| Literature DB >> 8994599 |
G C Kowdley1, S J Ackerman, Z Chen, G Szabo, L R Jones, J R Moorman.
Abstract
Phospholemman (PLM), a 72-amino acid membrane protein with a single transmembrane domain, forms taurine-selective ion channels in lipid bilayers. Because taurine forms zwitterions, a taurine-selective channel might have binding sites for both anions and cations. Here we show that PLM channels indeed allow fluxes of both cations and anions, making instantaneous and voltage-dependent transitions among conformations with drastically different ion selectivity characteristics. This surprising and novel ion channel behavior offers a molecular explanation for selective taurine flux across cell membranes and may explain why molecules in the phospholemman family can induce cation- or anion-selective conductances when expressed in Xenopus oocytes.Entities:
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Year: 1997 PMID: 8994599 PMCID: PMC1184303 DOI: 10.1016/S0006-3495(97)78653-3
Source DB: PubMed Journal: Biophys J ISSN: 0006-3495 Impact factor: 4.033