CDK1 phosphorylates lamins and facilitates depolymerization of lamin filaments

Stable Identifier
Homo sapiens
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Phosphorylation of the N-termini of lamins by CDK1 (serine S23 of lamin B, serin S22 of lamin A and C) probably happens consequentially with phosphorylation of C-termini of lamins by PKC, and contributes to the depolymerization of lamin filaments and solubilization of the nuclear lamina (Ward and Kirschner 1990, Peter et al. 1990, Heald and McKeon 1990, Mall et al. 2012).

Literature References
PubMed ID Title Journal Year
22986494 Mitotic lamin disassembly is triggered by lipid-mediated signaling

Mall, M, Davidson, IF, Walter, T, Ellenberg, J, Nga Ly-Hartig, TB, Mattaj, IW, Gorjánácz, M

J. Cell Biol. 2012
2344612 Mutations of phosphorylation sites in lamin A that prevent nuclear lamina disassembly in mitosis

Heald, R, McKeon, F

Cell 1990
2188731 In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase

Nakagawa, J, Peter, M, Dorée, M, Nigg, EA, Labbé, JC

Cell 1990
2188730 Identification of cell cycle-regulated phosphorylation sites on nuclear lamin C

Ward, GE, Kirschner, MW

Cell 1990
Catalyst Activity

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

Orthologous Events
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