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SUMOylation of RepoMan During Late Telophase Regulates Dephosphorylation of Lamin A

Overview
Journal J Cell Sci
Specialty Cell Biology
Date 2021 Aug 13
PMID 34387316
Citations 5
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Abstract

Dephosphorylation of lamin A, which triggers nuclear lamina reconstitution, is crucial for the completion of mitosis. However, the specific phosphatase and regulatory mechanism that allow timely lamin A dephosphorylation remain unclear. Here, we report that RepoMan (also known as CDCA2), a regulatory subunit of protein phosphatase 1γ (PP1γ) is transiently modified with SUMO-2 at K762 during late telophase. SUMOylation of RepoMan markedly enhanced its binding affinity with lamin A. Moreover, SUMOylated RepoMan contributes to lamin A recruitment to telophase chromosomes and dephosphorylation of the mitotic lamin A phosphorylation. Expression of a SUMO-2 mutant that has a defective interaction with the SUMO-interacting motif (SIM) resulted in failure of the lamin A and RepoMan association, along with abrogation of lamin A dephosphorylation and subsequent nuclear lamina formation. These findings strongly suggest that RepoMan recruits lamin A through SUMO-SIM interaction. Thus, transient SUMOylation of RepoMan plays an important role in the spatiotemporal regulation of lamin A dephosphorylation and the subsequent nuclear lamina formation at the end of mitosis.

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References
1.
Zhang X, Goeres J, Zhang H, Yen T, Porter A, Matunis M . SUMO-2/3 modification and binding regulate the association of CENP-E with kinetochores and progression through mitosis. Mol Cell. 2008; 29(6):729-41. PMC: 2366111. DOI: 10.1016/j.molcel.2008.01.013. View

2.
Goss V, Hocevar B, Thompson L, Stratton C, Burns D, Fields A . Identification of nuclear beta II protein kinase C as a mitotic lamin kinase. J Biol Chem. 1994; 269(29):19074-80. View

3.
Foss K, Robeson A, Kornbluth S, Zhang L . Mitotic phosphatase activity is required for MCC maintenance during the spindle checkpoint. Cell Cycle. 2015; 15(2):225-33. PMC: 4825922. DOI: 10.1080/15384101.2015.1121331. View

4.
Qian J, Lesage B, Beullens M, Van Eynde A, Bollen M . PP1/Repo-man dephosphorylates mitotic histone H3 at T3 and regulates chromosomal aurora B targeting. Curr Biol. 2011; 21(9):766-73. DOI: 10.1016/j.cub.2011.03.047. View

5.
Andres V, Gonzalez J . Role of A-type lamins in signaling, transcription, and chromatin organization. J Cell Biol. 2009; 187(7):945-57. PMC: 2806284. DOI: 10.1083/jcb.200904124. View