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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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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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The SUMO protease SENP6 regulates the constitutive centromere-associated network by group

Project description:Project 1: Identification of SUMOylated proteins which are regulated by the SUMO protease SENP6. SENP6 knockdown was performed by two independent shRNAs and SUMOylated proteins were purified from U2OS expressing His10-tagged SUMO2 by means of Ni-NTA pulldown. Purified SUMOylated proteins were identified and quantified by label-free quantification. Project 2: Dynamics of chromatin-associated proteins influenced by SENP6. After siRNA-mediated knockdown of SENP6, chromatin fractions of U2OS cells were isolated and abundances of proteins were quantified. Project 3: Analysis of in vitro SUMOylated CENP-T for the presence of SUMOylated SUMO peptides. For this aim purified CENP-T-HA was in vitro SUMOylated with a SUMO Q87R mutant to reduce the length of the tryptic peptide and therefore to be able to identified sit-specific SUMOylation.

2019-09-13 | PXD011963 | Pride

Probing the Roles of SUMOylation in Cancer Cell Biology Using a Selective SAE inhibitor

Project description:Small ubiquitin-like modifier (SUMO) family proteins regulate target protein functions by post-translational modification. However, a potent and selective inhibitor to target the SUMO pathway has been lacking. Here we describe ML-792, the first mechanism-based SUMO-activating enzyme (SAE) inhibitor with nanomolar potency in cellular assays. ML-792 selectively blocks SAE enzyme activity and total SUMOylation, which leads to reduced cancer cell proliferation. Moreover, induction of the MYC oncogene increased the ML-792 mediated viability effect in cancer cells, indicating potential application of SAE inhibitors in MYC-amplified tumors. Using ML-792, we further explored the critical roles of SUMOylation in mitotic progression and chromosome segregation. Furthermore, expression of an SAE catalytic subunit (UBA2) mutant S95N/M97T rescued SUMOylation loss and the mitotic defect induced by ML-792, confirming the selectivity of ML-792. As a potent and selective SAE inhibitor, ML-792 provides rapid loss of endogenously SUMOylated proteins allowing for novel insights into SUMO biology.

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Project description:Chromatin insulators shield promoters and chromatin domains from neighbouring enhancers or chromatin regions with opposing activities. Insulator binding proteins and their cofactors mediate the boundary function. In general, covalent modification of proteins by the Small Ubiqutin-like Modifier (SUMO) is an important mechanism to control the interaction of proteins within complexes. Here we addressed the impact of SUMO in respect to insulator function, chromatin binding of insulator factors and formation of insulator speckles. SUMOylation augments the enhancer blocking function of four different insulator sequences and increases the genome-wide binding of the insulator cofactor CP190. A model is discussed with enhanced chromatin binding of SUMOylated CP190 causing fusion of insulator speckles, which may allow for more efficient insulation.

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Is transthyretin a regulator of Ubc9 SUMOylation?

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2016-08-15 | PXD004515 | Pride

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2023-08-01 | PXD043398 | Pride

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