Nature Neuroscience5, 963 - 970 (2002)
Published online: 9 September 2002; | doi:10.1038/nn918
A transmembrane motif governs the surface trafficking of nicotinic acetylcholine receptors
Jun-Mei Wang, Lili Zhang, Yun Yao, Nitnara Viroonchatapan, Elizabeth Rothe
& Zuo-Zhong Wang
Department of Neurobiology, University of Pittsburgh School of Medicine, 3500 Terrace Street, Pittsburgh, Pennsylvania 15261, USA
Correspondence should be addressed to Zuo-Zhong Wang zzwang+@pitt.edu
Surface expression of the nicotinic acetylcholine receptor (AChR) requires the assembly of multiple subunits in the endoplasmic reticulum (ER). Little is known, however, about the mechanism by which assembled receptor pentamers are transported to the cell membrane while unassembled subunits are retained in the ER. Here we report that a motif conserved in the transmembrane domain of AChR subunits is critically involved in this process. In COS cells, mutation within this signal allowed surface expression of unassembled subunits. Conversely, insertion of the sequence to unrelated proteins that are normally transported to the surface resulted in ER retention. The signal is buried in AChR pentamers, but is exposed on unassembled subunits in the ER, where it promotes protein degradation. We therefore conclude that this signal ensures surface trafficking of only functional AChRs.
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