Dynamics and nanoenvironment of biological membranes
(Aix-Marseille Université & INSERM)
Overview
We are an interdisciplinary research unit with an important international openness and direct collaboration between cell biologists, biochemists and biophysicists.
We are combining classical biochemical and cell biology approaches with the development of new force microscopy nanotools to map the dynamics, interactions and mechanics of the cell membrane and its nanoenvironment.
This interdisciplinary approach is developed at different scales, from the nanoscale of proteins and membranes to the microscale of cells and tissues, and at different timescales, from microseconds to minutes.
Research lines
Dynamics and interactions of the cell membrane and its nanoenvironment
Dynamics of membrane proteins and membrane remodeling, in health and disease
We are aiming to understand how proteins and lipids interact to drive membrane deformation, fusion and fission and how the mosaic membrane generates complexity and biological function. We are investigating minimal in vitro reconstituted systems to precisely evaluate the biophysical aspects and the physical chemistry of lipid membranes and protein assemblies. In particular, we are studying the effect of antimicrobial peptides on bacterial membranes (with an eye on pharmaceutical applications), calcium-triggered exocytosis, dynamics voltage-gated ion channels and in situ conversion of ceramides altering membrane composition.
Protein-protein and protein-lipid interactions of neuronal synapse
At neuronal membranes, several cis and trans protein-protein and protein-lipid interactions take place and play important roles in neuronal physiology. Our interest focuses on (1) neuronal receptors of botulinum neurotoxin and (2) the secreted LGI1 (Leucin-rich Glioma inactivated 1).
(1) Botulinum neurotoxins are widely used therapeutic agents that interact membrane-exposed protein/lipid double receptors involving two distinct synaptic proteins synaptotagmin and SV2. Our data suggest that these interactions are necessary for botulinum neurotoxin binding. Synaptotagmin isoforms 1 and 2, the principal Ca2+-sensors for exocytosis, abundantly expressed in synaptic vesicles at most nerve terminals and target for autoantibodies that occur in immune-mediated Lambert-Eaton myasthenic syndrome. We aim at understanding the physiological importance of synaptotagmin as well as SV2/gangliosides interaction in neuronal physiology and address the detailed molecular parameters of botulinum neurotoxins binding and translocation through membranes.
(2) LGI1 is a secreted glycoprotein involved in the control of neuronal excitability and implicated in human pathology. The absence of LGI1 secretion or its targeting by autoimmune antibodies lead to an important change in a class of potassium channels (Kv1) expression known to be enriched in specific lipid nanodomains. How an extracellular protein modulates Kv1 membrane stability is unknown. Recently, we discovered that LGI1 interacts with brain gangliosides and we postulate that, by this interaction, LGI1 may organize lipid domains that traps Kv1 channels. We will dissect the implication of LGI1 in preparing such membrane domains.
Single molecule interaction and membrane mechanics
The interaction of the membrane proteins with the cytosolic and extracellular nanoenvironment is mediated by individual molecules. We are probing the interaction of protein-protein and membrane-protein interaction using single molecule force spectroscopy with AFS and AFM. These measurements are complemented with bulk, ensemble measurements with surface plasmon resonance. In addition, the mechanical response of membranes modulates membrane and membrane protein dynamics. We are using similar approaches to better understand the mechanics of membranes over a wide range of timescales.
Biological physics and mechanobiology of cells and tissues in health and disease
Multiscale adhesion and mechanics in cell function
Adhesion and mechanics are interrelated and difficult to understand one without the other. We are studying the interplay between adhesion and mechanics involved in two specific biological processes: cancer cell malignancy and the leukocyte adhesion cascade. Cancer cell malignancy implies formation of metastases and it is known that malignancy correlates with cell softness, in turn modulated by the interaction with the nanoenvironment. The leukocyte adhesion cascade is the first response of the immune system and a highly mechanical process, involving adhesion of leukocytes to the vascular endothelium through single molecules, the formation of long membrane tethers and the deformation and reorganization of the cell cytoskeleton. Complete understanding of the physics behind these two processes requires an approach over multiple length and time scales, from single molecules to the whole cell. Our approach involves mechanical measurements at multiple length and time scales: probing the binding strength of single adhesion complexes and unfolding of proteins, as well as the membrane deformation and tether formation and cytoskeleton microrheology across the cell surface, from microseconds to minutes and hours.
Cancer stem cells and microenvironment mechanics
Although overlook for a while, the relevance of mechanical cues for the cell fate and normal functions is now widely admitted. This research line involves stem cells and their pathological counter-part responsible of cancer (cancer stem cells, CSCs). Recent works suggest that mechanical properties of the microenvironment exert a crucial role in stemness maintenance. This raises a genuine new field of investigation, rheo-histology, that will provide new information about tissue organization and function adding a new dimension beyond the 3D-space.
Fundamental mechanical response of single molecules, membranes, cells and tissues
Mechanics of cells and tissues play a crucial role in many cell functions. Cells and tissues are complex materials that, as such, have a complex, heterogeneous viscoelastic response. The development of advance tools to better probe cell and tissue mechanics at the nanometre and micrometre scales and over the wider dynamic regime is thus essential to understand the role of mechanics in cell function. Moreover, knowledge of the mechanical response of their molecular components such as membranes and single protein filaments, is crucial to obtain a mechanistic description. We developed new techniques, approaches, models and protocols to more robustly and accurately probe cell and tissue rheology and the membrane and single molecule mechanics. Our work is based on nanotools available in the laboratory, mainly atomic force microscopy (AFM) and acoustic force spectroscopy (AFS). This is complemented with other approaches available through collaboration or accessible to the lab such as traction force microscopy, optical tweezers, nanoindentation and cell and tissue stretchers.
Nanotechnology innovation
A strong and unique capacity of our lab is the innovation, development and application of nanotechnology tools. Importantly, atomic force microscopy techniques complemented with traditional approaches. In particular, we are one of the pioneer laboratories of high-speed atomic force microscopy (HS-AFM) and high-speed force spectroscopy (HS-FS), a unique nanotool that allows label-free imaging of the dynamics of molecular processes at the nanoscale and is capable of probing the mechanics of biomolecules, membranes and cells with microsecond time resolution.
More recently, we have implemented acoustic force spectroscopy (AFS) to probe single molecule receptor-ligand interactions at low loading rate and mechanics of living cells at low frequencies.
Selected Publications
Mangeol P, Massey-Harroche D, Sebbagh M, Richard F, Le Bivic A, Lenne PF. 2024 The zonula adherens matura redefines the apical junction of intestinal epithelia. PNAS. 121(9):e2316722121. doi: 10.1073/pnas.2316722121. PMID: 38377188
Mesbah, I., B. Habermann, and F. Rico*. 2024. MechanoProDB: a web-based database for exploring the mechanical properties of proteins. Database. 2024:baae047.
López-Alonso, J., M. Eroles, S. Janel, M. Berardi, J. Pellequer, V. Dupres, F. Lafont, and F. Rico. 2023. PyFMLab: Open-source software for atomic force microscopy microrheology data analysis [version 1; peer review: 2 approved with reservations]. Open Research Europe. 3. doi:10.12688/openreseurope.16550.1
Eroles, M., J. Lopez-Alonso, A. Ortega, T. Boudier, K. Gharzeddine, F. Lafont, C.M. Franz, A. Millet, C. Valotteau, and F. Rico. 2023. Coupled mechanical mapping and interference contrast microscopy reveal viscoelastic and adhesion hallmarks of monocyte differentiation into macrophages. Nanoscale. 15:12255–12269. doi:10.1039/D3NR00757J
Casuso, I, L Redondo-Morata and F Rico *. 2020. Biological physics by high-speed atomic force microscopy. Phil Trans Royal Society A, 378, 20190604, 10.1098/rsta.2019.06
Sumbul, F., Hassanpour, N., Rodriguez Ramos, J., and Rico, F*. 2020. One-step calibration of AFM in liquid. Front. Phys. 8. 10.3389/fphy.2020.00301
Zuttion, F., A Colom, S Matile, D Farago, F Pompeo, J Kokavecz, A Galinier, J Sturgis, and I Casuso. 2020. High-speed atomic force microscopy highlights new molecular mechanism of daptomycin action. Nature Communications, 11 (1), 6312.
Santoni, MJ ¶*, R Kashyap¶, L Camoin, and JP Borg*. 2020. The Scribble family in cancer: twentieth anniversary. Oncogene 39 (47), 7019-7033. doi: 10.1038/s41388-020-01478-7
Rico, F*¶, A Russek¶, L González, H Grubmüller*, and S Scheuring*. 2019. Heterogeneous and Rate-Dependent Streptavidin–Biotin Unbinding Revealed by High-Speed Force Spectroscopy and Atomistic Simulations. PNAS 116, 14, 6594–6601, https://doi.org/10.1073/pnas.1816909116
Valotteau, C, F. Sumbul, F. Rico*. 2019. High-speed force spectroscopy: microsecond force measurements using ultrashort cantilevers. Biophysical reviews, 11, 689–699 doi.org/110.1007/s12551-019-00585-4
Flores, A, J Ramirez-Franco, R Desplantes, K Debreux, G Ferracci, F Wernert, MP Blanchard, Y Maulet, F Youssouf, M Sangiardi, C Iborra, MR Popoff, M Seagar, J Fantini, C Lévêque, and O El Far. 2019. Gangliosides interact with synaptotagmin to form the high-affinity receptor complex for botulinum neurotoxin B. Proceedings of the National Academy of Sciences, 116(36), 18098-18108.
Sumbul F, A Marchesi, F Rico*. 2018. History, Rare And Multiple Events Of Mechanical Unfolding Of Repeat Proteins. J Chem Phys, 148(12), 123335
Lopez Almeida, L. ¶, M Sebbagh ¶, F Bertucci, P Finetti, J Wicinski, S Marchetto, R Castellano, E Josselin, E Charafe-Jauffret, C Ginestier, JP Borg, MJ Santoni*. 2018. The SCRIB paralog LANO/LRRC1 regulates breast cancer stem cell fate through WNT/β-catenin signaling. Stem cell reports, 11(5), 1040-1050. doi: 10.1016/j.stemcr.2018.09.008.
Rigato A., A Miyagi, S, Scheuring, F Rico. 2017. High-frequency microrheology reveals cytoskeleton dynamics in living cells. Nature Physics, 13(8), 771-775
Bays JL, Campbell HK, Heidema C, Sebbagh M, DeMali KA. Linking E-cadherin mechanotransduction to cell metabolism through force-mediated activation of AMPK. Nat Cell Biol. 19(6):724-731. doi: 10.1038/ncb3537. PMID: 28553939
Rowart P, Erpicum P, Krzesinski JM, Sebbagh M, Jouret F. 2017 Mesenchymal Stromal Cells Accelerate Epithelial Tight Junction Assembly via the AMP-Activated Protein Kinase Pathway, Independently of Liver Kinase B1. Stem Cells Int. doi:10.1155/2017/9717353.
Chiaruttini, N.*; L. Redondo-Morata*; A. Colom, F. Humbert, M. Lenz, S. Scheuring, A. Roux. 2015. Relaxation of loaded ESCRT-III spiral springs drives membrane deformation, Cell, 163 (4): 866-79 (*, equal contribution).
Rico F, L González, I Casuso, M Puig, and S Scheuring. 2013. High-speed force spectroscopy unfolds titin at the velocity of molecular dynamics simulations. Science 342 (6159), 741-743 2013
Upcoming events
Forum Sondes Locales, April 2024, Lyon
European South Atlantic Biophysics Meeting, June 2024, San Sebastian
Past events
Single Molecule Biophysics, January 2024, Les Houches
BSI, November 2023, Marseille
AFMBioMed summer school, August 2023, Marcoule
EBSA meeting, August 2023, Sweden
DPG SKM23, March 2023, Dresden, Germany
Address:
DyNaMo U1325, INSERM & Aix-Marseille Unviersité
Parc Scientifique de Luminy, Bâtiment Inserm TPR2 bloc 5, case 909
163 avenue de Luminy, 13009 Marseille, France