Rapsyn, a 43-kDa protein on the cytoplasmic face of the postsynaptic m
embrane, is essential for clustering acetylcholine receptors (AChR) at
the neuromuscular junction. When transfected into nonmuscle cells (QT
-6), rapsyn forms discrete membrane domains and can cluster AChR into
these same domains. Here we examined whether rapsyn can cluster other
ion channels as well, When expressed in QT-6 cells, the GABA(A) recept
or (human alpha 1, beta 1, and gamma 2 subunits) and the skeletal musc
le sodium channel were each diffusely scattered across the cell surfac
e. Rapsyn, when co-expressed, clustered the GABAA receptor as effectiv
ely as it clustered AChR in previous studies. Rapsyn did not cluster c
o-transfected sodium channel, confirming that it does not cluster ion
channels indiscriminately. Rapsyn mRNA was detected at low levels in t
he brain by polymerase chain reaction amplification of reverse-transcr
ibed RNA, raising the possibility of a broader role for rapsyn.