Surface plasmon resonance spectroscopy in the study of membrane-mediated cell signalling.
Peptide-membrane interactions contribute to many important biological processes such as cellular signaling, protein trafficking and ion-channel formation. During receptor-mediated signalling, activated intracellular signalling molecules are often recruited into receptor-induced signaling complexes at the cytoplasmic surface of the cell membrane. Such recruitment can depend upon protein-protein and protein-lipid interactions as well as protein acylation. A wide variety of biophysical techniques have been combined with the use of model membrane systems to study these interactions and have provided important information on the relationship between the structure of these proteins involved in cell signalling and their biological function. More recently, surface plasmon resonance (SPR) spectroscopy has also been applied to the study of biomembrane-based systems using both planar mono- or bilayers or liposomes. This article provides an overview of these recent applications, which demonstrate the potential of SPR to enhance our molecular understanding of membrane-mediated cellular signalling.
Mozsolits
Henriette
H
Department of Biochemistry and Molecular Biology, PO Box 13D, Monash University, Clayton 3800, Victoria, Australia.
Thomas
Walter G
WG
Aguilar
Marie-Isabel
MI
D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism*; D007425:Intracellular Membranes / Q000737:chemistry / Q000378:metabolism; D008081:Liposomes / Q000737:chemistry / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D015398:Signal Transduction / Q000502:physiology*; D020349:Surface Plasmon Resonance / Q000379:methods*
D008081:Liposomes; D008565:Membrane Proteins