Structures of the FXYD regulatory proteins in lipid micelles and membranes. J Bioenerg Biomembr 2007 Dec;39(5-6):379-83
Date
11/15/2007Pubmed ID
18000745Pubmed Central ID
PMC2917602DOI
10.1007/s10863-007-9105-yScopus ID
2-s2.0-38349140152 (requires institutional sign-in at Scopus site) 25 CitationsAbstract
The FXYD membrane proteins constitute a family of conserved auxiliary subunits of the Na,K-ATPase, and have been the focus of recent attention due to their ability to finely regulate the activity of the enzyme complex in various physiological settings. In this review we describe the structures of the proteins, as well as their dynamics and their associations with the lipid bilayer membrane, which we have recently determined by NMR spectroscopy. Although the proteins are relatively small, their genes contain as many as six to nine small exons, and the coincidence of structured protein segments with their genetic elements suggests assembly from discrete structural modules through exon shuffling. The three-dimensional structures and backbone dynamics provide the foundation for understanding their intra-membrane association with the Na,K-ATPase alpha subunit, and the structure of FXYD1 suggests a mechanism whereby the phosphorylation of conserved Ser residues, by protein kinases A and C, could induce a conformational change in the cytoplasmic domain of the protein, to modulate its interaction with the alpha subunit.
Author List
Franzin CM, Gong XM, Teriete P, Marassi FMAuthor
Francesca M. Marassi PhD Chair, Professor in the Biophysics department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
AnimalsCell Membrane
Humans
Intracellular Signaling Peptides and Proteins
Lipids
Membrane Proteins
Mice
Micelles
Neoplasm Proteins
Phosphoproteins
Potassium Channels
Protein Subunits
Rats
Sodium-Potassium-Exchanging ATPase
