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.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8445599 | PMC |
| http://dx.doi.org/10.1242/jcs.247171 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Phosphorylation of Lamin A/C regulates the structural integrity of the nuclear envelope.
J Biol Chem
January 2025
MOE Key Laboratory for Cellular Dynamics, Center for Advanced Interdisciplinary Science and Biomedicine of IHM, Hefei National Research Center for Interdisciplinary Sciences at the Microscale, University of Science and Technology of China, Hefei, China; Anhui Key Laboratory of Cellular Dynamics and Chemical Biology, University of Science and Technology of China, Hefei, China. Electronic address:
Article Synopsis
- Dynamic disassembly and reconstruction of the nuclear lamina are crucial for cell division, with CDK1 phosphorylation playing a key role in this process.
- Mass spectrometry identified specific phosphorylation sites on Lamin A/C during mitosis, with mutations altering phosphorylation status affecting lamina structure and function.
- Disruption of Lamin A phosphorylation led to nuclear abnormalities, highlighting its importance for nuclear envelope dynamics and maintaining genomic stability during the cell cycle.
Caveolin-2 controls preadipocyte survival in the mitotic clonal expansion for adipogenesis.
Biochim Biophys Acta Mol Cell Res
October 2024
Division of Life Science, Graduate School of Applied Life Science, PMBBRC, Gyeongsang National University, Jinju 52828, Republic of Korea. Electronic address:
Here, we report that Caveolin-2 (Cav-2) is a cell cycle regulator in the mitotic clonal expansion (MCE) for adipogenesis. For the G2/M phase transition and re-entry into the G1 phase, dephosphorylated Cav-2 by protein tyrosine phosphatase 1B (PTP1B) controlled epigenetic activation of Ccnb1, Cdk1, and p21 in a lamin A/C-dependent manner, thereby ensuring the survival of preadipocytes. Cav-2, associated with lamin A/C, recruited the repressed promoters of Ccnb1 and Cdk1 for activation, and disengaged the active promoter of p21 from lamin A/C for inactivation through histone H3 modifications at the nuclear periphery.
View Article and Find Full Text PDFp300 nucleocytoplasmic shuttling underlies mTORC1 hyperactivation in Hutchinson-Gilford progeria syndrome.
Nat Cell Biol
February 2024
Cambridge Institute for Medical Research, University of Cambridge, Cambridge, UK.
The mechanistic target of rapamycin complex 1 (mTORC1) is a master regulator of cell growth, metabolism and autophagy. Multiple pathways modulate mTORC1 in response to nutrients. Here we describe that nucleus-cytoplasmic shuttling of p300/EP300 regulates mTORC1 activity in response to amino acid or glucose levels.
View Article and Find Full Text PDFFly clock, my clock, and lamin B receptor.
J Genet
January 2024
Centre for DNA Fingerprinting and Diagnostics, Hyderabad,
In the fruit fly , circadian rhythm was disrupted when the inner nuclear membrane protein lamin B receptor (LBR) was depleted from its clock neurons ( 118, e2019756118. 2021; https://doi.org/10.
View Article and Find Full Text PDFIdentification of PP2A-B55 targets uncovers regulation of emerin during nuclear envelope reassembly in .
Open Biol
July 2023
Institute for Research in Immunology and Cancer, Université de Montréal, Montréal, H3T 1J4, Quebec, Canada.
Mitotic exit requires the dephosphorylation of many proteins whose phosphorylation was needed for mitosis. Protein phosphatase 2A with its B55 regulatory subunit (PP2A-B55) promotes this transition. However, the events and substrates that it regulates are incompletely understood.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!