G
Guillaume Bossis
Researcher at University of Montpellier
Publications - 65
Citations - 3018
Guillaume Bossis is an academic researcher from University of Montpellier. The author has contributed to research in topics: SUMO protein & Transcription factor. The author has an hindex of 25, co-authored 56 publications receiving 2620 citations. Previous affiliations of Guillaume Bossis include Max Planck Society & Centre national de la recherche scientifique.
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Journal ArticleDOI
Regulation of SUMOylation by Reversible Oxidation of SUMO Conjugating Enzymes
Guillaume Bossis,Frauke Melchior +1 more
TL;DR: It is reported that ROS (reactive oxygen species) result in the rapid disappearance of most SUMO conjugates, including those of key transcription factors, and implicate ROS as key regulators of the sumoylation-desumoylation equilibrium.
Journal ArticleDOI
CNF1 exploits the ubiquitin-proteasome machinery to restrict Rho GTPase activation for bacterial host cell invasion.
Anne Doye,Amel Mettouchi,Guillaume Bossis,René L. Clément,Caroline Buisson-Touati,Gilles Flatau,Laurent Gagnoux,Marc Piechaczyk,Patrice Boquet,Emmanuel Lemichez +9 more
TL;DR: CNF1 toxicity thus results from a restricted activation of Rho GTPases through hijacking the host cell proteasomal machinery.
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E4F1 Is an Atypical Ubiquitin Ligase that Modulates p53 Effector Functions Independently of Degradation
Laurent Le Cam,Laetitia K. Linares,Conception Paul,Eric Julien,Matthieu Lacroix,Elodie Hatchi,Robinson Triboulet,Guillaume Bossis,Ayelet Shmueli,Manuel S. Rodriguez,Olivier Coux,Claude Sardet +11 more
TL;DR: The p53-associated factor E4F1 is identified, a ubiquitously expressed zinc-finger protein first identified as a cellular target of the viral oncoprotein E1A, as an atypical ubiquitin E3 ligase for p53 that modulates its effector functions without promoting proteolysis.
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Ubiquitin-independent degradation of proteins by the proteasome.
TL;DR: The identification of ubiquitin-independent mechanisms for proteasomal degradation poses the paramount question of the multiplicity of catabolic pathways targeting each protein substrate and may help design novel therapeutic strategies.
Journal ArticleDOI
Down-regulation of c-Fos/c-Jun AP-1 dimer activity by sumoylation.
Guillaume Bossis,Cécile E. Malnou,Rosa Farràs,Elisabetta Andermarcher,Robert A. Hipskind,Manuel S. Rodriguez,Darja Schmidt,Stefan Müller,Isabelle Jariel-Encontre,Marc Piechaczyk +9 more
TL;DR: It is shown that the sumoylation of c-Fos is a dynamic process that can be reversed via multiple mechanisms, which supports the idea that this modification does not constitute a final inactivation step that necessarily precedes protein degradation.