The α3β4 subtype is the predominant neuronal nicotinic acetylcholine receptor present in the sensory and autonomic ganglia and in a subpopulation of brain neurons. This subtype can form pentameric receptors with either 2 or 3 β4 subunits that have different pharmacologic and functional properties. To further investigate the role of the fifth subunit, we coexpressed a dimeric construct coding for a single polypeptide containing the β4 and α3 subunit sequences, with different monomeric subunits. With this strategy, which allowed the formation of single populations of receptors with unique stoichiometry, we demonstrated with immunofluorescence and biochemical and functional assays that only the receptors with 3 β4 subunits are efficiently expressed at the plasma membrane. Moreover, the LFM export motif of β4 subunit in the fifth position exerts a unique function in the regulation of the intracellular trafficking of the receptors, their exposure at the cell surface, and consequently, their function, whereas the same export motif present in the β4 subunits forming the acetylcholine binding site is dispensable.-Crespi, A., Plutino, S., Sciaccaluga, M., Righi, M., Borgese, N., Fucile, S., Gotti, C., Colombo, S. F. The fifth subunit in α3β4 nicotinic receptor is more than an accessory subunit.

The fifth subunit in α3β4 nicotinic receptor is more than an accessory subunit / Crespi, Arianna; Plutino, Simona; Sciaccaluga, Miriam; Righi, Marco; Borgese, Nica; Fucile, Sergio; Gotti, Cecilia; Colombo, Sara Francesca. - In: THE FASEB JOURNAL. - ISSN 0892-6638. - STAMPA. - 32:8(2018), pp. 4190-4202. [10.1096/fj.201701377R]

The fifth subunit in α3β4 nicotinic receptor is more than an accessory subunit

Plutino, Simona;Fucile, Sergio;
2018

Abstract

The α3β4 subtype is the predominant neuronal nicotinic acetylcholine receptor present in the sensory and autonomic ganglia and in a subpopulation of brain neurons. This subtype can form pentameric receptors with either 2 or 3 β4 subunits that have different pharmacologic and functional properties. To further investigate the role of the fifth subunit, we coexpressed a dimeric construct coding for a single polypeptide containing the β4 and α3 subunit sequences, with different monomeric subunits. With this strategy, which allowed the formation of single populations of receptors with unique stoichiometry, we demonstrated with immunofluorescence and biochemical and functional assays that only the receptors with 3 β4 subunits are efficiently expressed at the plasma membrane. Moreover, the LFM export motif of β4 subunit in the fifth position exerts a unique function in the regulation of the intracellular trafficking of the receptors, their exposure at the cell surface, and consequently, their function, whereas the same export motif present in the β4 subunits forming the acetylcholine binding site is dispensable.-Crespi, A., Plutino, S., Sciaccaluga, M., Righi, M., Borgese, N., Fucile, S., Gotti, C., Colombo, S. F. The fifth subunit in α3β4 nicotinic receptor is more than an accessory subunit.
2018
ER export signal; nAChR subtypes; nAChR trafficking; stoichiometry
01 Pubblicazione su rivista::01a Articolo in rivista
The fifth subunit in α3β4 nicotinic receptor is more than an accessory subunit / Crespi, Arianna; Plutino, Simona; Sciaccaluga, Miriam; Righi, Marco; Borgese, Nica; Fucile, Sergio; Gotti, Cecilia; Colombo, Sara Francesca. - In: THE FASEB JOURNAL. - ISSN 0892-6638. - STAMPA. - 32:8(2018), pp. 4190-4202. [10.1096/fj.201701377R]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/1141482
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