CHEMBIO_ATG

Chemical biology of autophagy

 Coordinatore AGENCIA ESTATAL CONSEJO SUPERIOR DE INVESTIGACIONES CIENTIFICAS 

 Organization address address: CALLE SERRANO 117
city: MADRID
postcode: 28006

contact info
Titolo: Ms.
Nome: Ana Maria
Cognome: De La Fuente
Email: send email
Telefono: 34915681709

 Nazionalità Coordinatore Spain [ES]
 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-2012-CIG
 Funding Scheme MC-CIG
 Anno di inizio 2014
 Periodo (anno-mese-giorno) 2014-01-01   -   2017-12-31

 Partecipanti

# participant  country  role  EC contrib. [€] 
1    AGENCIA ESTATAL CONSEJO SUPERIOR DE INVESTIGACIONES CIENTIFICAS

 Organization address address: CALLE SERRANO 117
city: MADRID
postcode: 28006

contact info
Titolo: Ms.
Nome: Ana Maria
Cognome: De La Fuente
Email: send email
Telefono: 34915681709

ES (MADRID) coordinator 100˙000.00

Mappa


 Word cloud

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autophagy    proteins    mechanism    autophagosome    tools    regulating    lc    recycling    degradation    membrane    lysosome    soluble    phagophore    generation    characterization   

 Obiettivo del progetto (Objective)

'Autophagy is a cellular pathway that regulates the degradation and recycling of proteins and organelles. This mechanism is initiated with the formation of a phagophore, a cup-shaped double membrane that engulfs the cytoplasmic material to be degraded. The phagophore is then elongated and sealed to generate an autophagosome that will be fused with a lysosome, thereby delivering the cargo for degradation. Several ubiquitin-like proteins have been shown to have a crucial role in regulating autophagosome generation and its fusion with the lysosome. One of these proteins is LC3-I, is a soluble cytosolic protein that associates with the autophagosome after C-terminal conjugation to a phosphatidylethanolamine unit (LC3-II). This membrane association is reversibly modulated by the cysteine protease atg4, which deconjugates PE from LC3-II, thus recycling the soluble LC3-I. Detailed studies of the molecular mechanism regulating autophagosome formation and the role of LC3-I and LC3-II are unknown, mainly due to the lack of tools enabling a profound characterization of these processes. Herein, we propose the generation of semisynthetic lipidated LC3 proteins using a chemical biology approach. The fully modified proteins should be unvaluable tools that will contribute to the characterization of the factors regulating autophagy.'

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