Abstract
The intracellular domains of the α4 and β2 neuronal nicotinic subunits between transmembrane segments 3 and 4 contain a number of predicted phosphorylation sites but there is no direct evidence that any of these sites are actually phosphorylated in vivo. We expressed rat α4β2 nicotinic receptors in Xenopus oocytes, labeled them by an overnight incubation in [ 32 P ]orthophosphate, and analyzed the immunoprecipitated receptors by autoradiography and Western blotting. Our results show that the oocytes contained three kinds of α4 subunits with apparent weights of 69, 79, and 89 kDa. The 89 kDa α4 subunit was the most heavily phosphorylated.
Full Text
Published Version
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call