MITOFUSION

Dissecting the discrete steps of mitochondrial fusion

 Coordinatore CENTRE NATIONAL DE LA RECHERCHE SCIENTIFIQUE 

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

contact info
Titolo: Ms.
Nome: Liliane
Cognome: Flabbée
Email: send email
Telefono: +33 1 42 34 94 19
Fax: +33 1 42 34 95 08

 Nazionalità Coordinatore France [FR]
 Totale costo 100˙000 €
 EC contributo 100˙000 €
 Programma FP7-PEOPLE
Specific programme "People" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)
 Code Call FP7-PEOPLE-2010-RG
 Funding Scheme MC-IRG
 Anno di inizio 2011
 Periodo (anno-mese-giorno) 2011-04-01   -   2015-03-31

 Partecipanti

# participant  country  role  EC contrib. [€] 
1    CENTRE NATIONAL DE LA RECHERCHE SCIENTIFIQUE

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

contact info
Titolo: Ms.
Nome: Liliane
Cognome: Flabbée
Email: send email
Telefono: +33 1 42 34 94 19
Fax: +33 1 42 34 95 08

FR (PARIS) coordinator 100˙000.00

Mappa


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directly    organelles    inner    ubiquitin    elucidating    gtpases    underlying    fusion    mitochondrial    proteasome    network    outer    membranes   

 Obiettivo del progetto (Objective)

'Mitochondria are not single isolated organelles but constitute a real network comparable to the Endoplasmic Reticulum or the Golgi apparatus. In wild type conditions, this network adopts a tubular morphology that is conditioned by active and constant processes of fission and fusion of mitochondrial membranes. Unlike other organelles, fusion of mitochondrial membranes is not catalyzed by SNAREs but involves two sets of large GTPases, the mitofusins and OPA/Mgm1, involved in fusion of outer and inner membranes, respectively. Consequently, these GTPases not only participate in transmission of mitochondrial DNA and therefore oxidative phosphorylation but also play a major role in apoptosis. In addition, impairment of mitochondrial fusion is directly linked to several neurodegenerative syndromes such as Parkinson and Charcot-Marie Tooth diseases as well as Dominant Optic Atrophy. The importance of elucidating the mechanism underlying mitochondrial fusion therefore becomes evident. We have previously shown that Fzo1, the yeast mitofusin, is subject to exquisite regulation by the Ubiquitin-Proteasome System. Based on this, we will aim at dissecting the involvement of the ubiquitin-proteasome system in movement, tethering and fusion of outer and inner membranes. To reach this goal, multidisciplinary in vivo and in vitro approaches will be employed, including genetics, biochemistry and cell biology imaging techniques. Besides elucidating molecular mechanisms underlying mitochondrial fusion, the present project is likely to generate concepts that may apply to all membrane fusion events within eukaryotic cells. Contributions to understanding of neuropathies directly caused by defects of mitochondrial dynamics are also to be expected.'

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