CDK1 phosphorylates LPIN

Stable Identifier
Reaction [transition]
Homo sapiens
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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
18694939 Temporal and spatial regulation of the phosphatidate phosphatases lipin 1 and 2

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

J Biol Chem 2008
20876142 A phosphorylation-regulated amphipathic helix controls the membrane translocation and function of the yeast phosphatidate phosphatase

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

Proc. Natl. Acad. Sci. U.S.A. 2010
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

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

J. Biol. Chem. 2011
Participant Of
Catalyst Activity
Catalyst Activity
cyclin-dependent protein serine/threonine kinase activity of CCNB1:p-T161-CDK1 [nucleoplasm]
Physical Entity
Orthologous Events
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