I
Isabelle Jariel-Encontre
Researcher at Centre national de la recherche scientifique
Publications - 46
Citations - 2016
Isabelle Jariel-Encontre is an academic researcher from Centre national de la recherche scientifique. The author has contributed to research in topics: Proteasome & Transcription factor. The author has an hindex of 25, co-authored 43 publications receiving 1775 citations. Previous affiliations of Isabelle Jariel-Encontre include University of Montpellier.
Papers
More filters
Journal ArticleDOI
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.
Journal ArticleDOI
Ubiquitinylation is not an absolute requirement for degradation of c- Jun protein by the 26 S proteasome
TL;DR: Using cell-free degradation assays, it is shown that ubiquitinylation, along with other types of tagging, is not an absolute prerequisite for ATP-dependent degradation of c-Jun by the 26 S proteasome, indicating that a protein may bear intrinsic structural determinants allowing its selective recognition and breakdown by the26 S proteAsome.
Journal ArticleDOI
The AP-1 transcriptional complex: Local switch or remote command?
TL;DR: These studies strikingly indicate that AP-1 principally operates as a remote command binding to distal enhancers, placing chromatin architecture dynamics at the heart of its transcriptional actions.
Journal ArticleDOI
Ubiquitin-independent proteasomal degradation of Fra-1 is antagonized by Erk1/2 pathway-mediated phosphorylation of a unique C-terminal destabilizer.
TL;DR: The presence of a single destabilizer within Fra-1, instead of two that are differentially regulated in c-Fos, explains the much faster turnover of the latter when cells traverse the G0/G1-to-S-phase transition.