| First Author | Wang ZZ | Year | 1996 |
| Journal | J Biol Chem | Volume | 271 |
| Issue | 44 | Pages | 27575-84 |
| PubMed ID | 8910344 | Mgi Jnum | J:36498 |
| Mgi Id | MGI:83925 | Doi | 10.1074/jbc.271.44.27575 |
| Citation | Wang ZZ, et al. (1996) Assembly of the nicotinic acetylcholine receptor. The first transmembrane domains of truncated alpha and delta subunits are required for heterodimer formation in vivo. J Biol Chem 271(44):27575-84 |
| abstractText | To investigate the mechanism of assembly of the mouse muscle acetylcholine receptor, we have expressed truncated N-terminal fragments of the alpha and delta subunits in COS cells and have examined their ability to fold, to associate into heterodimers, and to form a ligand-binding site. Truncated fragments of the alpha subunit that include all, part, or none of the first transmembrane domain (M1) folded to acquire alpha-bungarotoxin binding activity. Neither the full-length alpha subunit nor any of the fragments were expressed on the cell surface, although the shortest folded fragment lacking a transmembrane domain was secreted into the medium. When coexpressed with the delta subunit, the alpha subunit fragment possessing M1 formed a heterodimer containing a ligand-binding site, but shorter fragments, which lack transmembrane segments, did not associate with the delta subunit. N-terminal delta subunit fragments gave similar results. An N-terminal delta subunit fragment that contains M1 associated with the alpha subunit to form a heterodimer, while a fragment lacking M1 did not. These results show that a complete M1 domain is necessary for association of truncated N-terminal alpha and delta subunits into a heterodimer with high affinity ligand binding activity. |
