CHEMBIO_ATG

Chemical biology of autophagy

Coordinatore	AGENCIA ESTATAL CONSEJO SUPERIOR DE INVESTIGACIONES CIENTIFICAS    more  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

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 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.'