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SUMO Interaction Motif Of Influenza A Virus Matrix Protein 2

Jackson, Frederic St John Shore (2017) SUMO Interaction Motif Of Influenza A Virus Matrix Protein 2. Master of Science by Research (MScRes) thesis, University of Kent,. (Access to this publication is currently restricted. You may be able to access a copy if URLs are provided) (KAR id:63933)

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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.

Item Type: Thesis (Master of Science by Research (MScRes))
Thesis advisor: Rossman, Jeremy S.
Uncontrolled keywords: Influenza, SUMOylation, M2
Divisions: Faculties > Sciences > School of Biosciences
SWORD Depositor: System Moodle
Depositing User: System Moodle
Date Deposited: 10 Oct 2017 14:10 UTC
Last Modified: 29 May 2019 19:40 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/63933 (The current URI for this page, for reference purposes)
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