dc.contributor.author | Lizardi-Ortiz, José E. | |
dc.contributor.author | Hyzinski-García, María C. | |
dc.contributor.author | Fernández-Gerena, José L. | |
dc.contributor.author | Osorio-Martínez, Karen M. | |
dc.contributor.author | Velázquez-Rivera, Eric | |
dc.contributor.author | Valle-Avilés, Félix L. | |
dc.contributor.author | Lasalde-Dominicci, José A. | |
dc.date.accessioned | 2017-03-23T20:10:49Z | |
dc.date.available | 2017-03-23T20:10:49Z | |
dc.date.issued | 2008 | |
dc.identifier.citation | Lizardi-Ortiz JE, Hyzinski-García MC, Fernández-Gerena JL, Osorio-Martínez KM, Velázquez-Rivera E, Valle-Avilés FL, Lasalde-Dominicci JA. Aromaticity at the water-hydrocarbon core interface of the membrane: consequences on the nicotinic acetylcholine receptor. Channels (Austin, Tex.). 2: 191-201. PMID 18836298 | en_US |
dc.identifier.issn | 1933-6969 | |
dc.identifier.uri | http://hdl.handle.net/11721/1564 | |
dc.description.abstract | Almost all lipid-exposed transmembrane domains of integral proteins contain aromatic residues
flanking the hydrophobic segment of the domains. These residues generally reside close to the
carbonyl region of the membrane, and several structural and functional roles have been associated
to these residues. Although the roles and physicochemical reasons for aromatic preference have
been extensively studied using model systems, few studies have been done in a native membrane
system. To gain insight about the mechanistic implication for this aromatic preference, we selected
position αF426 of the muscle-type nicotinic acetylcholine receptor (nAChR). αF426 is a lipidexposed
residue at the extracellular segment of the αM4 transmembrane domain and is highly
conserved among different nAChR subunits and species. We used site-directed mutagenesis, α-
Bungarotoxin-binding assay, and two-electrodes voltage clamp in Xenopus laevis oocytes to
characterize mutations at position αF426, which impart different physicochemical properties like
volume, polarity, hydrogen bonds, aromaticity and net electrical charge. All mutations except the
aromatic residues resulted in a significant reduction of the nAChR cell-surface levels and the
macroscopic currents to acetylcholine. These results suggest that position αF426 contributes to
structural stability and open-close transitions of the nAChR. Finally, the present study also
provides information about how intermolecular interactions at position α426 modulate open-close
transitions of the nAChR. | en_US |
dc.language.iso | en | en_US |
dc.publisher | Channels (Austin) | en_US |
dc.subject | nicotinic acetylcholine receptor | en_US |
dc.subject | lipid-protein interface | en_US |
dc.subject | water-hydrocarbon core interface | en_US |
dc.subject | membrane-spanning domain | en_US |
dc.subject | aromaticity | en_US |
dc.title | Aromaticity at the water-hydrocarbon core interface of the membrane: Consequences on the nicotinic acetylcholine receptor | en_US |
dc.type | Article | en_US |
dc.contributor.campus | University of Puerto Rico, Río Piedras Campus | |