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SUMOylation of RepoMan during late telophase regulates dephosphorylation of lamin A.
Journal of Cell Science ( IF 4 ) Pub Date : 2021-09-09 , DOI: 10.1242/jcs.247171
Takanobu Moriuchi 1 , Fumiko Hirose 1
Affiliation  

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.

中文翻译:

RepoMan 在末期后期的 SUMOylation 调节 lamin A 的去磷酸化。

核纤层蛋白 A 的去磷酸化触发核层重建,对于有丝分裂的完成至关重要。然而,允许及时 lamin A 去磷酸化的特定磷酸酶和调节机制仍不清楚。在这里,我们报告了 RepoMan(也称为 CDCA2),一种蛋白磷酸酶 1γ(PP1γ)的调节亚基,在末期晚期被 K762 的 SUMO-2 瞬时修饰。RepoMan 的 SUMOylation 显着增强了其与 lamin A 的结合亲和力。此外,SUMOylated RepoMan 有助于 lamin A 募集到末期染色体和有丝分裂 lamin A 磷酸化的去磷酸化。与 SUMO 相互作用基序 (SIM) 相互作用有缺陷的 SUMO-2 突变体的表达导致 lamin A 和 RepoMan 关联的失败,随着核纤层蛋白 A 去磷酸化的废除和随后的核层形成。这些发现强烈表明 RepoMan 通过 SUMO-SIM 相互作用招募 lamin A。因此,RepoMan 的瞬时 SUMOylation 在核纤层蛋白 A 去磷酸化的时空调节和随后的有丝分裂末期核层形成中起着重要作用。
更新日期:2021-08-13
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