P-TYPE ATPASES

Structural studies of P-type ATPases and their characterization in native membranes

Coordinatore	AARHUS UNIVERSITET    more  Organization address address: Nordre Ringgade 1 city: AARHUS C postcode: 8000 contact info Titolo: Prof. Nome: Poul Cognome: Nissen Email: send email Telefono: -13922 Fax: -11745
Nazionalità Coordinatore	Denmark [DK]
Totale costo	203˙817 €
EC contributo	203˙817 €
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-IEF-2008
Funding Scheme	MC-IEF
Anno di inizio	2009
Periodo (anno-mese-giorno)	2009-04-01   -   2009-12-31

 Partecipanti

#	participant	country	role	EC contrib. [€]
1	AARHUS UNIVERSITET  Organization address address: Nordre Ringgade 1 city: AARHUS C postcode: 8000 contact info Titolo: Prof. Nome: Poul Cognome: Nissen Email: send email Telefono: -13922 Fax: -11745	DK (AARHUS C)	coordinator	203˙817.53

Mappa

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 Obiettivo del progetto (Objective)

'P-type ATPases are cell-membrane pumps that are of fundamental importance in eukaryotes. The ion gradients created by Ca2-ATPases or Na,K-ATPases are involved in signalling, maintaining the membrane potential as well as secondary active transport. Despite the recent progress in membrane protein crystallography, the lack of detailed structural information currently prevents a better understanding of function and specificity of cation pumps. One specific aim of this proposed research is to determine the structure of the plasma-membrane Ca2-ATPase (PMCA) and to understand its regulatory mechanism. The autoinhibited PMCA will be recombinantly expressed in yeast, purified and crystallized. In addition, it is also planned to determine the structure of the activated complex consisting of PMCA and calcium-bound calmodulin (Ca2-CaM). In order to deepen our understanding of cation pumps in their native environment, I further propose to investigate Na,K-ATPases in native membranes using a multi-technique approach. First, I will analyze complexes of Na,K-ATPase isolated from native membranes by mass spectrometry to identify peripheral proteins. In the next step, I plan to assemble those identified multi-protein complexes in vitro and structurally characterize them by cryo-EM. Finally, I plan to use AFM to investigate the oligomeric arrangement of Na,K-ATPases in native membranes. This multi-disciplinary project will hopefully expand our knowledge of cation pumps by putting atomic details in the context of the native environment and will concurrently allow me to gain experience in membrane protein crystallography that will complement my expertise in biophysical methods.'