ARFMEMBRANESENSORS

Membrane sensors in the Arf orbit

 Coordinatore CENTRE NATIONAL DE LA RECHERCHE SCIENTIFIQUE 

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 Nazionalità Coordinatore France [FR]
 Totale costo 1˙997˙321 €
 EC contributo 1˙997˙321 €
 Programma FP7-IDEAS-ERC
Specific programme: "Ideas" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)
 Code Call ERC-2010-AdG_20100317
 Funding Scheme ERC-AG
 Anno di inizio 2011
 Periodo (anno-mese-giorno) 2011-05-01   -   2015-04-30

 Partecipanti

# participant  country  role  EC contrib. [€] 
1    INSTITUT NATIONAL DE LA SANTE ET DE LA RECHERCHE MEDICALE (INSERM)

 Organization address address: 101 Rue de Tolbiac
city: PARIS
postcode: 75654

contact info
Titolo: Ms.
Nome: Véronique
Cognome: Legros
Email: send email
Telefono: +33 491 827 015
Fax: +33 491 742 067

FR (PARIS) beneficiary 79˙395.60
2    CENTRE NATIONAL DE LA RECHERCHE SCIENTIFIQUE

 Organization address address: Rue Michel -Ange 3
city: PARIS
postcode: 75794

contact info
Titolo: Dr.
Nome: Bruno
Cognome: Antonny
Email: send email
Telefono: +33 4 93957775
Fax: +33 4 93957710

FR (PARIS) hostInstitution 1˙917˙925.40
3    CENTRE NATIONAL DE LA RECHERCHE SCIENTIFIQUE

 Organization address address: Rue Michel -Ange 3
city: PARIS
postcode: 75794

contact info
Titolo: Ms.
Nome: Béatrice
Cognome: Saint-Cricq
Email: send email
Telefono: +33 4 93 95 42 22
Fax: +33 4 92 96 03 39

FR (PARIS) hostInstitution 1˙917˙925.40

Mappa


 Word cloud

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small    proteins    motifs    lipid    helix    organize    polar    chemical    iquest    motif    sensors    molecular    physical    membrane    sequences    residues    alps    membranes   

 Obiettivo del progetto (Objective)

'Cellular organelles are continuously remodelled by numerous cytosolic proteins that associate transiently with their lipid membrane. Some distort the bilayer, others change its composition, extract lipids or bridge membranes at distance. Previous works from my laboratory have underlined the importance of membrane sensors, i.e. elements within proteins that help to organize membrane-remodelling events by sensing the physical and chemical state of the underlying membrane. A membrane sensor is not necessarily of well-folded domain that interacts with a specific lipid polar head: some intrinsically unfolded motifs harboring deceptively simple sequences can display remarkable membrane adhesive properties. Among these are some amphipathic helices: the ALPS motif with a polar face made mostly by small uncharged polar residues, the Spo20 helix with several histidines in its polar face and, like a mirror image of the ALPS motif, the alpha-synuclein helix with very small hydrophobic residues. Using biochemistry and molecular dynamics, we will compare the membrane binding properties of these sequences (effect of curvature, charge, lipid unsaturation); using bioinformatics we will look for new motifs, using cell biology we will assess the adaptation of these motifs to the physical and chemical features of organelle membranes. Concurrently, we will use reconstitution approaches on artificial membranes to dissect how membrane sensors contribute to the organization of vesicle tethering by golgins and sterol transport by ORP proteins. We surmise that the combination of a molecular ¿switch¿, a small G protein of the Arf family, and of membrane sensors permit to organize these complex reactions in time and in space.'

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