicus
serine/threonine protein kinase B
-
Rattus norvegicus

General Information

General Information Comment Organism
malfunction inhibition of Akt activity results in the significant activation of PHLPP activity compared to insulin-treated conditions. Knocking down Akt1 does not affect photoreceptors during light stress Rattus norvegicus
physiological function Akt is an important kinase that is activated by a variety of growth factors and insulin. The insulin receptor-activated phosphoinositide 3-kinase/Akt pathway and serine/threonine kinase Akt activation controls the activity of retinal serine/threonine phosphatases, PHLPP and PHLPPL, which themselves regulate the dephosphorylation of Akt isoforms, location of PHLPPL in rod photoreceptors and absence of PHLPP from rods. PHLPPL activity is regulated by all three Akt isoforms Rattus norvegicus