ReviewNeuromolecular medicine2013
Proteomics strategies to identify SUMO targets and acceptor sites: a survey of RNA-binding proteins SUMOylation.
Review in Neuromolecular medicine, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Rice black-streaked dwarf virus-encoded P6 protein impairs OsPelota-mediated antiviral RNA decay defense via promoting OsSCE1b ubiquitination and degradation in rice.Journal of integrative plant biology · 2025Article
- Epigenetic modification in Parkinson's disease.Frontiers in cell and developmental biology · 2023Review
- Review
- Pathological implication of protein post-translational modifications in cancer.Molecular aspects of medicine · 2022Review
- SUMO conjugating enzyme: a vital player of SUMO pathway in plants.Physiology and molecular biology of plants : an international journal of functional plant biology · 2021Review
- Evaluation of post-translational modifications in histone proteins: A review on histone modification defects in developmental and neurological disorders.Journal of biosciences · 2020Review
- Protein SUMOylation modification and its associations with disease.Open biology · 2017Review
- Guanine-Rich Sequences Are a Dominant Feature of Exosomal microRNAs across the Mammalian Species and Cell Types.PloS one · 2016Article
- Proteome-wide identification of SUMO modification sites by mass spectrometry.Nature protocols · 2015Article
- Regulation of translesion DNA synthesis: Posttranslational modification of lysine residues in key proteins.DNA repair · 2015Review
- Quantitative proteomic analysis of histone modifications.Chemical reviews · 2015Review
- Ehrlichia chaffeensis exploits host SUMOylation pathways to mediate effector-host interactions and promote intracellular survival.Infection and immunity · 2014Article
- Proteome-wide identification of SUMO2 modification sites.Science signaling · 2014Article
- Identification and analysis of endogenous SUMO1 and SUMO2/3 targets in mammalian cells and tissues using monoclonal antibodies.Nature protocols · 2014Article
- SUMOylation in neuroplasticity and neurological disorders.Neuromolecular medicine · 2013Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SUMOylation is a protein posttranslational modification that participates in the regulation of numerous biological processes within the cells. Small ubiquitin-like modifier (SUMO) proteins are members of the ubiquitin-like protein family and, similarly to ubiquitin, are covalently linked to a lysine residue on a target protein via a multi-enzymatic cascade. To assess the specific mechanism triggered by SUMOylation, the identification of SUMO protein substrates and of the precise acceptor site to which SUMO is bound is of critical relevance. Despite hundreds of mammalian proteins have been described as targets of SUMOylation, the identification of the precise acceptor sites still represents an important analytical challenge because of the relatively low stoichiometry in vivo and the highly dynamic nature of this modification. Moreover, mass spectrometry-based identification of SUMOylated sites is hampered by the large peptide remnant of SUMO proteins that are left on the modified lysine residue upon tryptic digestion. The present review provides a survey of the strategies that have been exploited in order to enrich, purify and identify SUMOylation substrates and acceptor sites in human cells on a large-scale format. The success of the presented strategies helped to unravel the numerous activities of this modification, as it was shown by the exemplary case of the RNA-binding protein family, whose SUMOylation is here reviewed.
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Registered trials
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