The identification of N-glycosylated residues of the human 5-HT3B receptor subunit: importance for cell membrane expression.

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Massoura AN, Dover TJ, Newman AS, Barnes NM

The identification of N-glycosylated residues of the human 5-HT3B receptor subunit: importance for cell membrane expression.

J Neurochem. 2011 Mar;116(6):975-83. doi: 10.1111/j.1471-4159.2010.07129.x. Epub 2011 Jan 19.

PubMed ID
21138434 [ View in PubMed
]
Abstract

The 5-hydroxytryptamine 3 (5-HT(3)) receptor is a pentameric ligand-gated ion channel with potential molecular isoforms arising from different subunit combinations and/or different post-translational modifications of the individual subunits. Since N-glycosylation of the 5-HT3A subunit impacts cell surface trafficking, the presence of N-glycosylation of the human (h) 5-HT3B subunit and the influence upon cell membrane expression was investigated. Following transient expression of the h5-HT3B subunit by human embryonic kidney cells (HEK293 cells) stably expressing the h5-HT3A subunit, the N-glycosylation inhibitor tunicamycin reduced the size of the predominant h5-HT3B-immunoreactive protein ( approximately 55 kDa reduced to approximately 40 kDa). Disruption of each consensus N-glycosylation sequences in the h5-HT3B subunit (N31S, N75S, N117S, N147S and N182S) resulted in a reduced molecular weight (by approximately 2-4 kDa) of each mutant when expressed by HEK293 cells stably expressing the h5-HT3A subunit. Immunocytochemical studies demonstrated that disruption of each of the N-glycosylation sequences (individually or combined) reduced the expression of the mutant h5-HT3B subunit protein in the cell membrane when co-expressed with the h5-HT3A subunit. The present study has identified utilised N-glycosylation sites of the h5-HT3B subunit and demonstrated that they promote subunit expression in the cell membrane; a prerequisite for 5-HT(3) receptor function.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
5-hydroxytryptamine receptor 3BO95264Details