F
Florence Margottin
Researcher at University of Paris
Publications - 10
Citations - 1549
Florence Margottin is an academic researcher from University of Paris. The author has contributed to research in topics: Phosphorylation & Beta-Transducin Repeat-Containing Proteins. The author has an hindex of 5, co-authored 10 publications receiving 1491 citations.
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Journal ArticleDOI
A Novel Human WD Protein, h-βTrCP, that Interacts with HIV-1 Vpu Connects CD4 to the ER Degradation Pathway through an F-Box Motif
Florence Margottin,Stephan Bour,Hervé Durand,Luc Selig,Serge Benichou,Virginie Richard,Dominique Thomas,Klaus Strebel,Richard Benarous +8 more
TL;DR: HIV-1 Vpu interacts with CD4 in the endoplasmic reticulum and triggers CD4 degradation, presumably by proteasomes, and beta TrCP identified by interaction with Vpu connects CD4 to this proteolytic machinery, and CD4-Vpu-beta TrCP ternary complexes have been detected by coimmunoprecipitation.
Journal ArticleDOI
The F-box protein β-TrCP associates with phosphorylated β-catenin and regulates its activity in the cell
Matthew J. Hart,Jean-Paul Concordet,I. Lassot,Iris Albert,R. Del Los Santos,Hervé Durand,C. Perret,Bonnee Rubinfeld,Florence Margottin,Richard Benarous,Paul Polakis +10 more
TL;DR: It is concluded that β-TrCP is a component of an E3 ubiquitin ligase that is responsible for the targeted degradation of phosphorylated β-catenin.
Journal ArticleDOI
Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-mediated CD4 down-regulation.
Lang Xia Liu,Florence Margottin,Sylvie Le Gall,Olivier Schwartz,Luc Selig,Richard Benarous,Serge Benichou +6 more
TL;DR: Observations suggest that this human thioesterase is a cellular mediator of Nef-induced CD4 down-regulation and could mediate Nef function.
Journal ArticleDOI
Interaction between the cytoplasmic domains of HIV-1 Vpu and CD4: role of Vpu residues involved in CD4 interaction and in vitro CD4 degradation.
Florence Margottin,Serge Benichou,Hervé Durand,Virginie Richard,Lang Xia Liu,Emmanuel Gomas,Richard Benarous +6 more
TL;DR: In this article, the Vpu and CD4 cytoplasmic domains were found, by using a two-hybrid assay in yeast, to interact in the absence of their membrane anchor domains.
Journal ArticleDOI
Inhibition of prokaryotic cell growth by HIV1 Vpr.
TL;DR: Interestingly, using this GST prokaryotic model, it is demonstrated that Vpr, which is known to block the cell cycle of mammalian and yeast cells at the G2 phase, is also bacteriostatic for Escherichia coli, indicating that E. coli appears to be a convenient model system for studies on the function of Vpr.