Sophia-Antipolis

MDSC-bioinfo

Acronyme ou nom de la structure: 
Nom complet (en toutes lettres): 
équipe de bio-informatique du pôle MDSC de l'I3S
Adresse: 
Laboratoire d'Informatique, Signaux et Systèmes de Sophia Antipolis
SFBI: 
0

ABS

Acronyme ou nom de la structure: 
Nom complet (en toutes lettres): 
Algorithms-Biology-Structure
SFBI: 
0

DMMP

Acronyme ou nom de la structure: 
Nom complet (en toutes lettres): 
Dynamique des membranes et manteaux protéiques
Adresse: 
Institut de Pharmacologie Moléculaire et Cellulaire (IPMC) 660 Route des Lucioles SOPHIA ANTIPOLIS 06560 VALBONNE
Téléphone: 
04 93 95 77 69
Fax: 
04 93 95 77 08
Description (English): 

Various proteins remodel the membranes of organelles involved in intracellular transport. Protein coats deform membranes to promote the budding of vesicles. Golgins, sort of molecular strings, tether vesicles to restrict their diffusion. Lipid transporters adjust the membrane composition. Although very different, most of these mechanisms are controlled by small G proteins of the Arf family and by the physical chemistry of membranes.

We study these mechanisms through molecular, cellular and in silico approaches. With original assays based on fluorescence and light scattering, we follow elementary reactions such as the assembly cycle of protein coats, the tethering of liposomes by a golgin or the transfer of lipids. With fluorescence light microscopy and electron microscopy, we visualize these events in cells and in reconstituted systems. With molecular dynamics, we describe at the atomic level how specific protein motifs sense the chemistry and curvature of lipid membranes.

Recent Findings:

- Intracellular transport of cholesterol through the counter exchange of a phosphoinositide and its hydrolysis.
- Phospholipids with omega 3 acyl chains boost membrane deformation and fission
- Atomic description of the packing of lipids in membranes of various curvature and composition

HELIQUEST: a bioinformatics tools to analyze amphipathic helices with specific properties and search for sequences with similar properties (amino-acid composition, hydrophobic moment...).

Plate-forme: 
0
SFBI: 
Membre de la SFBI
Adhésion morale: 
0
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