INVESTIGADORES
ROSSI Juan Pablo Francisco
artículos
Título:
3. Diving Into the Lipid Bilayer to Investigate the Transmembrane Organization and Conformational State Transitions of P-type Ion ATPases
Autor/es:
IRENE C. MANGIALAVORI, ARIEL J. CARIDE, ROLANDO C. ROSSI, JUAN PABLO F.C. ROSSI*, AND EMANUEL E. STREHLER*
Revista:
CURRENT CHEMICAL BIOLOGY
Editorial:
BENTHAM
Referencias:
Año: 2011 vol. 5 p. 118 - 129
ISSN:
1872-3136
Resumen:
Abstract: Although membrane proteins constitute more than 20% of the total proteins, the structures of only a few areknown in detail. An important group of integral membrane proteins are ion-transporting ATPases of the P-type family,which share the formation of an acid-stable phosphorylated intermediate as part of their reaction cycle. There are severalcrystal structures of the sarcoplasmic reticulum Ca2+ pump (SERCA) revealing different conformations, and recently,crystal structures of the H+-ATPase and the Na+/K+-ATPase were reported as well. However, there are no atomic resolutionstructures for other P-type ATPases including the plasma membrane calcium pump (PMCA), which is integral to cellularCa2+ signaling. Crystallization of these proteins is challenging because there is often no natural source from whichthe protein can be obtained in large quantities, and the presence of multiple isoforms in the same tissue further complicatesefforts to obtain homogeneous samples suitable for crystallization. Alternative techniques to study structural aspectsand conformational transitions in the PMCAs (and other P-type ATPases) have therefore been developed. Specifically, informationabout the structure and assembly of the transmembrane domain of an integral membrane protein can be obtainedfrom an analysis of the lipidprotein interactions. Here, we review recent efforts using different hydrophobicphoto-labeling methods to study the non-covalent interactions between the PMCA and surrounding phospholipids underdifferent experimental conditions, and discuss how the use of these lipid probes can reveal valuable information on themembrane organization and conformational state transitions in the PMCA, Na+/K+-ATPase, and other P-type ATPases.
