Anion, cation, and zwitterion selectivity of phospholemman channel molecules

Gopal C. Kowdley, Stephen J. Ackerman, Zhenhui Chen, Gabor Szabo, Larry Jones, J. Randall Moorman

Research output: Contribution to journalArticle

45 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)141-145
Number of pages5
JournalBiophysical Journal
Volume72
Issue number1
StatePublished - 1997

Fingerprint

Taurine
Anions
Cations
Ion Channels
Lipid Bilayers
Xenopus
Oocytes
Membrane Proteins
Binding Sites
Cell Membrane
Ions
Amino Acids
phospholemman

ASJC Scopus subject areas

  • Biophysics

Cite this

Kowdley, G. C., Ackerman, S. J., Chen, Z., Szabo, G., Jones, L., & Moorman, J. R. (1997). Anion, cation, and zwitterion selectivity of phospholemman channel molecules. Biophysical Journal, 72(1), 141-145.

Anion, cation, and zwitterion selectivity of phospholemman channel molecules. / Kowdley, Gopal C.; Ackerman, Stephen J.; Chen, Zhenhui; Szabo, Gabor; Jones, Larry; Moorman, J. Randall.

In: Biophysical Journal, Vol. 72, No. 1, 1997, p. 141-145.

Research output: Contribution to journalArticle

Kowdley, GC, Ackerman, SJ, Chen, Z, Szabo, G, Jones, L & Moorman, JR 1997, 'Anion, cation, and zwitterion selectivity of phospholemman channel molecules', Biophysical Journal, vol. 72, no. 1, pp. 141-145.
Kowdley, Gopal C. ; Ackerman, Stephen J. ; Chen, Zhenhui ; Szabo, Gabor ; Jones, Larry ; Moorman, J. Randall. / Anion, cation, and zwitterion selectivity of phospholemman channel molecules. In: Biophysical Journal. 1997 ; Vol. 72, No. 1. pp. 141-145.
@article{4dafde888c514b6c840a77075ab39459,
title = "Anion, cation, and zwitterion selectivity of phospholemman channel molecules",
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.",
author = "Kowdley, {Gopal C.} and Ackerman, {Stephen J.} and Zhenhui Chen and Gabor Szabo and Larry Jones and Moorman, {J. Randall}",
year = "1997",
language = "English",
volume = "72",
pages = "141--145",
journal = "Biophysical Journal",
issn = "0006-3495",
publisher = "Biophysical Society",
number = "1",

}

TY - JOUR

T1 - Anion, cation, and zwitterion selectivity of phospholemman channel molecules

AU - Kowdley, Gopal C.

AU - Ackerman, Stephen J.

AU - Chen, Zhenhui

AU - Szabo, Gabor

AU - Jones, Larry

AU - Moorman, J. Randall

PY - 1997

Y1 - 1997

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0031019847&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031019847&partnerID=8YFLogxK

M3 - Article

VL - 72

SP - 141

EP - 145

JO - Biophysical Journal

JF - Biophysical Journal

SN - 0006-3495

IS - 1

ER -