Disordered region of nuclear membrane protein Bqt4 recruits phosphatidic acid to the nuclear envelope to maintain its structural integrity.

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  • Additional Information
    • Source:
      Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1083-351X (Electronic) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE
    • Publication Information:
      Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology
      Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology
    • Subject Terms:
      Nuclear Envelope*/metabolism ; Schizosaccharomyces*/metabolism ; Schizosaccharomyces*/genetics ; Schizosaccharomyces pombe Proteins*/metabolism ; Schizosaccharomyces pombe Proteins*/genetics ; Schizosaccharomyces pombe Proteins*/chemistry ; Phosphatidic Acids*/metabolism ; Phosphatidic Acids*/chemistry; Membrane Proteins/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/chemistry ; Intrinsically Disordered Proteins/metabolism ; Intrinsically Disordered Proteins/chemistry ; Intrinsically Disordered Proteins/genetics ; DNA-Binding Proteins ; Nuclear Proteins
    • Abstract:
      The nuclear envelope (NE) is a permeable barrier that maintains nuclear-cytoplasmic compartmentalization and ensures nuclear function; however, it ruptures in various situations such as mechanical stress and mitosis. Although the protein components for sealing a ruptured NE have been identified, the mechanism by which lipid components are involved in this process remains to be elucidated. Here, we found that an inner nuclear membrane (INM) protein Bqt4 directly interacts with phosphatidic acid (PA) and serves as a platform for NE maintenance in the fission yeast Schizosaccharomyces pombe. The intrinsically disordered region (IDR) of Bqt4, proximal to the transmembrane domain, binds to PA and forms a solid aggregate in vitro. Excessive accumulation of Bqt4 IDR in INM results in membrane overproliferation and lipid droplet formation in the nucleus, leading to centromere dissociation from the NE and chromosome missegregation. Our findings suggest that Bqt4 IDR controls nuclear membrane homeostasis by recruiting PA to the INM, thereby maintaining the structural integrity of the NE.
      Competing Interests: Conflict of interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
      (Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved.)
    • Contributed Indexing:
      Keywords: Bqt4; Lem2; electron microscopy; fission yeast Schizosaccharomyces pombe; fluorescence microscopy; intrinsically disordered region; nuclear envelope; nuclear membrane; phosphatidic acid
    • Accession Number:
      0 (Schizosaccharomyces pombe Proteins)
      0 (Phosphatidic Acids)
      0 (Bqt4 protein, S pombe)
      0 (Membrane Proteins)
      0 (Intrinsically Disordered Proteins)
      0 (DNA-Binding Proteins)
      0 (Nuclear Proteins)
    • Publication Date:
      Date Created: 20240602 Date Completed: 20240725 Latest Revision: 20240829
    • Publication Date:
      20240830
    • Accession Number:
      PMC11253665
    • Accession Number:
      10.1016/j.jbc.2024.107430
    • Accession Number:
      38825008