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).