Overexpression of SARS-CoV-2 protein ORF6 dislocates RAE1 and NUP98 from the nuclear pore complex

By Koki Kato, Dini Kurnia Ikliptikawati, Akiko Kobayashi, H. Kondo, Keesiang Lim, M. Hazawa, R. Wong. 2020

67 citations recorded by the source corpus.

The novel human betacoronavirus SARS-CoV-2 has caused an unprecedented pandemic in the 21st century. Several studies have revealed interactions between SARS-CoV-2 viral proteins and host nucleoporins, yet their functions are largely unknown. Here, we demonstrate that the open-reading frame 6 (ORF6) of SARS-CoV-2 can directly manipulate localization and functions of nucleoporins. We found that ORF6 protein disrupted nuclear rim staining of nucleoporins RAE1 and NUP98. Consequently, this disruption caused aberrant nucleocytoplasmic trafficking and led to nuclear accumulation of mRNA transporters such as hnRNPA1. Ultimately, host cell nucleus size was reduced and cell growth was halted.

Subfields: Animal Science and Zoology, Genetics, Infectious Diseases

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1. Tinghan Li
2. Hangtian Guo
3. Tingting Yang
4. Yibo Wen
5. Haitao Yang
6. X. Ji

Citations in the corpus

• Molecular Mechanism of SARS-CoVs Orf6 Targeting the Rae1–Nup98 Complex to Compete With mRNA Nuclear Export (2022, background): “Several groups have also provided evidence to describe this interaction (Lei et al., 2020; Miorin et al., 2020; Addetia et al., 2021; Kato et al., 2021).”