ArticleMolecular biology of the cell2017
VRK2A is an A-type lamin-dependent nuclear envelope kinase that phosphorylates BAF.
Article in Molecular biology of the cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- Structure-based discovery of selective vaccinia-related kinase 1 inhibitors and fluorogenic active-site probes.The Journal of biological chemistry · 2026Article
- Phosphorylation of Barrier-to-Autointegration Factor (BAF) regulates anchoring of centromeric heterochromatin to the nuclear envelope (NE).Nucleic acids research · 2026Article
- Barrier-to-Autointegration Factor 1: a key regulator of nuclear envelope integrity, genome stability, and disease progression.Frontiers in immunology · 2026Review
- A Novel Emerin/Nesprin-3 Interaction Mediates Nuclear Size Changes Induced by Oncogenic KRAS in Pancreatic Cancer Cells.Molecular and cellular biology · 2026Article
- A novel antiviral role of ankyrin repeat and LEM domain-containing 2 (ANKLE2) in restricting vaccinia virus through barrier to autointegration factor (BAF).Journal of virology · 2025Article
- Excess surface area of the nuclear lamina enables unhindered cell migration through constrictions.Science advances · 2025Article
- Nuclear reassembly defects after mitosis trigger apoptotic and p53-dependent safeguard mechanisms in Drosophila.PLoS biology · 2024Article
- Mechanisms by which barrier-to-autointegration factor regulates dynamics of nucleocytoplasmic leakage and membrane repair following nuclear envelope rupture.bioRxiv : the preprint server for biology · 2023Article
- Comparative membrane proteomics reveals diverse cell regulators concentrated at the nuclear envelope.Life science alliance · 2023Article
- Comparative membrane proteomics reveals diverse cell regulators concentrated at the nuclear envelope.bioRxiv : the preprint server for biology · 2023Article
- VRK3 depletion induces cell cycle arrest and metabolic reprogramming of pontine diffuse midline glioma - H3K27 altered cells.Frontiers in oncology · 2023Article
- Nucleoplasmic lamin C rapidly accumulates at sites of nuclear envelope rupture with BAF and cGAS.The Journal of cell biology · 2022Article
- Emerin prevents BAF-mediated aggregation of lamin A on chromosomes in telophase to allow nuclear membrane expansion and nuclear lamina formation.Molecular biology of the cell · 2022Article
- VRK1 Is a Synthetic-Lethal Target in VRK2-Deficient Glioblastoma.Cancer research · 2022Article
- VRK1 as a synthetic lethal target in VRK2 promoter-methylated cancers of the nervous system.JCI insight · 2022Article
- The Nucleus Bypasses Obstacles by Deforming Like a Drop with Surface Tension Mediated by Lamin A/C.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Article
- Dephosphorylation in nuclear reassembly after mitosis.Frontiers in cell and developmental biology · 2022Review
- Mapping the micro-proteome of the nuclear lamina and lamina-associated domains.Life science alliance · 2021Article
- Vaccinia-related kinase 2 blunts sorafenib's efficacy against hepatocellular carcinoma by disturbing the apoptosis-autophagy balance.Oncogene · 2021Article
- Barrier-to-autointegration factor: a first responder for repair of nuclear ruptures.Cell cycle (Georgetown, Tex.) · 2021Review
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Authors and funding
9 authors.
Funding
Abstract
The nuclear envelope (NE) is critical for numerous fundamental cellular functions, and mutations in several NE constituents can lead to a heterogeneous spectrum of diseases. We used proximity biotinylation to uncover new constituents of the inner nuclear membrane (INM) by comparative BioID analysis of lamin A, Sun2 and a minimal INM-targeting motif. These studies identify vaccinia-related kinase-2 (VRK2) as a candidate constituent of the INM. The transmembrane VRK2A isoform is retained at the NE by association with A-type lamins. Furthermore, VRK2A physically interacts with A-type, but not B-type, lamins. Finally, we show that VRK2 phosphorylates barrier to autointegration factor (BAF), a small and highly dynamic chromatin-binding protein, which has roles including NE reassembly, cell cycle, and chromatin organization in cells, and subtly alters its nuclear mobility. Together these findings support the value of using BioID to identify unrecognized constituents of distinct subcellular compartments refractory to biochemical isolation and reveal VRK2A as a transmembrane kinase in the NE that regulates BAF.
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