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- W4386738535 endingPage "e1011619" @default.
- W4386738535 startingPage "e1011619" @default.
- W4386738535 abstract "The host cell membrane-associated RING-CH 8 protein (MARCH8), a member of the E3 ubiquitin ligase family, regulates intracellular turnover of many transmembrane proteins and shows potent antiviral activities. Generally, 2 antiviral modes are performed by MARCH8. On the one hand, MARCH8 catalyzes viral envelope glycoproteins (VEGs) ubiquitination and thus leads to their intracellular degradation, which is the cytoplasmic tail (CT)-dependent (CTD) mode. On the other hand, MARCH8 traps VEGs at some intracellular compartments (such as the trans -Golgi network, TGN) but without inducing their degradation, which is the cytoplasmic tail-independent (CTI) mode, by which MARCH8 hijacks furin, a cellular proprotein convertase, to block VEGs cleavage. In addition, the MARCH8 C-terminal tyrosine-based motif (TBM) 222 YxxL 225 also plays a key role in its CTI antiviral effects. In contrast to its antiviral potency, MARCH8 is occasionally hijacked by some viruses and bacteria to enhance their invasion, indicating a duplex role of MARCH8 in host pathogenic infections. This review summarizes MARCH8’s antiviral roles and how viruses evade its restriction, shedding light on novel antiviral therapeutic avenues." @default.
- W4386738535 created "2023-09-15" @default.
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- W4386738535 date "2023-09-14" @default.
- W4386738535 modified "2023-09-29" @default.
- W4386738535 title "The emerging roles of MARCH8 in viral infections: A double-edged Sword" @default.
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- W4386738535 doi "https://doi.org/10.1371/journal.ppat.1011619" @default.
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- W4386738535 hasPublicationYear "2023" @default.
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