Strategies to Identify Recognition Signals and Targets of SUMOylation

SUMOylation contributes to the regulation of many essential cellular factors. Diverse techniques have been used to explore the functional consequences of protein SUMOylation. Most approaches consider the identification of sequences on substrates, adaptors, or receptors regulating the SUMO conjugatio...

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Main Authors: Elisa Da Silva-Ferrada, Fernando Lopitz-Otsoa, Valérie Lang, Manuel S. Rodríguez, Rune Matthiesen
Format: Article
Language:English
Published: Wiley 2012-01-01
Series:Biochemistry Research International
Online Access:http://dx.doi.org/10.1155/2012/875148
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author Elisa Da Silva-Ferrada
Fernando Lopitz-Otsoa
Valérie Lang
Manuel S. Rodríguez
Rune Matthiesen
author_facet Elisa Da Silva-Ferrada
Fernando Lopitz-Otsoa
Valérie Lang
Manuel S. Rodríguez
Rune Matthiesen
author_sort Elisa Da Silva-Ferrada
collection DOAJ
description SUMOylation contributes to the regulation of many essential cellular factors. Diverse techniques have been used to explore the functional consequences of protein SUMOylation. Most approaches consider the identification of sequences on substrates, adaptors, or receptors regulating the SUMO conjugation, recognition, or deconjugation. The large majority of the studied SUMOylated proteins contain the sequence [IVL]KxE. SUMOylated proteins are recognized by at least 3 types of hydrophobic SUMO-interacting motifs (SIMs) that contribute to coordinate SUMO-dependent functions. Typically, SIMs are constituted by a hydrophobic core flanked by one or two clusters of negatively charged amino acid residues. Multiple SIMs can integrate SUMO binding domains (SBDs), optimizing binding, and control over SUMO-dependent processes. Here, we present a survey of the methodologies used to study SUMO-regulated functions and provide guidelines for the identification of cis and trans sequences controlling SUMOylation. Furthermore, an integrative analysis of known and putative SUMO substrates illustrates an updated landscape of several SUMO-regulated events. The strategies and analysis presented here should contribute to the understanding of SUMO-controlled functions and provide rational approach to identify biomarkers or choose possible targets for intervention in processes where SUMOylation plays a critical role.
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spelling doaj-art-4c262d4561ce42e187837938cb3c36c12025-02-03T05:59:48ZengWileyBiochemistry Research International2090-22472090-22552012-01-01201210.1155/2012/875148875148Strategies to Identify Recognition Signals and Targets of SUMOylationElisa Da Silva-Ferrada0Fernando Lopitz-Otsoa1Valérie Lang2Manuel S. Rodríguez3Rune Matthiesen4Proteomics Unit, CIC bioGUNE, CIBERehd, Building 801A, Bizkaia Technology Park, 48160 Derio Bizkaia, SpainProteomics Unit, CIC bioGUNE, CIBERehd, Building 801A, Bizkaia Technology Park, 48160 Derio Bizkaia, SpainUbiqutylation and Cancer Molecular Biology Laboratory, Inbiomed, Paseo Mikeletegi 61, 20009 San Sebastian, Gipuzkoa, SpainProteomics Unit, CIC bioGUNE, CIBERehd, Building 801A, Bizkaia Technology Park, 48160 Derio Bizkaia, SpainProteolysis in Diseases Laboratory, Institute of Molecular Pathology and Immunology, University of Porto, Rua Dr. Roberto Frias s/n, 4200-465 Porto, PortugalSUMOylation contributes to the regulation of many essential cellular factors. Diverse techniques have been used to explore the functional consequences of protein SUMOylation. Most approaches consider the identification of sequences on substrates, adaptors, or receptors regulating the SUMO conjugation, recognition, or deconjugation. The large majority of the studied SUMOylated proteins contain the sequence [IVL]KxE. SUMOylated proteins are recognized by at least 3 types of hydrophobic SUMO-interacting motifs (SIMs) that contribute to coordinate SUMO-dependent functions. Typically, SIMs are constituted by a hydrophobic core flanked by one or two clusters of negatively charged amino acid residues. Multiple SIMs can integrate SUMO binding domains (SBDs), optimizing binding, and control over SUMO-dependent processes. Here, we present a survey of the methodologies used to study SUMO-regulated functions and provide guidelines for the identification of cis and trans sequences controlling SUMOylation. Furthermore, an integrative analysis of known and putative SUMO substrates illustrates an updated landscape of several SUMO-regulated events. The strategies and analysis presented here should contribute to the understanding of SUMO-controlled functions and provide rational approach to identify biomarkers or choose possible targets for intervention in processes where SUMOylation plays a critical role.http://dx.doi.org/10.1155/2012/875148
spellingShingle Elisa Da Silva-Ferrada
Fernando Lopitz-Otsoa
Valérie Lang
Manuel S. Rodríguez
Rune Matthiesen
Strategies to Identify Recognition Signals and Targets of SUMOylation
Biochemistry Research International
title Strategies to Identify Recognition Signals and Targets of SUMOylation
title_full Strategies to Identify Recognition Signals and Targets of SUMOylation
title_fullStr Strategies to Identify Recognition Signals and Targets of SUMOylation
title_full_unstemmed Strategies to Identify Recognition Signals and Targets of SUMOylation
title_short Strategies to Identify Recognition Signals and Targets of SUMOylation
title_sort strategies to identify recognition signals and targets of sumoylation
url http://dx.doi.org/10.1155/2012/875148
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AT valerielang strategiestoidentifyrecognitionsignalsandtargetsofsumoylation
AT manuelsrodriguez strategiestoidentifyrecognitionsignalsandtargetsofsumoylation
AT runematthiesen strategiestoidentifyrecognitionsignalsandtargetsofsumoylation