title: Detection of Protein SUMOylation In Situ by Proximity Ligation Assays.
abstract: Sumoylation is a posttranslational process essential for life and concerns a growing number of crucial proteins. Understanding the influence of this phenomenon on individual proteins or on cellular pathways in which they function has become an intense area of research. A critical step in studying protein sumoylation is to detect sumoylated forms of a particular protein. This has proven to be a challenging task for a number of reasons, especially in the case of endogenous proteins and in vivo studies or when studying rare cells such as stem cells. Proximity ligation assays that allow detection of closely interacting protein partners can be adapted for initial detection of endogenous sumoylation or ubiquitination in a rapid, ultrasensitive, and cheap manner. In addition, modified forms of a given protein can be detected in situ in various cellular compartments. Finally, the flexibility of this technique may allow rapid screening of drugs and stress signals that may modulate protein sumoylation.
authors.affiliation: INSERM U944 - CNRS UMR7212 - Université Paris Diderot, Sorbonne Paris Cité - Equipe labellisée par la Ligue Nationale contre le Cancer, IUH, Hôpital St. Louis 1, Avenue Claude Vellefaux, 75475, Paris cedex 10, France. umut.sahin@boun.edu.tr.|Department of Molecular Biology and Genetics, Center for Life Sciences and Technologies, Boğaziçi University, Istanbul, 34342, Turkey. umut.sahin@boun.edu.tr.
authors.forename: Umut
authors.initials: U
authors.lastname: Sahin
authors.affiliation: INSERM U944 - CNRS UMR7212 - Université Paris Diderot, Sorbonne Paris Cité - Equipe labellisée par la Ligue Nationale contre le Cancer, IUH, Hôpital St. Louis 1, Avenue Claude Vellefaux, 75475, Paris cedex 10, France.
authors.forename: Florence
authors.initials: F
authors.lastname: Jollivet
authors.affiliation: INSERM U944 - CNRS UMR7212 - Université Paris Diderot, Sorbonne Paris Cité - Equipe labellisée par la Ligue Nationale contre le Cancer, IUH, Hôpital St. Louis 1, Avenue Claude Vellefaux, 75475, Paris cedex 10, France.|Collège de France, University of Paris Science Lettre, Paris, France.
authors.forename: Caroline
authors.initials: C
authors.lastname: Berthier
authors.affiliation: INSERM U944 - CNRS UMR7212 - Université Paris Diderot, Sorbonne Paris Cité - Equipe labellisée par la Ligue Nationale contre le Cancer, IUH, Hôpital St. Louis 1, Avenue Claude Vellefaux, 75475, Paris cedex 10, France.|Collège de France, University of Paris Science Lettre, Paris, France.|AP-HP, Service de Biochimie, Hôpital St. Louis, Paris, France.
authors.forename: Hugues
authors.initials: H
authors.lastname: de Thé
authors.affiliation: INSERM U944 - CNRS UMR7212 - Université Paris Diderot, Sorbonne Paris Cité - Equipe labellisée par la Ligue Nationale contre le Cancer, IUH, Hôpital St. Louis 1, Avenue Claude Vellefaux, 75475, Paris cedex 10, France. valerie.lallemand@inserm.fr.|Collège de France, University of Paris Science Lettre, Paris, France. valerie.lallemand@inserm.fr.
authors.forename: Valérie
authors.initials: V
authors.lastname: Lallemand-Breitenbach
mesh_terms: D000906:Antibodies / Q000737:chemistry; D034961:Antigens, Nuclear / Q000235:genetics / Q000378:metabolism*; D001151:Arsenic / Q000494:pharmacology; D001324:Autoantigens / Q000235:genetics / Q000378:metabolism*; D001681:Biological Assay; D005455:Fluorescent Antibody Technique; D006367:HeLa Cells; D006801:Humans; D016898:Interferon-alpha / Q000494:pharmacology; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D011499:Protein Processing, Post-Translational; D025842:SUMO-1 Protein / Q000235:genetics / Q000378:metabolism*; D058207:Sumoylation
chemical_list: D000906:Antibodies; D034961:Antigens, Nuclear; D001324:Autoantigens; D016898:Interferon-alpha; D025842:SUMO-1 Protein; C495501:SUMO1 protein, human; C066642:SP100 protein, human; D001151:Arsenic
keywords: PML nuclear bodies; Proximity ligation assay; SUMO; SUMO-interacting motif; Ubiquitin