Vesiculoviral matrix (M) protein occupies nucleic acid binding site at nucleoporin pair (Rae1•Nup98)

By Beili Quan, H. Seo, Günter Blobel, Yi Ren. 2014

67 citations recorded by the source corpus.

Subfields: Epidemiology, Genetics, Infectious Diseases

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In Epidemiology

1. Ren Sun
2. M. Gale

In Genetics

1. Ren Sun
2. T. Rana

Citations in the corpus

• A herpesvirus protein selectively inhibits cellular mRNA nuclear export (2016, background): “A previous structure study of VSV M-Rae1Nup98 has suggested that M protein mimics phosphate backbone of nucleic acid to compete for nucleic acid binding to Rae1 (Quan et al., 2014).”
• SARS-CoV-2 ORF6 disrupts nucleocytoplasmic transport through interactions with Rae1 and Nup98 (2020, background): “Similar to VSV M and KSHV ORF10, SARS-CoV-2 ORF6 contains a methionine in its C-terminus that is surrounded by acidic residues, which may facilitate an interaction with the nucleic binding site of the Rae1•Nup98 complex (13).”
• SARS-CoV-2 ORF6 Disrupts Bidirectional Nucleocytoplasmic Transport through Interactions with Rae1 and Nup98 (2021, background): “The methionine residue in the Rae1-Nup98 interacting motif of VSV M forms multiple intermolecular interactions with amino acid residues in the nucleic acid binding site of Rae1 and facilitates the interaction between VSV M and the Rae1·Nup98 complex (8).”
• Overexpression of SARS-CoV-2 protein ORF6 dislocates RAE1 and NUP98 from the nuclear pore complex (2020, unknown): “Unsurprisingly, VSV promotes Abbreviations COVID-19 Corona Virus Disease 2019 hnRNPA1 Heterogeneous nuclear ribonucleoprotein A1 NUP98 Nucleoporin 98 ORF6 Open-reading frame 6 RAE1 RNA export factor 1 SARS-CoV-2 Severe Acute Respiratory Syndrome Corona Virus 2 heterogeneous ribonucleoprotein A1 (hnR”
• Molecular Mechanism of SARS-CoVs Orf6 Targeting the Rae1–Nup98 Complex to Compete With mRNA Nuclear Export (2022, background): “It has been reported that some viruses from unrelated species, such as vesicular stomatitis virus (VSV) and Kaposi’s sarcoma-associated herpesvirus (KSHV), can target the Rae1–Nup98 complex and suppress the host immune response (Quan et al., 2014; Feng et al., 2020).”