INSERM Research Director (DR1)
Phone: +33 1 57 27 80 39
Thierry Galli's papers are at:
Membrane trafficking allows for the communication between the different membrane compartments of the biosynthetic and endocytic pathways and for the communication between cells and their environment through the secretion of signalling molecules by exocytosis and capture of nutrients by endocytosis. Exocytosis and endocytosis are crucial to maintain cell homeostasis and are also involved in differentiation and morphogenesis of cells.
Neuronal cell differentiation and de-differentiation of epithelial into mesenchymal cells represent two fundamental models of important cellular changes in shape and function. These two processes share common principles because both imply the presence of a domain specialized for cell movement at the leading edge of the cell, the axonal growth cone and the pseudopodium respectively.
Our working hypothesis is that exocytosis is responsible for the release and expression at the plasma membrane of proteins that are important for cell migration, outgrowth of axons and dendrites, formation and maintenance of cell-cell contacts (including synapses), and the repair and plasticity of neuronal and epithelial cells.
The aim of the team is to understand the basic mechanisms and the regulation of membrane trafficking in the context of brain development and plasticity and cancer. Our favorite molecules are the vesicular SNARE proteins Sec22b, Cellubrevin/VAMP3 and TI-VAMP/VAMP7. We study the function of these proteins at the molecular, cellular and organism level.
We use classical techniques of cellular and molecular biology with special emphasis on live cell imaging and proteomics, as well as biophysical approaches to study membrane dynamics, adhesion and fusion in vitro. Our models include mutant mice, cultured neuronal and epithelial cells, and the reconstitution of proteins into artificial membranes.
Phone: +33 1 57 27 80 39
(Illustration by Jean-Pierre Laigneau)
Phone: +33 1 57 27 80 38
(Illustration by Daniel de Fuenmayor)
Daste F, Galli T, Tareste D (2015) Structure and Function of Longin SNAREs. J. Cell Sci. 128:4263
Petkovic M, Jemaiel A, Daste F, Specht CG, Izeddin I, Vorkel D, Verbavatz JM, Darzacq X, Triller A, Pfenninger KH, Tareste D, Jackson CL, Galli T (2014) The SNARE Sec22b has a non-fusogenic function in plasma membrane expansion. Nat Cell Biol 16:434
Burgo A, Casano AM, Kuster A, Arold ST, Wang G, Nola S, Verraes A, Dingli F, Loew D, Galli T (2013) Increased activity of the Vesicular Soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Receptor TI-VAMP/VAMP7 by Tyrosine Phosphorylation in the Longin Domain. J Biol Chem 288:11960
Larghi P, Williamson DJ, Carpier JM, Dogniaux S, Chemin K, Bohineust A, Danglot L, Gaus K, Galli T, Hivroz C (2013) VAMP7 controls T cell activation by regulating the recruitment and phosphorylation of vesicular Lat at TCR-activation sites. Nat Immunol 14:723
Burgo A, Proux-Gillardeaux V, Sotirakis E, Bun P, Casano A, Verraes A, Liem RK, Formstecher E, Coppey-Moisan M, Galli T (2012) A molecular network for the transport of the TI-VAMP/VAMP7 vesicles from cell center to periphery. Dev Cell 17:166
Danglot L, Zylbersztejn K, Petkovic M, Gauberti M, Meziane H, Combe R, Champy MF, Birling MC, Pavlovic G, Bizot JC, Trovero F, Della Ragione F, Proux-Gillardeaux V, Sorg T, Vivien D, D'Esposito M, Galli T (2012) Absence of TI-VAMP/VAMP7 leads to increased anxiety in mice. J Neurosci 32:1962
Danglot L, Freret T, Le Roux N, Nême NN, Burgo A, Hyenne V, Roumier A, Contremoulins V, Dauphin F, Bizot JC, Vodjdani G, Gaspar P, Boulouard M, Poncer JC, Galli T, Simmler MC (2012) Vezatin is essential for dendritic spine morphogenesis and functional synaptic maturation. J Neurosci 32:9007
Zylbersztejn K, Petkovic M, Burgo A, Deck M, Garel S, Marcos S, Bloch-Gallego E, Nothias F, Serini G, Bagnard D, Binz T, Galli T (2012) The vesicular SNARE Synaptobrevin is required for Semaphorin 3A axonal repulsion. J Cell Biol 196:37
Li F, Pincet F, Perez E, Giraudo C, Tareste D, Rothman J (2011) Complexin activates and clamps SNAREpins by a common mechanism involving an intermediate energetic state. Nat Struct Mol Biol 18:941