bims-nucpor Biomed News
on Nuclear pore complex and nucleoporins in stress, aging and disease
Issue of 2023–11–05
two papers selected by
Sara Mingu, Johannes Gutenberg University
  1. Non-classical functions of nuclear pore proteins in ciliopathy.
  2. Retroviral hijacking of host transport pathways for genome nuclear export.
  1. Front Mol Biosci. 2023 ;10 1278976
    Non-classical functions of nuclear pore proteins in ciliopathy.
    Yan Chen, Yuan Zhang, Xiangyu Zhou.
      Nucleoporins (NUPs) constitute integral nuclear pore protein (NPC) elements. Although traditional NUP functions have been extensively researched, evidence of additional vital non-NPC roles, referred to herein as non-classical NUP functions, is also emerging. Several NUPs localise at the ciliary base. Indeed, Nup188, Nup93 or Nup205 knockdown results in cilia loss, impacting cardiac left-right patterning in models and cell lines. Genetic variants of Nup205 and Nup188 have been identified in patients with congenital heart disease and situs inversus totalis or heterotaxy, a prevalent human ciliopathy. These findings link non-classical NUP functions to human diseases. This mini-review summarises pivotal NUP interactions with NIMA-related kinases or nephronophthisis proteins that regulate ciliary function and explores other NUPs potentially implicated in cilia-related disorders. Overall, elucidating the non-classical roles of NUPs will enhance comprehension of ciliopathy aetiology.
    Keywords:  NEK3; Nup188; Nup205; cilia; ciliopathy; left-right patterning; nuclear pore proteins; nucleoporins
    DOI:  https://doi.org/10.3389/fmolb.2023.1278976
  2. mBio. 2023 Nov 01. e0007023
    Retroviral hijacking of host transport pathways for genome nuclear export.
    Ryan T Behrens, Nathan M Sherer.
      Recent advances in the study of virus-cell interactions have improved our understanding of how viruses that replicate their genomes in the nucleus (e.g., retroviruses, hepadnaviruses, herpesviruses, and a subset of RNA viruses) hijack cellular pathways to export these genomes to the cytoplasm where they access virion egress pathways. These findings shed light on novel aspects of viral life cycles relevant to the development of new antiviral strategies and can yield new tractable, virus-based tools for exposing additional secrets of the cell. The goal of this review is to summarize defined and emerging modes of virus-host interactions that drive the transit of viral genomes out of the nucleus across the nuclear envelope barrier, with an emphasis on retroviruses that are most extensively studied. In this context, we prioritize discussion of recent progress in understanding the trafficking and function of the human immunodeficiency virus type 1 Rev protein, exemplifying a relatively refined example of stepwise, cooperativity-driven viral subversion of multi-subunit host transport receptor complexes.
    Keywords:  CRM1; Exportin-1; NXF1; Rev; Rex; human immunodeficiency virus; nuclear envelope; nuclear export; nuclear membrane budding; nuclear pore complex; subcellular trafficking; virus
    DOI:  https://doi.org/10.1128/mbio.00070-23
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