PLASMODIUM CDPKS

Regulatory roles of calcium-dependent protein kinases in the Plasmodium life cycle

Coordinatore	IMPERIAL COLLEGE OF SCIENCE, TECHNOLOGY AND MEDICINE    more  Organization address address: SOUTH KENSINGTON CAMPUS EXHIBITION ROAD city: LONDON postcode: SW7 2AZ contact info Titolo: Ms. Nome: Brooke Cognome: Alasya Email: send email Telefono: +44 20 7594 1181 Fax: +44 20 7594 1219
Nazionalità Coordinatore	United Kingdom [UK]
Totale costo	168˙823 €
EC contributo	168˙823 €
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-2007-2-1-IEF
Funding Scheme	MC-IEF
Anno di inizio	2008
Periodo (anno-mese-giorno)	2008-10-01   -   2010-09-30

 Partecipanti

#	participant	country	role	EC contrib. [€]
1	IMPERIAL COLLEGE OF SCIENCE, TECHNOLOGY AND MEDICINE  Organization address address: SOUTH KENSINGTON CAMPUS EXHIBITION ROAD city: LONDON postcode: SW7 2AZ contact info Titolo: Ms. Nome: Brooke Cognome: Alasya Email: send email Telefono: +44 20 7594 1181 Fax: +44 20 7594 1219	UK (LONDON)	coordinator	0.00

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 Obiettivo del progetto (Objective)

'The aim of the proposed project is a characterization of a set of unique and understudied kinases that have essential functions in Apicomplexan life cycle control. These kinases, which interestingly are only found in plants and protists and not in animals or fungi, are calcium-dependent and are thought to allow for a translation of intra- or extracellular Ca2 signals into an appropriate cellular response. The specific objectives of this proposal are (1) functional studies of two Plasmodium calcium-dependent protein kinases (CDPK1 and CDPK5) to elucidate their regulatory role in the Plasmodium life cycle, and (2) to validate these proteins as essential signaling molecules that can serve as drug targets in an attempt to effectively treat Plasmodium infection/malaria. Our proposed studies involve the construction of transgenic parasites that express epitope-tagged copies of CDPK1 and CDPK5, as well as state-of-the-art conditional knock-out and chemical genetics approaches to investigate the biological function of these proteins. In addition, a collaboration with the biophysics laboratory of Professor Jane Endicott at the University of Oxford is proposed, to produce crystallized protein for structural analysis.'