Abstract
Here we describe an approach to investigate di- or oligomerization
of transmembrane receptors in living cells with fluorescence recovery
after photobleaching (FRAP). We immobilized a defined fraction of
receptors with antibodies and then measured lateral mobility of the
nonimmobilized fraction by FRAP. We validated this approach with
CD86 and CD28 as monomeric and dimeric reference proteins, respectively.
Di- or oligomerization of G protein-coupled receptors is strongly
debated. We studied human beta-adrenergic receptors as prototypical
G protein-coupled receptors and found that beta(1)-AR shows transient
interactions whereas beta(2)-AR can form stable oligomers. We propose
that this FRAP method can be widely applied to study di- or oligomerization
of cell-surface proteins.
Users
Please
log in to take part in the discussion (add own reviews or comments).