SIGNAL2THEHUB

Integrin: signalling from the tail and the hub

Coordinatore	MAX PLANCK GESELLSCHAFT ZUR FOERDERUNG DER WISSENSCHAFTEN E.V.    more Spiacenti, non ci sono informazioni su questo coordinatore. Contattare Fabio per maggiori infomrazioni, grazie.
Nazionalità Coordinatore	Germany [DE]
Totale costo	2˙462˙689 €
EC contributo	2˙462˙689 €
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-2012-ADG_20120314
Funding Scheme	ERC-AG
Anno di inizio	2013
Periodo (anno-mese-giorno)	2013-03-01   -   2018-02-28

 Partecipanti

#	participant	country	role	EC contrib. [€]
1	MAX PLANCK GESELLSCHAFT ZUR FOERDERUNG DER WISSENSCHAFTEN E.V.  Organization address address: Hofgartenstrasse 8 city: MUENCHEN postcode: 80539 contact info Titolo: Dr. Nome: Anne Katrin Cognome: Werenskiold Email: send email Telefono: +49 89 85782601	DE (MUENCHEN)	hostInstitution	2˙462˙689.00
2	MAX PLANCK GESELLSCHAFT ZUR FOERDERUNG DER WISSENSCHAFTEN E.V.  Organization address address: Hofgartenstrasse 8 city: MUENCHEN postcode: 80539 contact info Titolo: Prof. Nome: Reinhard Cognome: Fässler Email: send email Telefono: +49 89 8578 2072 Fax: +49 89 8578 2422	DE (MUENCHEN)	hostInstitution	2˙462˙689.00

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 Obiettivo del progetto (Objective)

'Integrin-mediated cell adhesion is essential for the development and homeostasis of multicellular organisms. Integrins are ubiquitously expressed heterodimeric adhesion receptors consisting of α and β subunits. They exhibit two striking properties; they can regulate their affinity for ligands and assemble large signalling hubs called adhesomes. Both properties depend on the α and β cytoplasmic tails; when integrins switch from inactive to active conformations their weakly associated tails separate and recruit adhesion proteins leading to adhesome assembly. How active integrins revert to the inactive state, and how the weak α/β tail association is maintained is largely unknown. The mechanistic contribution of individual integrin classes to the recruitment of proteins to the adhesome and how adhesome signalling is induced is also unclear. In this proposal we will address these fundamental questions in 4 specific aims. In the first aim we will identify proteins that keep integrin tails associated and define the roles of their tail binding with respect to integrin inactivation and turn over. In the second aim we will utilize high-resolution quantitative mass spectrometry to define how different integrins assemble adhesomes with common and specific components that signal in highly regulated manners. Our third aim will determine how integrin tails nucleate an adhesion complex that expedites further interactions with multiple binding partners by performing crosslinking proteomics of adhesion proteins bound to different β integrin tails in vitro. In the fourth aim we will use genetically engineered mice to determine how ubiquitously expressed proteins of the adhesome perform organ- and cell type-specific functions. Completion of these aims will help define the fundamental mechanisms whereby integrins control their complex signalling networks. This has implications for our understanding of development and disease as integrins play key roles for almost all cellular functions.'