Membrane Dynamics and Regulation

Program: Cell Biology

Group Leader: Anne SCHMIDT

Tel.: +33 (0)157278012
schmidt.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.

1figure1 41730

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domain of a BAR domain-containing protein (unpublished).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.
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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.
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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.
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Last modified 03/12/2012

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