CDK1 phosphorylates LPIN

Stable Identifier
R-HSA-5195402
Type
Reaction
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
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

Lipins (LPIN1, LPIN2, LPIN3) possess several proline-directed phosphorylation sites that can be phosphorylated by CDK1 (Grimsey et al. 2008), including S106. Serine S106 in lipins is a preferred target for dephosphorylation by the evolutionarilly conserved CTDNEP1:CNEP1R1 complex (ortholog of yeast NEM1:SPO7 complex). Lipin phosphorylation regulates lipin localization, with phosphorylated lipins being soluble and dephosphorylated lipins being membrane-bound. The yeast ortholog of CDK1, CDC28, as well as human CDK1 can phosphorylate yeast lipin PAH1, inducing its dissociation from the nuclear envelope and endoplasmic reticulum membrane (Choi et al. 2011).

Literature References
PubMed ID Title Journal Year
20876142 A phosphorylation-regulated amphipathic helix controls the membrane translocation and function of the yeast phosphatidate phosphatase

Carman, GM, Xu, Z, Siniossoglou, S, Karanasios, E, Han, GS

Proc. Natl. Acad. Sci. U.S.A. 2010
18694939 Temporal and spatial regulation of the phosphatidate phosphatases lipin 1 and 2

O'Hara, L, Rochford, JJ, Carman, GM, Grimsey, N, Siniossoglou, S, Han, GS

J Biol Chem 2008
21081492 Phosphorylation of phosphatidate phosphatase regulates its membrane association and physiological functions in Saccharomyces cerevisiae: identification of SER(602), THR(723), AND SER(744) as the sites phosphorylated by CDC28 (CDK1)-encoded cyclin-dependent kinase

Morgan, JM, Carman, GM, Su, WM, Choi, HS, Xu, Z, Siniossoglou, S, Karanasios, E, Han, GS

J. Biol. Chem. 2011
Participants
Participates
Catalyst Activity

cyclin-dependent protein serine/threonine kinase activity of CCNB1:p-T161-CDK1 [nucleoplasm]

Orthologous Events
Authored
Reviewed
Created
Cite Us!