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Laboratory | Simulation ＆ modelling
Caveolin-1, a small membrane protein (21 KDa) plays a key role in the formation of caveolae defined from a morphological point of view as plasma membrane invaginations. These membrane structures are implicated in numerous cellular functions such as endocytosis, signalization, lipid transport and more recently mechanical stress. Our objective is to establish the molecular basis of the interactions networks associated with proteins and lipids in order to understand how the different networks of protein-lipid interactions are organized within these structures.
Some membrane proteins possess acylated anchors covalently linked to cysteine. In the few cases studies of membrane proteins, it was shown that the consequences of these post-translational modifications are: protein conformational modifications, association with specific lipid domains, regulation of interactions with their partner and/or interplay with other post-translational modifications. To better understand the structural and functional role of cysteine acylation, different membrane proteins having one or more acylations are studied via complementary biochemical (production, function), biophysics (NMR) and bio-informatics (modelisation and molecular dynamics simulations) approaches.
Biomembranes can be viewed as a mosaic of lipid domains with unique biochemical compositions, controlled by a variety of lateral segregation processes occurring with the lipid matrix. In our group, we study the formation of phase induced by the interaction at the membrane interface of polysaccharide (cyclodextrins) inserted into lipid bilayers via an hydrophobic anchor as an example of such segregation processes. Cyclodextrins are water-soluble cyclic oligosaccharides possessing an internal rather hydrophobic cavity that can include hydrophobic compounds leading to water-soluble inclusion complexes.
Under standard conditions, phosphatidylserines (PS) are localized mainly in the internal leaflet of the plasma membrane. This asymmetric distribution is altered during apoptosis, and exposure of PS at the cell surface constitutes one of the early steps of this cellular process. Our objective is to develop high affinity peptide probes to PS for the in vivo detection of apoptosis. Our project is based on previous results characterizing the membrane recognition properties of annexin domains. Simultaneously, we are pursuing more fundamental studies to understand the mechanisms involved in specific interactions at the membrane interface between lipids (anionic phospholipids and sterols) and membrane-anchored protein domains.
CEA is a French government-funded technological research organisation in four main areas: low-carbon energies, defense and security, information technologies and health technologies. A prominent player in the European Research Area, it is involved in setting up collaborative projects with many partners around the world.