Cargando…

Gating Properties Conferred on Bk Channels by the β3b Auxiliary Subunit in the Absence of Its Nh(2)- and Cooh Termini

Both β1 and β2 auxiliary subunits of the BK-type K(+) channel family profoundly regulate the apparent Ca(2)+ sensitivity of BK-type Ca(2)+-activated K(+) channels. Each produces a pronounced leftward shift in the voltage of half-activation (V(0.5)) at a given Ca(2)+ concentration, particularly at Ca...

Descripción completa

Detalles Bibliográficos
Autores principales: Zeng, Xu-Hui, Ding, J.-P., Xia, Xiao-Ming, Lingle, Christopher J.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2001
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2232397/
https://www.ncbi.nlm.nih.gov/pubmed/11382809
_version_ 1782150259387924480
author Zeng, Xu-Hui
Ding, J.-P.
Xia, Xiao-Ming
Lingle, Christopher J.
author_facet Zeng, Xu-Hui
Ding, J.-P.
Xia, Xiao-Ming
Lingle, Christopher J.
author_sort Zeng, Xu-Hui
collection PubMed
description Both β1 and β2 auxiliary subunits of the BK-type K(+) channel family profoundly regulate the apparent Ca(2)+ sensitivity of BK-type Ca(2)+-activated K(+) channels. Each produces a pronounced leftward shift in the voltage of half-activation (V(0.5)) at a given Ca(2)+ concentration, particularly at Ca(2)+ above 1 μM. In contrast, the rapidly inactivating β3b auxiliary produces a leftward shift in activation at Ca(2)+ below 1 μM. In the companion work (Lingle, C.J., X.-H. Zeng, J.-P. Ding, and X.-M. Xia. 2001. J. Gen. Physiol. 117:583–605, this issue), we have shown that some of the apparent β3b-mediated shift in activation at low Ca(2)+ arises from rapid unblocking of inactivated channels, unlike the actions of the β1 and β2 subunits. Here, we compare effects of the β3b subunit that arise from inactivation, per se, versus those that may arise from other functional effects of the subunit. In particular, we examine gating properties of the β3b subunit and compare it to β3b constructs lacking either the NH(2)- or COOH terminus or both. The results demonstrate that, although the NH(2) terminus appears to be the primary determinant of the β3b-mediated shift in V(0.5) at low Ca(2)+, removal of the NH(2) terminus reveals two other interesting aspects of the action of the β3b subunit. First, the conductance-voltage curves for activation of channels containing the β3b subunit are best described by a double Boltzmann shape, which is proposed to arise from two independent voltage-dependent activation steps. Second, the presence of the β3b subunit results in channels that exhibit an anomalous instantaneous outward current rectification that is correlated with a voltage dependence in the time-averaged single-channel current. The two effects appear to be unrelated, but indicative of the variety of ways that interactions between β and α subunits can affect BK channel function. The COOH terminus of the β3b subunit produces no discernible functional effects.
format Text
id pubmed-2232397
institution National Center for Biotechnology Information
language English
publishDate 2001
publisher The Rockefeller University Press
record_format MEDLINE/PubMed
spelling pubmed-22323972008-04-22 Gating Properties Conferred on Bk Channels by the β3b Auxiliary Subunit in the Absence of Its Nh(2)- and Cooh Termini Zeng, Xu-Hui Ding, J.-P. Xia, Xiao-Ming Lingle, Christopher J. J Gen Physiol Original Article Both β1 and β2 auxiliary subunits of the BK-type K(+) channel family profoundly regulate the apparent Ca(2)+ sensitivity of BK-type Ca(2)+-activated K(+) channels. Each produces a pronounced leftward shift in the voltage of half-activation (V(0.5)) at a given Ca(2)+ concentration, particularly at Ca(2)+ above 1 μM. In contrast, the rapidly inactivating β3b auxiliary produces a leftward shift in activation at Ca(2)+ below 1 μM. In the companion work (Lingle, C.J., X.-H. Zeng, J.-P. Ding, and X.-M. Xia. 2001. J. Gen. Physiol. 117:583–605, this issue), we have shown that some of the apparent β3b-mediated shift in activation at low Ca(2)+ arises from rapid unblocking of inactivated channels, unlike the actions of the β1 and β2 subunits. Here, we compare effects of the β3b subunit that arise from inactivation, per se, versus those that may arise from other functional effects of the subunit. In particular, we examine gating properties of the β3b subunit and compare it to β3b constructs lacking either the NH(2)- or COOH terminus or both. The results demonstrate that, although the NH(2) terminus appears to be the primary determinant of the β3b-mediated shift in V(0.5) at low Ca(2)+, removal of the NH(2) terminus reveals two other interesting aspects of the action of the β3b subunit. First, the conductance-voltage curves for activation of channels containing the β3b subunit are best described by a double Boltzmann shape, which is proposed to arise from two independent voltage-dependent activation steps. Second, the presence of the β3b subunit results in channels that exhibit an anomalous instantaneous outward current rectification that is correlated with a voltage dependence in the time-averaged single-channel current. The two effects appear to be unrelated, but indicative of the variety of ways that interactions between β and α subunits can affect BK channel function. The COOH terminus of the β3b subunit produces no discernible functional effects. The Rockefeller University Press 2001-06-01 /pmc/articles/PMC2232397/ /pubmed/11382809 Text en © 2001 The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Original Article
Zeng, Xu-Hui
Ding, J.-P.
Xia, Xiao-Ming
Lingle, Christopher J.
Gating Properties Conferred on Bk Channels by the β3b Auxiliary Subunit in the Absence of Its Nh(2)- and Cooh Termini
title Gating Properties Conferred on Bk Channels by the β3b Auxiliary Subunit in the Absence of Its Nh(2)- and Cooh Termini
title_full Gating Properties Conferred on Bk Channels by the β3b Auxiliary Subunit in the Absence of Its Nh(2)- and Cooh Termini
title_fullStr Gating Properties Conferred on Bk Channels by the β3b Auxiliary Subunit in the Absence of Its Nh(2)- and Cooh Termini
title_full_unstemmed Gating Properties Conferred on Bk Channels by the β3b Auxiliary Subunit in the Absence of Its Nh(2)- and Cooh Termini
title_short Gating Properties Conferred on Bk Channels by the β3b Auxiliary Subunit in the Absence of Its Nh(2)- and Cooh Termini
title_sort gating properties conferred on bk channels by the β3b auxiliary subunit in the absence of its nh(2)- and cooh termini
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2232397/
https://www.ncbi.nlm.nih.gov/pubmed/11382809
work_keys_str_mv AT zengxuhui gatingpropertiesconferredonbkchannelsbytheb3bauxiliarysubunitintheabsenceofitsnh2andcoohtermini
AT dingjp gatingpropertiesconferredonbkchannelsbytheb3bauxiliarysubunitintheabsenceofitsnh2andcoohtermini
AT xiaxiaoming gatingpropertiesconferredonbkchannelsbytheb3bauxiliarysubunitintheabsenceofitsnh2andcoohtermini
AT linglechristopherj gatingpropertiesconferredonbkchannelsbytheb3bauxiliarysubunitintheabsenceofitsnh2andcoohtermini