Cargando…
Molecular Mechanism of SARS-CoVs Orf6 Targeting the Rae1–Nup98 Complex to Compete With mRNA Nuclear Export
The accessory protein Orf6 is uniquely expressed in sarbecoviruses including severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) which is an ongoing pandemic. SARS-CoV-2 Orf6 antagonizes host interferon signaling by inhibition of mRNA nuclear export through its interactions with the ribonuc...
Autores principales: | Li, Tinghan, Wen, Yibo, Guo, Hangtian, Yang, Tingting, Yang, Haitao, Ji, Xiaoyun |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8790125/ https://www.ncbi.nlm.nih.gov/pubmed/35096974 http://dx.doi.org/10.3389/fmolb.2021.813248 |
Ejemplares similares
-
SARS-CoV-2 ORF6 Disrupts Bidirectional Nucleocytoplasmic Transport through Interactions with Rae1 and Nup98
por: Addetia, Amin, et al.
Publicado: (2021) -
Overexpression of SARS-CoV-2 protein ORF6 dislocates RAE1 and NUP98 from the nuclear pore complex
por: Kato, Koki, et al.
Publicado: (2021) -
RAE1 Is a Shuttling mRNA Export Factor That Binds to a GLEBS-like NUP98 Motif at the Nuclear Pore Complex through Multiple Domains
por: Pritchard, Colin E.J., et al.
Publicado: (1999) -
Complexes of Vesicular Stomatitis Virus Matrix Protein with Host Rae1 and Nup98 Involved in Inhibition of Host Transcription
por: Rajani, Karishma R., et al.
Publicado: (2012) -
NUP98 and RAE1 sustain progenitor function through HDAC-dependent chromatin targeting to escape from nucleolar localization
por: Neely, Amy E., et al.
Publicado: (2023)