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NSP9 of SARS-CoV-2 attenuates nuclear transport by hampering nucleoporin 62 dynamics and functions in host cells.
Makiyama, Kei; Hazawa, Masaharu; Kobayashi, Akiko; Lim, Keesiang; Voon, Dominic C; Wong, Richard W.
  • Makiyama K; Laboratory of Molecular Cell Biology, School of Biological Science and Technology, College of Science and Technology, Kanazawa University, Kanazawa, Ishikawa, Japan.
  • Hazawa M; Laboratory of Molecular Cell Biology, School of Biological Science and Technology, College of Science and Technology, Kanazawa University, Kanazawa, Ishikawa, Japan; Institute for Frontier Science Initiative, Kanazawa University, Kanazawa, Ishikawa, Japan; WPI Nano Life Science Institute, Kanazawa U
  • Kobayashi A; Institute for Frontier Science Initiative, Kanazawa University, Kanazawa, Ishikawa, Japan.
  • Lim K; WPI Nano Life Science Institute, Kanazawa University, Kanazawa, Ishikawa, Japan.
  • Voon DC; Institute for Frontier Science Initiative, Kanazawa University, Kanazawa, Ishikawa, Japan; Cancer Research Institute, Kanazawa University, Ishikawa, Japan.
  • Wong RW; Laboratory of Molecular Cell Biology, School of Biological Science and Technology, College of Science and Technology, Kanazawa University, Kanazawa, Ishikawa, Japan; Institute for Frontier Science Initiative, Kanazawa University, Kanazawa, Ishikawa, Japan; WPI Nano Life Science Institute, Kanazawa U
Biochem Biophys Res Commun ; 586: 137-142, 2022 01 01.
Article in English | MEDLINE | ID: covidwho-1520712
ABSTRACT
Nuclear pore complexes (NPC) regulate molecular traffics on nuclear envelope, which plays crucial roles during cell fate specification and diseases. The viral accessory protein NSP9 of SARS-CoV-2 is reported to interact with nucleoporin 62 (NUP62), a structural component of the NPC, but its biological impact on the host cell remain obscure. Here, we established new cell line models with ectopic NSP9 expression and determined the subcellular destination and biological functions of NSP9. Confocal imaging identified NSP9 to be largely localized in close proximity to the endoplasmic reticulum. In agreement with the subcellular distribution of NSP9, association of NSP9 with NUP62 was observed in cytoplasm. Furthermore, the overexpression of NSP9 correlated with a reduction of NUP62 expression on the nuclear envelope, suggesting that attenuating NUP62 expression might have contributed to defective NPC formation. Importantly, the loss of NUP62 impaired translocation of p65, a subunit of NF-κB, upon TNF-α stimulation. Concordantly, NSP9 over-expression blocked p65 nuclear transport. Taken together, these data shed light on the molecular mechanisms underlying the modulation of host cells during SARS-CoV-2 infection.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Membrane Glycoproteins / RNA-Binding Proteins / Viral Nonstructural Proteins / Nuclear Pore Complex Proteins / Host Microbial Interactions / SARS-CoV-2 / COVID-19 Limits: Humans Language: English Journal: Biochem Biophys Res Commun Year: 2022 Document Type: Article Affiliation country: J.bbrc.2021.11.046

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Membrane Glycoproteins / RNA-Binding Proteins / Viral Nonstructural Proteins / Nuclear Pore Complex Proteins / Host Microbial Interactions / SARS-CoV-2 / COVID-19 Limits: Humans Language: English Journal: Biochem Biophys Res Commun Year: 2022 Document Type: Article Affiliation country: J.bbrc.2021.11.046