SUMO-SIM interactions: From structure to biological functions

Lascorz, Jara; Codina-Fabra, Joan; Reverter, David; Torres-Rosell, Jordi

doi:10.1016/j.semcdb.2021.11.007

Cited by 42 publications

(29 citation statements)

References 77 publications

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“…Transient up-regulation of SUMOylation is associated with responses to cellular stress (Ilic et al, 2022). The modification can alter protein localisation, activity, turnover, and protein interactions (Lascorz et al, 2021, Pichler et al, 2017). SUMOylation is a transient process often confined to a subset of the target protein that may be spatially and temporally restricted.…”

Section: Introductionmentioning

confidence: 99%

SUMO monoclonal antibodies vary in sensitivity, specificity, and ability to detect SUMO conjugate types

Garvin

Lanz

Morris

2022

Preprint

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Monoclonal antibodies (MAb) to members of the Small Ubiquitin-like modifier (SUMO) family are essential tools in the study of cellular SUMOylation. However, many reagents are poorly validated, and the choice of which antibody to use for which detection format is without an evidence base. Here we test twenty-four anti-SUMO monoclonal antibodies for sensitivity and specificity to SUMO1-4 in monomeric and polymeric states in dot-blots, immunoblots, immunofluorescence and immunoprecipitation. We find substantial variability between SUMO MAbs for different conjugation states, detection of increased SUMOylation in response to thirteen different stress agents and as enrichment reagents for analysis of SUMOylated RanGAP1 or KAP1. All four anti-SUMO4 monoclonal antibodies tested cross-reacted with SUMO2/3, and several SUMO2/3 monoclonal antibodies cross-reacted with SUMO4. ~10% of tested monoclonal antibodies produced specific results across multiple applications.

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Section: Introductionmentioning

confidence: 99%

SUMO monoclonal antibodies vary in sensitivity, specificity, and ability to detect SUMO conjugate types

Garvin

Lanz

Morris

2022

Preprint

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“…Besides PIAS, RanBP2 and CBX4, enhanced sumoylation of specific targets has been associated with additional proteins, including: TOPORS, RSUME, MUL1, RHES, some proteins of the tripartite motif family (TRIM), ARF, SF2, class IIa histone deacetylases (HDACs), the PIAS-related proteins NSMCE2 and ZMIZ1-2, SLX4, KROX20, RNF212, UHRF2, TRAF7, ZBED1, MDM2 and ZNF451 (Table 1). Among TRIM proteins, SUMO ligase activity has been attributed to TRIM1, 11,19,22,27,28,32,33,36,38,39 and L2 (Table 1). Interestingly, in some cases, as for TRIM27, and in relation to TP53, ligase activity has been reported for both SUMO and ubiquitin [37].…”

Section: Sumo Ligasesmentioning

confidence: 99%

“…Despite being able to covalently modify other proteins, SUMO is also able to non-covalently interact with many proteins through SUMO interacting motifs (SIMs) present in interactors [ 11 , 12 ]. SIMs are of special relevance for sumoylation-dependent ubiquitination, through the action of SUMO-targeted ubiquitin ligases (STUbLs) like RNF4, which present tandem SIMs able to recognize poly-SUMO chains in ubiquitin targets to be degraded [ 13 ].…”

Section: Introductionmentioning

confidence: 99%

Cancer-Associated Dysregulation of Sumo Regulators: Proteases and Ligases

Lara-Ureña

Jafari

García‐Domínguez

2022

IJMS

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SUMOylation is a post-translational modification that has emerged in recent decades as a mechanism involved in controlling diverse physiological processes and that is essential in vertebrates. The SUMO pathway is regulated by several enzymes, proteases and ligases being the main actors involved in the control of sumoylation of specific targets. Dysregulation of the expression, localization and function of these enzymes produces physiological changes that can lead to the appearance of different types of cancer, depending on the enzymes and target proteins involved. Among the most studied proteases and ligases, those of the SENP and PIAS families stand out, respectively. While the proteases involved in this pathway have specific SUMO activity, the ligases may have additional functions unrelated to sumoylation, which makes it more difficult to study their SUMO-associated role in cancer process. In this review we update the knowledge and advances in relation to the impact of dysregulation of SUMO proteases and ligases in cancer initiation and progression.

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“…SUMOylation is similar to the ubiquitin cascade with 3 coupled enzymes E1, E2, and E3 SUMOylation enzymes where a small ubiquitin-related modifier (SUMO) protein is transferred to the substrate ( Figure 1 ). The majority of functions of this PTM process are to establish non-covalent protein-protein interactions between SUMOylated substrates and their binding partners ( Lascorz et al, 2021 ). This process has been linked to the most studied inflammasome component NLRP3, but how this PTM could regulate other inflammasome components is still an area of unexplored biology.…”

Section: Inflammasome Components Sumoylationmentioning

confidence: 99%

Posttranslational Regulation of Inflammasomes, Its Potential as Biomarkers and in the Identification of Novel Drugs Targets

Nanda

Vollmer²,

Pérez-Oliva

2022

Front. Cell Dev. Biol.

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In this review, we have summarized classical post-translational modifications (PTMs) such as phosphorylation, ubiquitylation, and SUMOylation of the different components of one of the most studied NLRP3, and other emerging inflammasomes. We will highlight how the discovery of these modifications have provided mechanistic insight into the biology, function, and regulation of these multiprotein complexes not only in the context of the innate immune system but also in adaptive immunity, hematopoiesis, bone marrow transplantation, as well and their role in human diseases. We have also collected available information concerning less-studied modifications such as acetylation, ADP-ribosylation, nitrosylation, prenylation, citrullination, and emphasized their relevance in the regulation of inflammasome complex formation. We have described disease-associated mutations affecting PTMs of inflammasome components. Finally, we have discussed how a deeper understanding of different PTMs can help the development of biomarkers and identification of novel drug targets to treat diseases caused by the malfunctioning of inflammasomes.

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SUMO-SIM interactions: From structure to biological functions

Cited by 42 publications

References 77 publications

SUMO monoclonal antibodies vary in sensitivity, specificity, and ability to detect SUMO conjugate types

SUMO monoclonal antibodies vary in sensitivity, specificity, and ability to detect SUMO conjugate types

Cancer-Associated Dysregulation of Sumo Regulators: Proteases and Ligases

Posttranslational Regulation of Inflammasomes, Its Potential as Biomarkers and in the Identification of Novel Drugs Targets

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