Transmembrane protein (perfringolysin o) association with ordered membrane domains (rafts) depends upon the raft-associating properties of protein-bound sterol.

ABSTRACT: Because transmembrane (TM) protein localization, or nonlocalization, in ordered membrane domains (rafts) is a key to understanding membrane domain function, it is important to define the origin of protein-raft interaction. One hypothesis is that a tight noncovalent attachment of TM proteins to lipids that have a strong affinity for ordered domains can be sufficient to induce raft-protein interaction. The sterol-binding protein perfringolysin O (PFO) was used to test this hypothesis. PFO binds both to sterols that tend to localize in ordered domains (e.g., cholesterol), and to those that do not (e.g., coprostanol), but it does not bind to epicholesterol, a raft-promoting 3α-OH sterol. Using a fluorescence resonance energy transfer assay in model membrane vesicles containing coexisting order

SUBMITTER: Lin Q 

PROVIDER: S-EPMC3882507 | biostudies-literature | 2013 Dec

REPOSITORIES: biostudies-literature