Reactome | Depolymerization of the Nuclear Lamina

Depolymerization of the Nuclear Lamina

Stable Identifier

R-HSA-4419969

DOI

10.3180/REACT_200828.1

Type

Pathway

Species

Homo sapiens

ReviewStatus

5/5

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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 Golden, A, Liu, J, Cohen-Fix, O	J. Cell. Sci.	2009
22986494	Mitotic lamin disassembly is triggered by lipid-mediated signaling Mall, M, Walter, T, Gorjánácz, M, Davidson, IF, Nga Ly-Hartig, TB, Ellenberg, J, Mattaj, IW	J. Cell Biol.	2012
8034666	Identification of nuclear beta II protein kinase C as a mitotic lamin kinase Goss, VL, Hocevar, BA, Thompson, LJ, Stratton, CA, Burns, DJ, Fields, AP	J. Biol. Chem.	1994
19494125	Lipin is required for efficient breakdown of the nuclear envelope in Caenorhabditis elegans Gorjánácz, M, Mattaj, IW	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 Hocevar, BA, Burns, DJ, 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 Peter, M, Nakagawa, J, Dorée, M, Labbé, JC, Nigg, EA	Cell	1990
21413788	Homo sapiens dullard protein phosphatase shows a preference for the insulin-dependent phosphorylation site of lipin1 Wu, R, Garland, M, Dunaway-Mariano, D, Allen, KN	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 Han, S, Bahmanyar, S, Zhang, P, Grishin, N, Oegema, K, Crooke, R, Graham, M, Reue, K, Dixon, JE, Goodman, JM	J. Biol. Chem.	2012