ArticleThe Journal of biological chemistry2010
Requirement for lamin B receptor and its regulation by importin {beta} and phosphorylation in nuclear envelope assembly during mitotic exit.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 39 citations in OpenAlex.
- Nuclear Pore Complexes in Various States of HL-60/S4 Cells.bioRxiv : the preprint server for biology · 2026Article
- Setting Up to Divide: Nuclear Mechanotransduction in the Regulation of Mitosis.Results and problems in cell differentiation · 2026Review
- cTAGE5/MEA6 Regulates LBR Localization to Maintain Nuclear Envelope Integrity and Safeguard Against Aging.Aging cell · 2025Article
- Reconstitution of nuclear envelope subdomain formation on mitotic chromosomes in semi-intact cells.Cell structure and function · 2024Article
- Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023Review
- Dephosphorylation in nuclear reassembly after mitosis.Frontiers in cell and developmental biology · 2022Review
- Inhibition of NUPR1-Karyopherin β1 Binding Increases Anticancer Drug Sensitivity.International journal of molecular sciences · 2021Article
- Postmitotic annulate lamellae assembly contributes to nuclear envelope reconstitution in daughter cells.The Journal of biological chemistry · 2019Article
- Article
- KPNB1 inhibition disrupts proteostasis and triggers unfolded protein response-mediated apoptosis in glioblastoma cells.Oncogene · 2018Article
- Review
- Article
- ELYS regulates the localization of LBR by modulating its phosphorylation state.Journal of cell science · 2016Article
- Cooperative Activity of GABP with PU.1 or C/EBPε Regulates Lamin B Receptor Gene Expression, Implicating Their Roles in Granulocyte Nuclear Maturation.Journal of immunology (Baltimore, Md. : 1950) · 2016Article
- Xenopus LAP2β protein knockdown affects location of lamin B and nucleoporins and has effect on assembly of cell nucleus and cell viability.Protoplasma · 2016Article
- Nuclear transport factors: global regulation of mitosis.Current opinion in cell biology · 2015Review
- Building a nuclear envelope at the end of mitosis: coordinating membrane reorganization, nuclear pore complex assembly, and chromatin de-condensation.Chromosoma · 2012Review
- Chromatin-bound NLS proteins recruit membrane vesicles and nucleoporins for nuclear envelope assembly via importin-α/β.Cell research · 2012Article
- The nucleoporin ELYS/Mel28 regulates nuclear envelope subdomain formation in HeLa cells.Nucleus (Austin, Tex.) · 2012Article
- Temporal control of nuclear envelope assembly by phosphorylation of lamin B receptor.Molecular biology of the cell · 2011Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lamin B receptor (LBR), a chromatin and lamin B-binding protein in the inner nuclear membrane, has been proposed to target the membrane precursor vesicles to chromatin mediated by importin β during the nuclear envelope (NE) assembly. However, the mechanisms for the binding of LBR with importin β and the membrane targeting by LBR in NE assembly remain largely unknown. In this report, we show that the amino acids (aa) 69-90 of LBR sequences are required to bind with importin β at aa 45-462, and the binding is essential for the NE membrane precursor vesicle targeting to the chromatin during the NE assembly at the end of mitosis. We also show that this binding is cell cycle-regulated and dependent on the phosphorylation of LBR Ser-71 by p34(cdc2) kinase. RNAi knockdown of LBR causes the NE assembly failure and abnormal chromatin decondensation of the daughter cell nuclei, leading to the daughter cell death at early G(1) phase by apoptosis. Perturbation of the interaction of LBR with importin β by deleting the LBR N-terminal spanning region or aa 69-73 also induces the NE assembly failure, the abnormal chromatin decondensation, and the daughter cell death. The first transmembrane domain of LBR promotes the NE production and expansion, because overexpressing this domain is sufficient to induce membrane overproduction of the NE. Thus, these results demonstrate that LBR targets the membrane precursor vesicles to chromatin by interacting with importin β in a LBR phosphorylation-dependent manner during the NE assembly at the end of mitosis and that the first transmembrane domain of LBR promotes the LBR-bearing membrane production and the NE expansion in interphase.
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