SUMOylation of RepoMan during late telophase regulates dephosphorylation of lamin A

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 1. (PP1.) 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 themitotic 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.

Automated summary

RepoMan, a regulatory subunit of protein phosphatase 1 (PP1), is transiently modified with SUMO-2 during late telophase, which enhances its binding affinity with lamin A and contributes to the recruitment and dephosphorylation of lamin A. Transient SUMOylation of RepoMan plays a crucial role in the spatiotemporal regulation of lamin A dephosphorylation and subsequent nuclear lamina formation at the end of mitosis.