bims-nucpor Biomed News
on Nuclear pore complex and nucleoporins in stress, aging and disease
Issue of 2023–02–19
nine papers selected by
Sara Mingu, Johannes Gutenberg University
  1. Spatial dimension and binding kinetics between FG-repeats characterize the free/bound diffusion of molecules inside the nuclear pore complex.
  2. Single-molecule studies of nuclear transport using biomimetic nuclear pore complexes.
  3. Structure and mechanics of the human nuclear pore complex basket using correlative AFM-fluorescence superresolution microscopy.
  4. Plant nuclear envelope as a hub connecting genome organization with regulation of gene expression.
  5. A nuclear Pandora's box: functions of nuclear envelope proteins in cell division.
  6. Herpesviruses deform membrane during capsid nuclear export by lipid ordering and protein scaffolding.
  7. Nucleocytoplasmic transport determines the biophysical properties in the nucleus.
  8. The role of O-GlcNAcylation in mRNA nuclear export studied by single-molecule super-resolution microscopy.
  9. Uncovering the leukemogenic mechanism of non-canonical NUP98 fusion oncoproteins.
  1. Biophys J. 2023 Feb 10. pii: S0006-3495(22)02838-7. [Epub ahead of print]122(3S1): 346a
    Spatial dimension and binding kinetics between FG-repeats characterize the free/bound diffusion of molecules inside the nuclear pore complex.
    Atsushi Matsuda, Mohammad R K Mofrad.
      
    DOI:  https://doi.org/10.1016/j.bpj.2022.11.1922
  2. Biophys J. 2023 Feb 10. pii: S0006-3495(22)03230-1. [Epub ahead of print]122(3S1): 427a-428a
    Single-molecule studies of nuclear transport using biomimetic nuclear pore complexes.
    Anders Barth, Eva Bertosin, Nils Klughammer, Alejandro M Gonzalez, Eli van der Sluis, Maurice Dekker, Patrick R Onck, Cees Dekker.
      
    DOI:  https://doi.org/10.1016/j.bpj.2022.11.2314
  3. Nanoscale. 2023 Feb 14.
    Structure and mechanics of the human nuclear pore complex basket using correlative AFM-fluorescence superresolution microscopy.
    Anthony Vial, Luca Costa, Patrice Dosset, Pietro Rosso, Gaëlle Boutières, Orestis Faklaris, Heiko Haschke, Pierre-Emmanuel Milhiet, Christine M Doucet.
      Nuclear pore complexes (NPCs) are the only gateways between the nucleus and cytoplasm in eukaryotic cells. They restrict free diffusion to molecules below 5 nm while facilitating the active transport of selected cargoes, sometimes as large as the pore itself. This versatility implies an important pore plasticity. Recently, cryo-EM and AI-based protein modeling of human NPC revealed with acute precision how most constituents are arranged. But the basket, a fish trap-like structure capping the nucleoplasmic side of the pore, remains poorly resolved. Here by atomic force microscopy (AFM) coupled to single molecule localization microscopy (SMLM) we revealed that the basket is very soft and explores a large conformational landscape: apart from its canonical basket shape, it dives into the central pore channel or opens, with filaments reaching to the pore sides. Our observations highlight how this structure can adapt and let morphologically diverse cargoes shuttle through NPCs.
    DOI:  https://doi.org/10.1039/d2nr06034e
  4. Nucleus. 2023 Dec;14(1): 2178201
    Plant nuclear envelope as a hub connecting genome organization with regulation of gene expression.
    Yu Tang.
      Eukaryotic cells organize their genome within the nucleus with a double-layered membrane structure termed the nuclear envelope (NE) as the physical barrier. The NE not only shields the nuclear genome but also spatially separates transcription from translation. Proteins of the NE including nucleoskeleton proteins, inner nuclear membrane proteins, and nuclear pore complexes have been implicated in interacting with underlying genome and chromatin regulators to establish a higher-order chromatin architecture. Here, I summarize recent advances in the knowledge of NE proteins that are involved in chromatin organization, gene regulation, and coordination of transcription and mRNA export. These studies support an emerging view of plant NE as a central hub that contributes to chromatin organization and gene expression in response to various cellular and environmental cues.
    Keywords:  Nuclear envelope; gene expression; genome organization; nuclear lamina; nuclear membrane; nuclear pore complex; plants
    DOI:  https://doi.org/10.1080/19491034.2023.2178201
  5. AoB Plants. 2023 Feb;15(2): plac065
    A nuclear Pandora's box: functions of nuclear envelope proteins in cell division.
    M Arif Ashraf.
      The nucleus is characteristic of eukaryotic cells and nuclear envelope proteins are conserved across the kingdoms. Over the years, the function of these proteins was studied in the intact nuclear envelope. Knowledge regarding the localization and function of nuclear envelope proteins during mitosis, after the nuclear envelope breaks down, is limited. Until recently, the localization of nuclear envelope proteins during mitosis has been observed with the mitotic apparatus. In this context, research in plant cell biology is more advanced compared to non-plant model systems. Although current studies shed light on the localization of nuclear envelope proteins, further experiments are required to determine what, if any, functional role different nuclear envelope proteins play during mitosis. This review will highlight our current knowledge about the role of nuclear envelope proteins and point out the unanswered questions as future direction.
    Keywords:  Cell division; LINC complexes; land plant evolution; mitosis; nuclear envelope proteins; nuclear pore complex
    DOI:  https://doi.org/10.1093/aobpla/plac065
  6. Biophys J. 2023 Feb 10. pii: S0006-3495(22)02633-9. [Epub ahead of print]122(3S1): 305a
    Herpesviruses deform membrane during capsid nuclear export by lipid ordering and protein scaffolding.
    Ekaterina Heldwein.
      
    DOI:  https://doi.org/10.1016/j.bpj.2022.11.1717
  7. Biophys J. 2023 Feb 10. pii: S0006-3495(22)03175-7. [Epub ahead of print]122(3S1): 416a
    Nucleocytoplasmic transport determines the biophysical properties in the nucleus.
    Yi-Shuan Tseng, Liam J Holt.
      
    DOI:  https://doi.org/10.1016/j.bpj.2022.11.2259
  8. Biophys J. 2023 Feb 10. pii: S0006-3495(22)02098-7. [Epub ahead of print]122(3S1): 193a
    The role of O-GlcNAcylation in mRNA nuclear export studied by single-molecule super-resolution microscopy.
    Samuel L Junod, Weidong Yang.
      
    DOI:  https://doi.org/10.1016/j.bpj.2022.11.1182
  9. Biophys J. 2023 Feb 10. pii: S0006-3495(22)03515-9. [Epub ahead of print]122(3S1): 486a
    Uncovering the leukemogenic mechanism of non-canonical NUP98 fusion oncoproteins.
    Brittany J Pioso, Nicole L Michmerhuizen, Swarnendu Tripathi, Toler Freyaldenhoven, Aaron H Phillips, Charles G Mullighan, Richard Kriwacki.
      
    DOI:  https://doi.org/10.1016/j.bpj.2022.11.2599
This page is being maintained by Thomas Krichel. It was last updated on 2024‒11‒22 at 4:25.