Membrane Dynamics and Regulation
Sommaire
Program: Cell Biology
Group Leader: Anne SCHMIDT
Tel.: +33 (0)157278012schmidt.anne@ijm.univ-paris-diderot.fr
Floor 2
Understanding the molecular principles underlying the action of cytosolic machineries involved in membrane dynamics and vesicle budding is a hallmark of research in Cell Biology. Over the last fifteen years, the interplay between membrane lipids and proteins acting on biological membranes has come into the spotlight and triggered a series of fundamental concepts on the function of these interactions in key steps of membrane dynamics and in particular vesicle budding and fission.
Our research is currently focused on studying the functional properties, both at the molecular and the cellular level, of proteins that contain lipid-interacting domains. In particular, we are currently studying domains that have been proposed to sense membrane curvature. These domains belong to the so-called Bin/Amphiphysin/Rvs (BAR) domain family and are present in many cytosolic proteins (predicted to be over 200 in number, in mammalian cells).
On a long run, our general goal is to determine the consensus, as well as the peculiarities, between machineries involved in membrane constriction/fission processes.

Intracellular phenotype triggered by a mutation in the BAR
domain of a BAR domain-containing protein (unpublished).
Selection of publications:
Gortat A, Jouve San-Roman M, Vannier C, and A. A. Schmidt.
Single point mutation in the bin/amphiphysin/RVS (BAR) sequence of endophilin impairs dimerization, membrane shaping, and SRC homology 3 domain-mediated partnership.
J Biol Chem. Published online, 2011.
Abstract
Vinatier, J., Herzog, E., Plamont, M.A., Wojcik, S.M., Schmidt, A., Brose, N., Daviet, L., El Mestikawy, S. and Giros, B.
Interaction between the vesicular glutamate transporter type 1 and endophilin A1, a protein essential for endocytosis.
J Neurochem., 97, 1111-1125, 2006.
Free Full Text
Modregger J, Schmidt A.A. Ritter B, Huttner W.B, and Plomann M.
Characterization of endophilin B1b, a brain-specific membrane-associated lysophosphatidic acid acyl transferase with properties distinct from endophilin A1.
J. Biol. Chem. 278 ; 6, 4160-4167, 2003.
Abstract
Guichet A, Wucherpfennig T., Dudu V., Etter S., Wilsch-Bräuniger M., Hellwig A., González-Gaitán M., Huttner W.B. and Schmidt A.A.
Essential role of endophilin A in synaptic vesicle budding at the Drosophila neuromuscular junction,
EMBO J., 21, pp. 1661-1672, 2002.
Free Full Text
Schmidt A.A., M. Wolde, C. Thiele, W. Fest, H. Kratzin, A. V. Podtelejnikov, W. Witke, W. B. Huttner, and H.-D. Söling.
Endophilin I mediates synaptic vesicle formation by transfer of arachidonate to lysophosphatidic acid.
Nature, 401, 133-141, 1999.
Free Full Text
Last modified 03/12/2012
