Modulation of a brain voltage-gated K+ channel by syntaxin 1A requires
the physical interaction of Gbetagamma with the channel
I. Michaelevski, D. Chikvashvili, S. Tsuk, O. Fili, M. Lohse, D. Singer-Lahat, and I. Lotan. J Biol Chem, 277 (38):
34909-17(September 2002)Michaelevski, Izhak Chikvashvili, Dodo Tsuk, Sharon Fili, Oded Lohse,
Martin J Singer-Lahat, Dafna Lotan, Ilana Research Support, Non-U.S.
Gov't Research Support, U.S. Gov't, Non-P.H.S. United States The
Journal of biological chemistry J Biol Chem. 2002 Sep 20;277(38):34909-17.
Epub 2002 Jul 11..
Abstract
Recently we suggested that direct interactions between voltage-gated
K(+) channels and proteins of the exocytotic machinery, such as those
observed between the Kv1.1/Kvbeta channel, syntaxin 1A, and SNAP-25
may be involved in neurotransmitter release. Furthermore, we demonstrated
that the direct interaction with syntaxin 1A enhances the fast inactivation
of Kv1.1/Kvbeta1.1 in oocytes. Here we show that G-protein betagamma
subunits play a crucial role in the enhancement of inactivation by
syntaxin 1A. The effect caused by overexpression of syntaxin 1A is
eliminated in the presence of chelators of endogenous betagamma subunits
in the whole cell and at the plasma membrane. Conversely, enhancement
of inactivation caused by overexpression of beta(1)gamma(2) subunits
is eliminated upon knock-down of endogenous syntaxin or its scavenging
at the plasma membrane. We further show that the N terminus of Kv1.1
binds brain synaptosomal and recombinant syntaxin 1A and concomitantly
binds beta(1)gamma(2); the binding of beta(1)gamma(2) enhances that
of syntaxin 1A. Taken together, we suggest a mechanism whereby syntaxin
and G protein betagamma subunits interact concomitantly with a Kv
channel to regulate its inactivation.
%0 Journal Article
%1 Michaelevski2002
%A Michaelevski, I.
%A Chikvashvili, D.
%A Tsuk, S.
%A Fili, O.
%A Lohse, M. J.
%A Singer-Lahat, D.
%A Lotan, I.
%D 2002
%J J Biol Chem
%K *Ion 1 Animals Antigens, Base Binding Brain/metabolism/*physiology Channel Channels/metabolism/*physiology DNA GTP-Binding Gating Nerve Potassium Presynaptic Primers Protein Proteins/*physiology Sequence Surface/*physiology Syntaxin Terminals/physiology Tissue Xenopus laevis Proteins/metabolism
%N 38
%P 34909-17
%T Modulation of a brain voltage-gated K+ channel by syntaxin 1A requires
the physical interaction of Gbetagamma with the channel
%U http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12114518
%V 277
%X Recently we suggested that direct interactions between voltage-gated
K(+) channels and proteins of the exocytotic machinery, such as those
observed between the Kv1.1/Kvbeta channel, syntaxin 1A, and SNAP-25
may be involved in neurotransmitter release. Furthermore, we demonstrated
that the direct interaction with syntaxin 1A enhances the fast inactivation
of Kv1.1/Kvbeta1.1 in oocytes. Here we show that G-protein betagamma
subunits play a crucial role in the enhancement of inactivation by
syntaxin 1A. The effect caused by overexpression of syntaxin 1A is
eliminated in the presence of chelators of endogenous betagamma subunits
in the whole cell and at the plasma membrane. Conversely, enhancement
of inactivation caused by overexpression of beta(1)gamma(2) subunits
is eliminated upon knock-down of endogenous syntaxin or its scavenging
at the plasma membrane. We further show that the N terminus of Kv1.1
binds brain synaptosomal and recombinant syntaxin 1A and concomitantly
binds beta(1)gamma(2); the binding of beta(1)gamma(2) enhances that
of syntaxin 1A. Taken together, we suggest a mechanism whereby syntaxin
and G protein betagamma subunits interact concomitantly with a Kv
channel to regulate its inactivation.
@article{Michaelevski2002,
abstract = {Recently we suggested that direct interactions between voltage-gated
K(+) channels and proteins of the exocytotic machinery, such as those
observed between the Kv1.1/Kvbeta channel, syntaxin 1A, and SNAP-25
may be involved in neurotransmitter release. Furthermore, we demonstrated
that the direct interaction with syntaxin 1A enhances the fast inactivation
of Kv1.1/Kvbeta1.1 in oocytes. Here we show that G-protein betagamma
subunits play a crucial role in the enhancement of inactivation by
syntaxin 1A. The effect caused by overexpression of syntaxin 1A is
eliminated in the presence of chelators of endogenous betagamma subunits
in the whole cell and at the plasma membrane. Conversely, enhancement
of inactivation caused by overexpression of beta(1)gamma(2) subunits
is eliminated upon knock-down of endogenous syntaxin or its scavenging
at the plasma membrane. We further show that the N terminus of Kv1.1
binds brain synaptosomal and recombinant syntaxin 1A and concomitantly
binds beta(1)gamma(2); the binding of beta(1)gamma(2) enhances that
of syntaxin 1A. Taken together, we suggest a mechanism whereby syntaxin
and G protein betagamma subunits interact concomitantly with a Kv
channel to regulate its inactivation.},
added-at = {2010-12-14T18:12:02.000+0100},
author = {Michaelevski, I. and Chikvashvili, D. and Tsuk, S. and Fili, O. and Lohse, M. J. and Singer-Lahat, D. and Lotan, I.},
biburl = {https://www.bibsonomy.org/bibtex/240b718be80223361ab848e73fabbd29b/pharmawuerz},
endnotereftype = {Journal Article},
interhash = {01e2b3039ea3f97067c740f2f770f34b},
intrahash = {40b718be80223361ab848e73fabbd29b},
issn = {0021-9258 (Print) 0021-9258 (Linking)},
journal = {J Biol Chem},
keywords = {*Ion 1 Animals Antigens, Base Binding Brain/metabolism/*physiology Channel Channels/metabolism/*physiology DNA GTP-Binding Gating Nerve Potassium Presynaptic Primers Protein Proteins/*physiology Sequence Surface/*physiology Syntaxin Terminals/physiology Tissue Xenopus laevis Proteins/metabolism},
month = {Sep 20},
note = {Michaelevski, Izhak Chikvashvili, Dodo Tsuk, Sharon Fili, Oded Lohse,
Martin J Singer-Lahat, Dafna Lotan, Ilana Research Support, Non-U.S.
Gov't Research Support, U.S. Gov't, Non-P.H.S. United States The
Journal of biological chemistry J Biol Chem. 2002 Sep 20;277(38):34909-17.
Epub 2002 Jul 11.},
number = 38,
pages = {34909-17},
shorttitle = {Modulation of a brain voltage-gated K+ channel by syntaxin 1A requires
the physical interaction of Gbetagamma with the channel},
timestamp = {2010-12-14T18:21:43.000+0100},
title = {Modulation of a brain voltage-gated K+ channel by syntaxin 1A requires
the physical interaction of Gbetagamma with the channel},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12114518},
volume = 277,
year = 2002
}