Quantitative Biology of Membrane Traffic and Pathogenesis


Our team aims at understanding the molecular mechanisms that control the spatiotemporal organization of endocytic proteins and cell architecture, which has a fundamental biologic relevance and might be key to identify new therapeutic targets.

Endocytosis is a fundamental cellular process that is dedicated to nutrient uptake and to the regulation of signaling and adhesion platforms. The biogenesis of endocytic vesicles is built on the precise spatial and temporal control of a protein machinery to undergo the remodeling of the plasma membrane.
The impaired function of several endocytic components is associated to human disorders such as cancer, myopathies or neurologic diseases. In addition, viruses and bacteria can exploit endocytic pathways as a means of entry into host cells, such as the HIV-1.


We apply quantitative approaches at the interface of cell biology, biophysics and nanotechnologies that we combine with the development of bottom up synthetic methods and cell-free systems to infer on the organization of cells at different length scales: from the single molecule to the cellular level.

 



Using minimal and in cellulo systems we could previously show that phosphoinositide clustering induced by the endocytic protein BIN1 could mediate the recruitment of its downstream phosphoinositide-binding partner dynamin on membranes (Picas L., et al. Nature Communications 2014). This mechanism was key to better understand why different BIN1 mutations in the autosomal form of centronuclar myopathies display a similar phenotype in dynamin binding. An important research line of the group is dedicated to elucidate if a similar mechanism is implicated in the coordination of trafficking events that rely on the local accessibility to phosphoinositide pools, such is the case of clathrin-mediated endocytosis (Picas L. et al. F1000 Research 2015).

We have also developed new methods to infer on the nanoscale organization of cellular membranes by combining Atomic Force Microscopy and Fluorescence Microscopy (Picas L. et al. ACS Nano 2013).









credits team picture: https://illustration4science.com/

Recent publications

2016
  1. Picas, L.; Gaits-Iacovoni, F.; Goud, B., The emerging role of phosphoinositide clustering in intracellular trafficking and signal transduction. F1000Res 2016, 5.
2015
  1. Carretero-Genevrier, A.; Gich, M.; Picas, L.; Sanchez, C.; Rodriguez-Carvajal, J., Chiral habit selection on nanostructured epitaxial quartz films. Faraday Discuss 2015, 179, 227-33.
2014
  1. Picas, L.; Viaud, J.; Schauer, K.; Vanni, S.; Hnia, K.; Fraisier, V.; Roux, A.; Bassereau, P.; Gaits-Iacovoni, F.; Payrastre, B.; Laporte, J.; Manneville, J. B.; Goud, B., BIN1/M-Amphiphysin2 induces clustering of phosphoinositides to recruit its downstream partner dynamin. Nat Commun 2014, 5, 5647.
2013
  1. Rico, F.; Rigato, A.; Picas, L.; Scheuring, S., Mechanics of proteins with a focus on atomic force microscopy. J Nanobiotechnology 2013, 11 Suppl 1, S3.
  2. Picas, L.; Rico, F.; Deforet, M.; Scheuring, S., Structural and mechanical heterogeneity of the erythrocyte membrane reveals hallmarks of membrane stability. ACS Nano 2013, 7 (2), 1054-63.
  3. Rico, F.; Picas, L.; Colom, A.; Buzhynskyy, N.; Scheuring, S., The mechanics of membrane proteins is a signature of biological function. Soft Matter 2013, 9 (32), 7866-7873.
  4. Carretero-Genevrier, A.; Gich, M.; Picas, L.; Gazquez, J.; Drisko, G. L.; Boissiere, C.; Grosso, D.; Rodriguez-Carvajal, J.; Sanchez, C., Soft-chemistry-based routes to epitaxial alpha-quartz thin films with tunable textures. Science 2013, 340 (6134), 827-31.
2012
  1. Picas, L.; Suarez-Germa, C.; Montero, M. T.; Domenech, O.; Hernandez-Borrell, J., Miscibility behavior and nanostructure of monolayers of the main phospholipids of Escherichia coli inner membrane. Langmuir 2012, 28 (1), 701-6.
  2. Picas, L.; Rico, F.; Scheuring, S., Direct measurement of the mechanical properties of lipid phases in supported bilayers. Biophys J 2012, 102 (1), L01-3.
  3. Picas, L.; Milhiet, P. E.; Hernandez-Borrell, J., Atomic force microscopy: a versatile tool to probe the physical and chemical properties of supported membranes at the nanoscale. Chem Phys Lipids 2012, 165 (8), 845-60.

Team members

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Local

National

International

Post-Doc, Thesis, Internship

We search for highly motivated candidates (biologists, biochemists, biophysicists, physicist) interested on interdisciplinary approaches applied to biological systems: from the single molecule to the cellular level.

Team leader

Laura Picas

ATIP-Avenir Team Leader
Tenure researcher CRCN CNRS
En savoir +


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At a glance



Welcome to the NanoCytoLab!

We are a young and multidisciplinary team that has been established at IRIM in Septembre 2017 thanks to the support of the ATIP-Avenir program.

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Funding

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Contact us


     
       

   

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IRIM
Institut de Recherche en Infectiologie de Montpellier
UMR 9004 - CNRS / UM
1919 route de Mende - 34293 Montpellier cedex 5
FRANCE

 

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