CILITRANSPORT

Structural Studies and Regulation of Intraflagellar Transport Complexes

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	1˙498˙650 €
EC contributo	1˙498˙650 €
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-StG_20111109
Funding Scheme	ERC-SG
Anno di inizio	2012
Periodo (anno-mese-giorno)	2012-09-01   -   2017-08-31

 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 Fax: +49 89 85783174	DE (MUENCHEN)	hostInstitution	1˙498˙650.00
2	MAX PLANCK GESELLSCHAFT ZUR FOERDERUNG DER WISSENSCHAFTEN E.V.  Organization address address: Hofgartenstrasse 8 city: MUENCHEN postcode: 80539 contact info Titolo: Dr. Nome: Esben Cognome: Lorentzen Email: send email Telefono: +49 89 8578 3479	DE (MUENCHEN)	hostInstitution	1˙498˙650.00

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 Obiettivo del progetto (Objective)

'The cilium is an organelle that protrudes from the cell body and is responsible for the motility of unicellular organisms and of vertebrate cell types such as sperm cells. In addition, most vertebrate cells have primary non-motile cilia important for sensory reception and signalling. The assembly and function of cilia rely on intraflagellar transport (IFT), the bi-directional movement of macromolecules between the cell body and the cilium. As cilia do not contain ribosomes, IFT is required to move the approximately 600 different ciliary proteins from their site of synthesis in the cell body to their site of function in the cilium. IFT is powered by kinesin and dynein motors, which move cargoes along the microtubule-based axoneme of the cilium. The interaction between motors and cargoes is mediated by the IFT complex, a 1.6 MDa complex formed by 20 different proteins. Despite the importance of the IFT complex, very little is known about its architecture and how it is regulated. In this proposal, we want to address both aspects using a combination of structural and functional studies. The structural analysis of the IFT complex is daunting given its size and complexity. We are proceeding with the biochemical reconstitution of the core subcomplexes, which we plan to analyze using X-ray crystallography and electron microscopy. To date, we have solved the X-ray structure of a dimeric complex between an IFT GTPase and its binding factor, and have reconstituted one of the two core complexes (the 8-subunit IFT-B complex) in amounts and purity suitable for structural studies. While these studies are progressing, we plan to use similar approaches to tackle the other core complex (IFT-A) and the plethora of ciliary GTPases, with the ambitious goal of understanding the architecture and regulation of the the entire IFT complex. This will shed light on the molecular basis of ciliogenesis and the pathological consequences of its disruption.'