PMC:7321036 / 20958-22117 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7321036","sourcedb":"PMC","sourceid":"7321036","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7321036","text":"The SARS-CoV-2 N protein is known to interact with several RNA-processing proteins that are differentially phosphorylated during infection, including LARP1 and RRP9. Here LARP1 phosphorylation decreases on several sites, which is known to consequently increase LARP1 affinity for 3′ untranslated regions (UTRs) of mRNAs encoding ribosomal proteins, driving inhibition of protein synthesis (Hong et al., 2017). This mechanism may be utilized by SARS-CoV-2 to prioritize synthesis of viral proteins over host proteins. In addition, ORF6 interacts with the NUP98/RAE complex, and NUP98 phosphorylation was observed to increase at S888, a site within its peptidase domain. NUP98 autocatalytic cleavage is required for localization to the nuclear pore; thus, it is possible that NUP98 interaction with ORF6 and/or its virus-induced phosphorylation prevents host mRNA export through the nuclear pore (Krull et al., 2010; Hodel et al., 2002). A similar mechanism is employed by vesicular stomatitis virus (VSV) matrix protein to block host mRNA export by targeting the NUP98/RAE complex, leading to exclusive translation of cytoplasmic VSV mRNAs (Quan et al., 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