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Interferon-induced global cellular SUMOylation Changes

ABSTRACT: This proteomics dataset was generated to study the changes in SUMO site abundances between control cells and Interferon-alpha treated cells using SILAC. Cells were first fractionated into the cytoplasmic and nuclear fractions. SUMOylated proteins were then purified from these extracts by Ni-NTA via the 6xHIS tag on the SUMO3 construct. The proteins were then digested with trypsin and the peptides desalted on HLB cartridges. The SUMOylated peptides, which harbor an NQTGG remnant after tryptic digestion, were enriched with our anti-NQTGG antibody. The resulting peptides were injected on the orbitrap fusion instrument. The .raw files were analyzed with maxqunt.

INSTRUMENT(S): Orbitrap Fusion ETD

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Mounira K. Chelbi-Alix Pierre Thibault

PROVIDER: MSV000081525 | MassIVE |

SECONDARY ACCESSION(S): PXD007730

REPOSITORIES: MassIVE

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Publications

Promyelocytic Leukemia Protein (PML) Requirement for Interferon-induced Global Cellular SUMOylation.

Maroui Mohamed Ali MA Maarifi Ghizlane G McManus Francis P FP Lamoliatte Frédéric F Thibault Pierre P Chelbi-Alix Mounira K MK

Molecular & cellular proteomics : MCP 20180313 6

We report that interferon (IFN) α treatment at short and long periods increases the global cellular SUMOylation and requires the presence of the SUMO E3 ligase promyelocytic leukemia protein (PML), the organizer of PML nuclear bodies (NBs). Several PML isoforms (PMLI-PMLVII) derived from a single <i>PML</i> gene by alternative splicing, share the same N-terminal region but differ in their C-terminal sequences. Introducing each of the human PML isoform in PML-negative cells revealed that enhanced ...[more]

PMID: 29535160

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