An extracellular RRR motif flanking the M1 transmembrane domain governs the biogenesis of homomeric neuronal nicotinic acetylcholine receptors

作者：Alves Daiane S; Castello Banyuls Juan; Faura Clara C; Ballesta Juan J^*

来源：FEBS Letters, 2011, 585(8): 1169-1174.

DOI：10.1016/j.febslet.2011.03.028

• Nicotinic acetylcholine receptor
• Protein folding
• Protein assembly

We have previously demonstrated that the highly conserved R209, that flanks the M1 transmembrane segment of nicotinic acetylcholine (ACh) receptors, is required for the transport of assembled homomeric neuronal alpha 7 nicotinic ACh receptors to the cell surface. In the present paper we show that basic residues at positions 208 and 210 are necessary for the assembly of alpha 7 receptors. On the contrary, a basic residue at position 210 of alpha 3 subunit decreases the assembly of heteromeric neuronal alpha 3 beta 4 nicotinic ACh receptors. A basic residue at position 210 of the beta 4 subunit slightly decreases alpha 3 beta 4 receptor expression. We conclude that a pre-M1 RRR motif is necessary for the biogenesis of homomeric alpha-bungarotoxin-sensitive neuronal alpha 7 nicotinic ACh receptors.

• 出版日期2011-4-20