FRK phosphorylates PTEN

Stable Identifier
R-HSA-8847977
Type
Reaction [transition]
Species
Homo sapiens
Compartment
cytosol
ReviewStatus
5/5
Locations in the PathwayBrowser
Expand all
General
SVG | 
PNG
Low
Medium
High
 | PPTX  | SBGN
FRK phosphorylates PTEN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
FRK tyrosine kinase (RAK) phosphorylates PTEN on tyrosine residue Y336. FRK-mediated phosphorylation inhibits NEDD4-mediated polyubiquitination and subsequent degradation of PTEN, thus increasing PTEN half-life. FRK-mediated phosphorylation also increases PTEN enzymatic activity (Yim et al. 2009).
Literature References
PubMed ID Title Journal Year
19345329 Rak functions as a tumor suppressor by regulating PTEN protein stability and function

Yim, EK, Peng, G, Dai, H, Hu, R, Li, K, Lu, Y, Mills, GB, Meric-Bernstam, F, Hennessy, BT, Craven, RJ, Lin, SY

Cancer Cell 2009
Participants
Input
Output
Participates
as an event of
Catalyst Activity

protein tyrosine kinase activity of PTEN:p-Y387-FRK [cytosol]

Physical Entity
PTEN:p-Y387-FRK [cytosol] (Homo sapiens)
Activity
protein tyrosine kinase activity (GO:0004713)
Orthologous Events
FRK phosphorylates PTEN (Bos taurus)
FRK phosphorylates PTEN (Caenorhabditis elegans)
FRK phosphorylates PTEN (Canis familiaris)
FRK phosphorylates PTEN (Drosophila melanogaster)
FRK phosphorylates PTEN (Gallus gallus)
FRK phosphorylates PTEN (Mus musculus)
FRK phosphorylates PTEN (Rattus norvegicus)
FRK phosphorylates PTEN (Sus scrofa)
FRK phosphorylates PTEN (Xenopus tropicalis)
Authored
Orlic-Milacic, M  (2015-12-03)
Reviewed
Leslie, N  (2016-09-30)
Kriplani, N  (2016-09-30)
Carracedo, A  (2016-08-11)
Salmena, L  (2016-08-11)
Created
Orlic-Milacic, M  (2015-12-03)
Cite Us!