Projects per year
Abstract
Dynamic nuclear SUMO modifications play essential roles in orchestrating cellular responses to proteotoxic stress, DNA damage, and DNA virus infection. Here, we describe a non-canonical host SUMOylation response to the nuclear-replicating RNA pathogen, influenza virus, and identify viral RNA polymerase activity as a major contributor to SUMO proteome remodeling. Using quantitative proteomics to compare stress-induced SUMOylation responses, we reveal that influenza virus infection triggers unique re-targeting of SUMO to 63 host proteins involved in transcription, mRNA processing, RNA quality control, and DNA damage repair. This is paralleled by widespread host deSUMOylation. Depletion screening identified ten virus-induced SUMO targets as potential antiviral factors, including C18orf25 and the SMC5/6 and PAF1 complexes. Mechanistic studies further uncovered a role for SUMOylation of the PAF1 complex component, parafibromin (CDC73), in potentiating antiviral gene expression. Our global characterization of influenza virus-triggered SUMO redistribution provides a proteomic resource to understand host nuclear SUMOylation responses to infection.
Original language | English |
---|---|
Pages (from-to) | 1467-1480 |
Number of pages | 14 |
Journal | Cell Reports |
Volume | 13 |
Issue number | 7 |
Early online date | 5 Nov 2015 |
DOIs | |
Publication status | Published - 17 Nov 2015 |
ASJC Scopus subject areas
- General Biochemistry,Genetics and Molecular Biology
Fingerprint
Dive into the research topics of 'Global Reprogramming of Host SUMOylation during Influenza Virus Infection'. Together they form a unique fingerprint.Projects
- 1 Finished
-
Determining the Role and Mechanism of Action of SUMO Targeted Ubiquitin Ligase RNF4 in Maintaining Genome Integrity (Senior Investigator Award)
Hay, R. (Investigator)
1/10/12 → 31/01/20
Project: Research