Henri-François Renard

Henri-François Renard
University of Namur | FUNDP · NARILIS

PhD

About

21
Publications
2,589
Reads
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764
Citations
Citations since 2017
15 Research Items
671 Citations
2017201820192020202120222023020406080100120
2017201820192020202120222023020406080100120
2017201820192020202120222023020406080100120
2017201820192020202120222023020406080100120
Introduction
Additional affiliations
January 2020 - present
University of Namur
Position
  • Professor (Assistant)
Description
  • Starting to develop my own lab :-) Clathrin-independent endocytosis, BAR domain proteins, membrane biology, fancy microscopy.
October 2015 - December 2019
Université Catholique de Louvain - UCLouvain
Position
  • PostDoc Position
Description
  • Postdoc in the lab of Pierre Morsomme
January 2011 - July 2015
Institut Curie
Position
  • PostDoc Position
Description
  • Postdoc in the lab of Ludger Johannes
Education
September 2001 - September 2006
Université Catholique de Louvain - UCLouvain
Field of study
  • Bioengineering in Chemistry and Bio-industries - Molecular and Cellular Engineering

Publications

Publications (21)
Preprint
Full-text available
The facultative intracellular pathogen Brucella abortus interacts with several organelles of the host cell to reach its replicative niche inside the endoplasmic reticulum. However, little is known about the interplay between the bacteria and the host cell mitochondria. Here, we showed that B. abortus triggers a strong mitochondrial network fragment...
Preprint
Full-text available
In their environment, cells have to cope with mechanical stresses constantly. Among those, nanoscale deformations of plasma membrane induced by substrate nanotopography are now largely accepted as a biophysical stimulus influencing cell behaviour and function. However, the mechanotransduction cascades involved and their precise molecular effects on...
Article
Endocytic mechanisms actively regulate plasma membrane composition and sustain fundamental cellular functions. Recently, we identified a clathrin-independent endocytic (CIE) modality mediated by the BAR domain protein endophilin-A3 (endoA3, encoded by SH3GL3), which controls the cell surface homeostasis of the tumor marker CD166 (also known as ALCA...
Article
Endocytosis mediates the uptake of extracellular proteins, micronutrients and transmembrane cell surface proteins. Importantly, many viruses, toxins and bacteria hijack endocytosis to infect cells. The canonical pathway is clathrin-mediated endocytosis (CME) and is active in all eukaryotic cells to support critical house-keeping functions. Unconven...
Article
Full-text available
While several clathrin-independent endocytic processes have been described so far, their biological relevance often remains elusive, especially in pathophysiological contexts such as cancer. In this study, we find that the tumor marker CD166/ALCAM (Activated Leukocyte Cell Adhesion Molecule) is a clathrin-independent cargo. We show that endophilin-...
Article
Full-text available
The retrograde transport inhibitor Retro-2 has a protective effect on cells and in mice against Shiga-like toxins and ricin. Retro-2 causes toxin accumulation in early endosomes and relocalization of the Golgi SNARE protein syntaxin-5 to the endoplasmic reticulum. The molecular mechanisms by which this is achieved remain unknown. Here, we show that...
Article
Full-text available
Endocytosis of membrane proteins in yeast requires α-arrestin-mediated ubiquitylation by the ubiquitin ligase Rsp5. Yet, the diversity of α-arrestin targets studied is restricted to a small subset of plasma membrane (PM) proteins. Here, we performed quantitative proteomics to identify new targets of 12 α-arrestins and gained insight into the divers...
Article
Membrane fission is essential to life. It is required for many fundamental cellular processes, as diverse as cyto- and karyokinesis, organelle division, membrane repair, and membrane trafficking and endocytosis. While membrane fission was originally seen as resulting from the action of mechanoenzymes such as dynamin, it is clear that the reality is...
Data
Movie S1. EndoA2 N-BAR Domain Does Not Induce Scission of Tubular Membranes, Related to Figure 1 and Figure S1 Confocal fluorescence time-lapse during injection of an N-BAR domain of endoA2 near a tube pulled from a micropipette-aspired GUV. Movie shows spontaneous tubulation of the GUV and the formation of a scaffold on the tube (causing it to bu...
Data
Confocal fluorescence time lapse showing a scission event of a kinesin-pulled tube connected to a GUV seconds after endoA2 injection into the system. Shown is a different example from Movie S4. Scale bar, 2 μm.
Data
Movie shows extension of a tube partially scaffolded by endoA2 N-BAR domain leading up to scission at the tube-GUV interface. Shown are the confocal fluorescence time lapse (left) and the tube retraction force, f, both changing with time, t. Top left: N-BAR (green); center left: lipids (red); bottom left: overlay
Data
Movie shows extension of a tube initially fully scaffolded by endoA2 N-BAR domain leading up to scission. After initial extension, gaps form in the scaffold making fully and partially scaffolded tubes equivalent in FDS. Shown are confocal fluorescence time lapse (left) and tube retraction force, f, both changing with time, t. Top left: N-BAR (green...
Data
Confocal fluorescence time lapse showing two scission events of kinesin-pulled tubes connected to a GUV seconds after endoA2 injection into the system. Scale bar, 2 μm.
Article
Full-text available
Membrane scission is essential for intracellular trafficking. While BAR domain proteins such as endophilin have been reported in dynamin-independent scission of tubular membrane necks, the cutting mechanism has yet to be deciphered. Here, we combine a theoretical model, in vitro, and in vivo experiments revealing how protein scaffolds may cut tubul...
Article
Full-text available
Significance Lipid membranes are dynamic assemblies, changing shape on nano- to micron-sized scales. Some proteins can sculpt membranes by organizing into a molecular scaffold, dictating the membrane’s shape and properties. We combine microscopy, mathematical modeling, and simulations to explore how Bin/Amphiphysin/Rvs proteins assemble to form sca...
Article
Endocytosis is an essential cellular process that is often hijacked by pathogens and pathogenic products. Endocytic processes can be classified into two broad categories, dependent or not on clathrin. The SNARE proteins VAMP2, 3 and 8 are internalized in a clathrin-dependent manner. Yet, the full scope of their endocytic behavior has not yet been e...
Article
Full-text available
Antigen presenting cells have the remarkable capacity to transfer exogenous antigens to the cytosol for processing by proteasomes and subsequent presentation on MHC-I molecules, a process termed cross-presentation. It is the target of biomedical approaches that aim to trigger a therapeutic immune response. The receptor-binding B-subunit of Shiga to...
Article
Full-text available
During endocytosis, energy is invested to narrow the necks of cargo-containing plasma membrane invaginations to radii at which the opposing segments spontaneously coalesce, thereby leading to the detachment by scission of endocytic uptake carriers. In the clathrin pathway, dynamin uses mechanical energy from GTP hydrolysis to this effect, assisted...
Article
Several exogenous and endogenous cargo proteins are internalized independently of clathrin, including the bacterial Shiga toxin. The mechanisms underlying early steps of clathrin-independent uptake remain largely unknown. In this study, we have designed a protocol to obtain gradient fractions containing Shiga toxin internalization intermediates. Us...
Article
SNA (Sensitive to Na(+)) proteins form a membrane protein family, which, in the yeast Saccharomyces cerevisiae, is composed of four members: Sna1p/Pmp3p, Sna2p, Sna3p and Sna4p. In this study, we focused on the 79 residue Sna2p protein. We found that Sna2p is localized in the vacuolar membrane. Directed mutagenesis showed that two functional tyrosi...

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Projects

Project (1)
Project
Since several years, we are working on the characterization of clathrin-independent endocytic mechanisms in mammalian cells (1-3). Located at the interface of cell biology and immunology, the project tackles fundamental questions related to the regulation of adhesive/migratory and immunogenic properties of cancer cells by clathrin-independent endocytic mechanisms. Among other approaches, we use advanced tools of cell biology (cell migration) and cancer immunology, and start-of-the-art fluorescence microscopy approaches (fixed cell and live cell imaging: confocal, super resolution microscopy, TIRF, etc.). (1) Renard, H. F. et al. Endophilin-A3 and Galectin-8 control the clathrin-independent endocytosis of CD166. Nat Commun 11, 1457, doi:10.1038/s41467-020-15303-y (2020). (2) Renard, H. F. et al. Endophilin-A2 functions in membrane scission in clathrin-independent endocytosis. Nature 517, 493-496, doi:10.1038/nature14064 (2015). (3)Renard, H. F., Garcia-Castillo, M. D., Chambon, V., Lamaze, C. & Johannes, L. Shiga toxin stimulates clathrin-independent endocytosis of the VAMP2, VAMP3 and VAMP8 SNARE proteins. J Cell Sci 128, 2891-2902, doi:10.1242/jcs.171116 (2015).