Automated Author ProfileBenoist, Marion
0009-0004-8951-1970
Benoist, Marion
Current S-Index
Sum of Dataset Indices for all datasets
Average Dataset Index per Dataset
Average Dataset Index per dataset
Total Datasets
Total datasets for this author
Average FAIR Score
Average FAIR Score per dataset
Total Citations
Total citations to the author's datasets
Total Mentions
Total mentions of the author's datasets
S-Index Interpretation
The S-Index (Sharing Index) is a comprehensive metric that represents the cumulative impact of all your datasets. It is calculated as the sum of Dataset Index scores across all your claimed datasets.
What it means:
- A higher S-index indicates greater overall impact of your datasets relative to typical datasets in their fields of research
- The S-Index grows as you add more datasets or as existing datasets gain more citations and mentions
- It provides a single number to track your research data impact over time
Current S-Index: 3.2 (sum of 2 datasets Dataset Index scores)
More information here.
S-Index Over Time
Cumulative Citations Over Time
Cumulative Mentions Over Time
Datasets
Mechanotransduction, the process by which cells sense and respond to mechanical stimuli, relies on cell adhesion, actin cytoskeleton remodeling, and biochemical signal integration. Here, we demonstrate that dynamin 2 (DNM2), clathrin plaques and surrounding branched actin filaments are mechanotransduction platforms that regulate YAP/TAZ signaling. We show that branched actin filaments surrounding clathrin plaques recruit TAZ, whereas contractile stress fibers associated with focal adhesions promote YAP localization. DNM2, the actin capping protein gelsolin, YAP and TAZ organize the cortical actin network around clathrin plaques while actin disorganization due to DNM2 or clathrin depletion delocalize both YAP and TAZ. In centronuclear myopathy models, DNM2 mutations impair actin remodeling, leading to aberrant YAP/TAZ nuclear translocation and altered gene expression of their transcriptional targets. Importantly, allele-specific mutant DNM2 silencing restores YAP/TAZ balance, actin organization and normalizes gene expression. Our findings establish clathrin plaques and DNM2 as central regulators of YAP/TAZ-mediated mechanotransduction.
Authors
- Benoist, Marion ;
- Milliet, Kévin ;
- Franck, Agathe ;
- Moparthi, Satish ;
- Fongy, Anaïs ;
- Moulay, Gilles ;
- Lacene, Emmanuelle ;
- Mamchaoui, Kamel ;
- Chardonnet, Solenne ;
- Dingli, Florent ;
- Loew, Damarys ;
- Evangelista, Teresinha ;
- Coirault, Catherine ;
- Trochet, Delphine ;
- Bitoun, Marc ;
- vassilopoulos, stéphane
Mechanotransduction, the process by which cells sense and respond to mechanical stimuli, relies on cell adhesion, actin cytoskeleton remodeling, and biochemical signal integration. Here, we demonstrate that dynamin 2 (DNM2), clathrin plaques and surrounding branched actin filaments are mechanotransduction platforms that regulate YAP/TAZ signaling. We show that branched actin filaments surrounding clathrin plaques recruit TAZ, whereas contractile stress fibers associated with focal adhesions promote YAP localization. DNM2, the actin capping protein gelsolin, YAP and TAZ organize the cortical actin network around clathrin plaques while actin disorganization due to DNM2 or clathrin depletion delocalize both YAP and TAZ. In centronuclear myopathy models, DNM2 mutations impair actin remodeling, leading to aberrant YAP/TAZ nuclear translocation and altered gene expression of their transcriptional targets. Importantly, allele-specific mutant DNM2 silencing restores YAP/TAZ balance, actin organization and normalizes gene expression. Our findings establish clathrin plaques and DNM2 as central regulators of YAP/TAZ-mediated mechanotransduction.
Authors
- Benoist, Marion ;
- Milliet, Kévin ;
- Franck, Agathe ;
- Moparthi, Satish ;
- Fongy, Anaïs ;
- Moulay, Gilles ;
- Lacene, Emmanuelle ;
- Mamchaoui, Kamel ;
- Chardonnet, Solenne ;
- Dingli, Florent ;
- Loew, Damarys ;
- Evangelista, Teresinha ;
- Coirault, Catherine ;
- Trochet, Delphine ;
- Bitoun, Marc ;
- vassilopoulos, stéphane