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- W2955502414 abstract "SUMOylation is a post-translational modification where SUMO a Small Ubiquitin-like Modifier is covalently bound to a lysine residue by a small set of known enzymes. SUMOylation regulates transcription, cell-cycle progression and DNA repair. Influenza A virus (IAV) replicates in the host cell nucleus and as SUMOs are predominantly located in the cell nucleus, multiple influenza virus proteins become SUMOylated. Results from this project indicate that IAV Matrix Protein 2 (M2) has a SUMO Interaction Motif (SIM) within its cytoplasmic tail at residues 92- 96 which overlaps with a known LC3 interaction region (LIR). These results have implications for protein function and suggest an effect of SUMOylation on M2 interaction with IAV proteins, caspase cleavage of M2 cytoplasmic tail, phosphorylation and affecting the ability of M2 to localise LC3 to the plasma membrane through the LIR within M2 and its subversion of autophagy." @default.
- W2955502414 created "2019-07-12" @default.
- W2955502414 creator A5056781742 @default.
- W2955502414 date "2017-10-01" @default.
- W2955502414 modified "2023-09-27" @default.
- W2955502414 title "SUMO Interaction Motif Of Influenza A Virus Matrix Protein 2" @default.
- W2955502414 hasPublicationYear "2017" @default.
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