IndraLab
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"All together, these data revealed a previously undescribed mechanism by which RNF5 and POH1 mediate the ubiquitin modification of SARS-CoV-2 M for virion trafficking and release.As noted by previous studies, unlike with most enveloped viruses, in which M is necessary and sufficient to mediate VLP release, the E/M proteins of murine hepatitis virus (MHV) or the M/E/N proteins of SARS-CoV are necessary for efficient assembly, trafficking, and VLP release (7–9)."
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"Furthermore, POH1 and Rpn11, a proteasome subunit with deubiquitylation activity, stimulates the formation of IBs by generating free ubiquitin chains in proximity of the aggregated proteins and results in the recruitment of HDAC6, which orchestrates ubiquitin dependent transport of proteins to the aggresome."