Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

A short SUMOylation tag modulates transcription factor activity

ABSTRACT: This research demonstrates that a short peptide, composed of residues 24-55 of ZNF451, is sufficient to induce SUMOylation of target proteins, both in vitro and in human cells. Increased SUMOylation of the transcription factor p53 via fusion with the ZNF451 peptide inhibits its transcriptional activity, providing a proof of principle that targeted SUMOylation can be used to modulate the activity of targeted transcription factors.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell

SUBMITTER: Chongyang Li

LAB HEAD: Pierre Thibault

PROVIDER: PXD068083 | Pride | 2025-12-01

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	CL_SUMO_020925_1.raw	Raw
	CL_SUMO_020925_2.raw	Raw
	CL_SUMO_020925_3.raw	Raw
	CL_SUMO_020925_4.raw	Raw
	CL_SUMO_020925_5.raw	Raw

Items per page:

1 - 5 of 14

Publications

A short SUMOylation tag modulates transcription factor activity.

Bouchard Antoine Y AY Vivet Anaïs J I AJI Cabana Valérie C VC Li Chongyang C Thibault Pierre P Lussier Marc P MP Mader Sylvie S Cappadocia Laurent L

The Journal of biological chemistry 20251008 11

SUMOylation is a posttranslational modification that regulates multiple aspects of protein biology, including the activity of transcription factors such as p53. Although strategies exist to decrease protein SUMOylation in a targeted manner, options are limited to increase SUMOylation in a protein-specific manner. Here, we developed a strategy to induce SUMOylation of a target protein relying on its genetic fusion to a 32-residue tag termed ZNF and composed of the SUMO E3 module of ZNF451. Throug ...[more]

PMID: 41072767

Similar Datasets

SUMO operates from a unique long tandem repeat to keep innate immunity in check

Project description:The SUMO pathway mainly functions to repress innate immunity in myeloid cells. Inactivating sumoylation triggers a strong, noncanonical, type I interferon (IFN1) response, amplified and coupled with inflammation upon stimulation. These findings transposed to pre-clinical models with the demonstration that sumoylation inhibitors activate antitumor immunity in an IFN1-dependent manner. Yet, how sumoylation represses immune signaling remains largely unknown. Here, we identified MORC3, a negative regulator of IFNB1, as the top SUMO2/3 substrate in myeloid cells. We show that, in monocytes, SUMO functions to repress basal IFNB1 in cis through a single long tandem repeat regulated by MORC3 [MORC3-regulated element (MRE)] that concentrates multiple motifs for the myeloid-enriched PU.1 factor. Inhibiting sumoylation induces a 3D genome reorganization nucleated from the MRE, which acquires both insulator and PU.1-activated enhancer activities, together with loss of H3.3 and H3K9me3 repressive marks and recruitment of PU.1. Paradoxically, MORC3, that interacts with PU.1, is massively recruited, yet unable to repress the MRE. Finally, we show that both sumoylation and MORC3 ATPase cycle are critical for MORC3 repressive activity. Our study thus uncovers an unconventional mechanism in which sumoylation, in concert with MORC3, orchestrates a metastable H3.3/H3K9me3 heterochromatin state on a multi-PU.1 binding platform to prevent an uncontrolled myeloid-specific immune response.

2025-08-16 | PXD061276 | Pride

A Split-SUMO-ID proteomics approach to identify the Rad52 and SUMO-dependent interactome of Schizosaccharomyces pombe

Project description:A PTM known as sumoylation, manifested by an attachment of a SUMO molecule (small ubiquition-like modifier) to target proteins, may lead to changes in the tagged protein’s function, localization or stability. This PTM is present in all eukaryotes. In fission yeast, Rad52 is a DNA repair mediator protein, which enables stalled replicatory fork restart via a homologous recombination mechanism. Fork stalling was postulated to rely on the so-called SUMOylation waves of certain replisome components. Within the project we aimed to identify the protein content at the Rad52-dependent repair sites, which undergo a SUMO wave event. For this purpose, a peculiar proximity labelling approach was uptaken, which is based on fusing two interaction partners to distinct domains (N and C terminal) of a TurboID biotin ligase. Only upon partners’ contact, the ligase is reconstituted and active to label nearby proteins with a biotin molecule, hence providing elusive means of specifically capturing interaction-dependent interactomes.

2025-10-31 | PXD055556 | Pride

Uncovering Global SUMOylation Signaling Networks in a Site-Specific Manner

Project description:SUMOylation is a reversible post-translational modification essential for genome stability. Using high-resolution mass spectrometry, we have studied global SUMOylation in mammalian cells and in a site-specific manner, identifying a total of over 4,300 SUMOylation sites in over 1,600 proteins. Moreover, for the first time in excess of 1,000 SUMOylation sites were identified under standard growth conditions. SUMOylation dynamics were quantitatively studied in response to SUMO protease inhibition, proteasome inhibition and heat shock.

2014-09-04 | PXD001061 | Pride

MaxQuant.Live enables enhanced selectivity and identification of peptides modified by endogenous SUMO and ubiquitin

Project description:Small ubiquitin-like modifiers (SUMOs) and ubiquitin are frequent post-translational modifications of proteins that play pivotal roles in all cellular processes. We previously reported mass spectrometry-based proteomics methods that enable profiling of lysines modified by endogenous SUMO or ubiquitin in an unbiased manner, without requiring genetic engineering. Here we investigated the applicability of precursor mass filtering enabled by MaxQuant.Live (MQL) to our SUMO and ubiquitin proteomics workflows, which efficiently avoided sequencing of precursors too small to be modified but otherwise indistinguishable by mass-to-charge ratio. Using peptide mass filtering, we achieved much higher precursor selectivity, ultimately resulting in up to 30% more SUMO and ubiquitin sites identified from replicate samples. Real-time ‘untargeting’ of unmodified peptides by MQL resulted in 90% SUMO-modified precursor selectivity from a 25% pure sample, demonstrating great applicability for digging deeper into ubiquitin-like modificomes. We adapted the mass filtering strategy to the new Exploris 480 mass spectrometer, achieving comparable gains in SUMO precursor selectivity and identification rates. Collectively, mass filtering via MQL significantly increased identification rates of SUMO- and ubiquitin-modified peptides from the exact same samples, without the requirement for prior knowledge or spectral libraries.

2021-02-05 | PXD022367 | Pride

Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation (part 2)

Project description:Small ubiquitin-like modifiers (SUMOs) are post-translational modifications (PTMs) that regulate nuclear cellular processes. Here we used an augmented K0–SUMO proteomics strategy to identify 40,765 SUMO acceptor sites and quantify their fractional contribution for 6,747 human proteins. Structural–predictive analyses revealed that lysines residing in disordered regions are preferentially targeted by SUMO, in notable contrast to other widespread lysine modifications. In our data set, we identified 807 SUMOylated peptides that were co-modified by phosphorylation, along with dozens of SUMOylated peptides that were co-modified by ubiquitylation, acetylation and methylation. Notably, 9% of the identified SUMOylome occurred proximal to phosphorylation, and numerous SUMOylation sites were found to be fully dependent on prior phosphorylation events. SUMO-proximal phosphorylation occurred primarily in a proline-directed manner, and inhibition of cyclin-dependent kinases dynamically affected co-modification. Collectively, we present a comprehensive analysis of the SUMOylated proteome, uncovering the structural preferences for SUMO and providing system-wide evidence for a remarkable degree of cross-talk between SUMOylation and other major PTMs. (part 2)

2017-01-24 | PXD005296 | Pride

Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation (part 1)

2017-01-24 | PXD004927 | Pride

Protein SUMOylation in the Drosophila ovary

Project description:Genome regulation involves complex and highly regulated protein interactions that are often mediated through post-translational modifications (PTMs). SUMOylation – the covalent attachment of the small ubiquitin-like modifier (SUMO) – is a conserved PTM in eukaryotes that has been implicated in a number of essential processes such as nuclear import, DNA damage repair, transcriptional control, and chromatin organization. In Drosophila, SUMO is essential for viability and its depletion from the female germline causes infertility associated with global loss of heterochromatin, and illicit upregulation of transposons and lineage-inappropriate genes. However, the specific targets of SUMO and its mechanistic role in different cellular pathways are still poorly understood. Here, we developed a proteomics-based strategy to characterize the SUMOylated proteome in Drosophila that allowed us to identify ~1500 SUMO sites in 843 proteins in the fly ovary. A high confidence set of SUMOylated proteins is highly enriched in factors involved in heterochromatin regulation and the piRNA pathway that represses transposons. Furthermore, SUMOylation of several piRNA pathway proteins occurs in a Piwi-dependent manner, indicating a functional implication of this modification in the cellular response to transposon activity. Together, these data highlight the impact of SUMOylation on epigenetic regulation and reveal an unexpectedly broad role of the SUMO pathway in the cellular defense against genomic parasites. Finally, this work provides a valuable resource and a system that can be adapted to the study of SUMOylation in other Drosophila tissues.

2023-04-17 | PXD037421 | Pride

Brief suppression of SUMOylation in embryonic stem cells generates embryo-like structures

Project description:Recent advances in synthetic mammalian embryo models have opened new avenues to understand the complex events controlling lineage specification and morphogenetic processes occurring during peri-implantation and early organogenesis. Two main strategies have been developed to build embryo-like structures (ELSs): by assembling extraembryonic and embryonic stem cells (ESCs) or by subjecting ESCs to various morphogens. Here, we show that mouse ESCs solely exposed to chemical inhibition of SUMOylation, a post-translational modification which acts as a general chromatin barrier to cell fate transitions, generates ELSs comprising both anterior neural and trunk-associated regions. HypoSUMOylation-instructed ESCs first give rise to adherent spheroids which, once in suspension, self-organize into gastrulating structures containing cell types spatially and functionally related to embryonic and extraembryonic compartments. Alternatively, spheroids cultured in an optimized droplet-microfluidic device form elongated structures that undergo axial organization reminiscent of natural embryo morphogenesis. Single-cell RNA-sequencing further revealed a variety of cellular lineages including properly positioned anterior neuronal cell types, Schwann cell precursors and paraxial mesoderm segmented into somite-like structures. Mechanistically, transient SUMOylation suppression gradually increases DNA methylation genome-wide and repressive marks deposition at Nanog, enhancing ESC plasticity. Our approach provides a proof of principle for a potential strategy to study early embryogenesis by targeting molecular roadblocks of cell fate change to shape multicellular architecture.

2023-04-13 | PXD031548 | Pride

SUMO-2 activity is inhibited by non-covalent interactions with the Aβ peptide: an exploration of potential pathogenic mechanisms in Alzheimer’s Disease

Project description:SUMOylation is a post-translational modification involving the addition of SUMO isoforms to target proteins and plays a role in various biological processes, including neurodegenerative diseases and ocular pathologies. This study investigates the interaction between SUMO-2 and amyloid (Aβ) peptides, key contributors to Alzheimer’s disease, using techniques like cross-linking mass spectrometry, surface plasmon resonance and biolayer interferometry. The results show that Aβ1-40 and Aβ1-42 bind more strongly to SUMO-2 than to ubiquitin, with binding driven by specific hydrogen bonds and hydrophobic interactions. SUMO-2 was found to inhibit the conversion of Aβ into β-sheet structures and impede Aβ aggregation. Notably, Aβ competes with SUMO-2’s canonical substrates for binding, completely hindering SUMOylation reactions in vitro. Identifying SUMO-2/Aβ1-42 adducts in cellular extracts and live cells further highlights the biological significance of these interactions. Overall, the findings indicate that Aβ peptides impair SUMO-2 function, pointing to the necessity for more research on the implications of SUMOylation in Alzheimer's disease.

2025-08-25 | PXD066055 | Pride

Waves of sumoylation support transcription dynamics during adipocyte differentiation

Project description:Tight control of gene expression networks involved in adipose tissue formation and plasticity is required to adapt to energy needs and environmental cues. However, little is known about the mechanisms that orchestrate the dramatic transcriptional changes leading to adipocyte differentiation. We investigated the regulation of nascent transcription by SUMO during adipocyte differentiation using SLAMseq and ChIPseq. We discovered that SUMO has a dual function in differentiation; it supports the initial downregulation of pre-adipocyte-specific genes, while it promotes the establishment of the mature adipocyte transcriptional program. By characterizing SUMOylome dynamics in differentiating adipocytes by mass spectrometry, we found that SUMOylation of specific transcription factors like PPARG/RXR and chromatin modifiers promotes the transcription of adipogenic genes. Our data demonstrate that the sumoylation pathway helps coordinates the rewiring of transcriptional networks required for formation of functional adipocytes.

2022-02-18 | PXD024144 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data