MICROTUBULE PLUS END

Structural and kinetic basis of evolutionary conserved and divergent microtubule plus end tracking mechanisms

Coordinatore	CANCER RESEARCH UK    more  Organization address address: ST JOHN STREET 407 ANGEL BUILDING city: LONDON postcode: EC1V 4AD contact info Titolo: Ms. Nome: Holly Cognome: Elphinstone Email: send email Telefono: +44 207 269 3524 Fax: +44 207 269 3585
Nazionalità Coordinatore	United Kingdom [UK]
Totale costo	172˙240 €
EC contributo	172˙240 €
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-2009-IEF
Funding Scheme	MC-IEF
Anno di inizio	2011
Periodo (anno-mese-giorno)	2011-01-01   -   2012-12-31

 Partecipanti

#	participant	country	role	EC contrib. [€]
1	CANCER RESEARCH UK  Organization address address: ST JOHN STREET 407 ANGEL BUILDING city: LONDON postcode: EC1V 4AD contact info Titolo: Ms. Nome: Holly Cognome: Elphinstone Email: send email Telefono: +44 207 269 3524 Fax: +44 207 269 3585	UK (LONDON)	coordinator	172˙240.80

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 Obiettivo del progetto (Objective)

'In eukaryotic cells the microtubule (MT) cytoskeleton is of crucial importance for many essential cellular functions. The determination of cell morphology, intracellular transport, chromosome segregation in mitosis, and cell motility belong to the processes carried out by MTs. Aberrant cell morphology, developmental diseases and promotion of malignant transformations in animal cells are results of failures in these processes. The dynamically growing plus end of MTs is of special interest as it serves as a cellular hub integrating signals needed to regulate the MT cytoskeleton and its functions. Due to the plus end’s highly dynamic nature and the complexity of protein-protein interactions at the end, it is still unclear which structural transitions take place at microtubule ends and which structures are recognized by regulatory proteins that bind the growing ends selectively. This project aims at a mechanistic understanding of selective targeting of specialized proteins to microtubule ends that exhibit diverse functions there. Two layers of interactions at microtubule ends are addressed in this proposal: (1) We aim to elucidate the molecular origin for the conserved property of end binding proteins (EBs) to bind autonomously to the growing microtubule plus end region, which provides a dynamic platform for second-layer binding of more divergent proteins. (2) We aim to understand the logics underlying the less conserved interactions of these other microtubule associated proteins (MAPs) with EB-decorated MT ends. These two layers of the MT plus-end binding protein interaction network will be analyzed by a concerted, multidisciplinary experimental approach combining in vitro and in vivo experiments, using quantitative fluorescence microscopy to measure the dynamics of MT end tracking and electron microscopy to gain insight into the structural origin of function.'