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| Content Provider | Journal of Biological Chemistry (JBC) |
|---|---|
| Author | Keller, Steven H. Lindstrom, Jon Ellisman, Mark Taylor, Palmer |
| Abstract | The nicotinic acetylcholine receptor in muscle is a ligand-gated ion channel with an ordered subunit arrangement of α-γ-α-δ-β. The subunits are sequestered in the endoplasmic reticulum (ER) and assembled into the pentameric arrangement prior to their exit to the cell surface. Mutating the Arg313–Lys314 sequence in the large cytoplasmic loop of the α-subunit to K314Q promotes the trafficking of the mutant unassembled α-subunit from the ER to the Golgi in transfected HEK cells, identifying an important determinant that modulates the ER to Golgi trafficking of the subunit. The association of the K314Q α-subunit with γ-COP, a component of COP I coats implicated in Golgi to ER anterograde transport, is diminished to a level comparable to that observed for wild-type α-subunits when co-expressed with the β-, δ-, and γ-subunits. This suggests that the Arg313–Lys314 sequence is masked when the subunits assemble, thereby enabling ER to Golgi trafficking of the α-subunit. Although unassembled K314Q α-subunits accumulate in the Golgi, they are not detected at the cell surface, suggesting that a second post-Golgi level of capture exists. Expressing the K314Q α-subunit in the absence of the other subunits in ubiquitinating deficient cells (ts20) results in detecting this subunit at the cell surface, indicating that ubiquitination functions as a post-Golgi modulator of trafficking. Taken together, our findings support the hypothesis that subunit assembly sterically occludes the trafficking signals and ubiquitination at specific sites. Following the masking of these signals, the assembled ion channel expresses at the cell surface. |
| Related Links | http://www.jbc.org/content/276/21/18384.abstract |
| Ending Page | 18391 |
| Starting Page | 18384 |
| Page Count | 8 |
| File Format | HTM / HTML PDF |
| ISSN | 00219258 |
| Journal | Journal of Biological Chemistry (JBC) |
| Issue Number | 21 |
| Volume Number | 276 |
| DOI | 10.1074/jbc.M100691200 |
| e-ISSN | 1083351X |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology |
| Publisher Date | 2001-05-25 |
| Access Restriction | Open |
| Subject Keyword | Nicotinic acetylcholine receptors (nAchR) Endoplasmic reticulum (ER) Phosphate-buffered saline (PBS) Fluorescein isothiocyanate (FITC) Monoclonal antibody (mAb) Green fluorescent protein (GFP) Endo-β-N-acetylglucosaminidase H (Endo-H) MEMBRANE TRANSPORT STRUCTURE FUNCTION AND BIOGENESIS |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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