Depolymerization of the Nuclear Lamina

Stable Identifier
Homo sapiens
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The nuclear envelope breakdown in mitotic prophase involves depolymerization of lamin filaments, the main constituents of the nuclear lamina. The nuclear lamina is located at the nuclear face of the inner nuclear membrane and plays and important role in the structure and function of the nuclear envelope (reviewed by Burke and Stewart 2012). Depolymerization of lamin filaments, which consist of lamin homodimers associated through electrostatic interactions in head-to-tail molecular strings, is triggered by phosphorylation of lamins. While CDK1 phosphorylates the N-termini of lamins (Heald and McKeon 1990, Peter et al. 1990, Ward and Kirschner 1990, Mall et al. 2012), PKCs (PRKCA and PRKCB) phosphorylate the C-termini of lamins (Hocevar et al. 1993, Goss et al. 1994, Mall et al. 2012). PKCs are activated by lipid-mediated signaling, where lipins, activated by CTDNEP1:CNEP1R1 serine/threonine protein phosphatase complex, catalyze the formation of DAG (Gorjanacz et al. 2009, Golden et al. 2009, Wu et al. 2011, Han et al. 2012, Mall et al. 2012).
Literature References
PubMed ID Title Journal Year
19494126 Inactivation of the C. elegans lipin homolog leads to ER disorganization and to defects in the breakdown and reassembly of the nuclear envelope

Liu, J, Cohen-Fix, O, Golden, A

J. Cell. Sci. 2009
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
8034666 Identification of nuclear beta II protein kinase C as a mitotic lamin kinase

Thompson, LJ, Burns, DJ, Hocevar, BA, Stratton, CA, Goss, VL, Fields, AP

J. Biol. Chem. 1994
19494125 Lipin is required for efficient breakdown of the nuclear envelope in Caenorhabditis elegans

Mattaj, IW, Gorjánácz, M

J. Cell. Sci. 2009
8463284 Identification of protein kinase C (PKC) phosphorylation sites on human lamin B. Potential role of PKC in nuclear lamina structural dynamics

Burns, DJ, Hocevar, BA, Fields, AP

J. Biol. Chem. 1993
2344612 Mutations of phosphorylation sites in lamin A that prevent nuclear lamina disassembly in mitosis

Heald, R, McKeon, F

Cell 1990
23212477 The nuclear lamins: flexibility in function

Burke, B, Stewart, CL

Nat. Rev. Mol. Cell Biol. 2013
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
21413788 Homo sapiens dullard protein phosphatase shows a preference for the insulin-dependent phosphorylation site of lipin1

Wu, R, Garland, M, Allen, KN, Dunaway-Mariano, D

Biochemistry 2011
2188730 Identification of cell cycle-regulated phosphorylation sites on nuclear lamin C

Ward, GE, Kirschner, MW

Cell 1990
22134922 Nuclear envelope phosphatase 1-regulatory subunit 1 (formerly TMEM188) is the metazoan Spo7p ortholog and functions in the lipin activation pathway

Graham, M, Grishin, N, Han, S, Goodman, JM, Reue, K, Zhang, P, Crooke, R, Bahmanyar, S, Oegema, K, Dixon, JE

J. Biol. Chem. 2012
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