MITOFUSIN-PD

Regulation of mitochondria-endoplasmic reticulum tethering by Parkin: implication for Parkinson’s disease

 Coordinatore UNIVERSITE DE GENEVE 

 Organization address address: Rue du General Dufour 24
city: GENEVE
postcode: 1211

contact info
Titolo: Prof.
Nome: Luca
Cognome: Scorrano
Email: send email
Telefono: 41223795235

 Nazionalità Coordinatore Switzerland [CH]
 Totale costo 178˙101 €
 EC contributo 178˙101 €
 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-IEF
 Funding Scheme MC-IEF
 Anno di inizio 2012
 Periodo (anno-mese-giorno) 2012-03-01   -   2014-02-28

 Partecipanti

# participant  country  role  EC contrib. [€] 
1    UNIVERSITE DE GENEVE

 Organization address address: Rue du General Dufour 24
city: GENEVE
postcode: 1211

contact info
Titolo: Prof.
Nome: Luca
Cognome: Scorrano
Email: send email
Telefono: 41223795235

CH (GENEVE) coordinator 178˙101.60

Mappa


 Word cloud

Esplora la "nuvola delle parole (Word Cloud) per avere un'idea di massima del progetto.

death    parkin    ubiquitination    ca    mitochondria    mfn    fusion    regulating    er    dependent    tethering   

 Obiettivo del progetto (Objective)

'Parkin, an E3 ubiquitin ligase and a Parkinsons's disease related gene, translocates to impaired mitochondria upon mitochondria intoxication and drives their elimination via autophagy, a process known as mitophagy. Mitochondrial pro-fusion protein Mitofusin (Mfn) was found to be a target for Parkin mediated ubiquitination. In absence of Parkin, Mfn fails to be ubiquitinated, thus accumulates in the mitochondria, leading to increased mitochondria fusion. The host laboratory discovered that Mfn2 has an additional role in tethering mitochondria to endoplasmic reticulum (ER), a structural feature essential for Ca2 transfer between the organelles and Ca2 dependent cell death. This project hypothesizes that Parkin dependent ubiquitination of Mfn is crucial in regulating mitochondria-ER tethering and neuronal survival. We therefore aim to (i) address whether impairment of Parkin-dependent Mfn ubiquitination affects mitochondria-ER tethering and death by Ca2-dependent stimuli; (ii) identify a potential Deubiquitinase (DUB) enzyme opposing Parkin activity in the regulation of Mfn ubiquitination; iii) identify novel interactors of the PINK1/Parkin pathway, regulating Parkin translocation to mitochondria and therefore Mfn steady-state levels. This project will therefore clarify if ER-mitochondria tethering participates in the neurodegenerative pathways controlled by Parkin'

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