Store-operated interactions between plasmalemmal STIM1 and TRPC1 proteins stimulate PLCβ1 to induce TRPC1 channel activation in vascular smooth muscle cells

Autores
Shi, Jian; Miralles, Francesc; Birnbaumer, Lutz; Large, William A.; Albert, Anthony P.
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Depletion of sarcoplasmic reticulum (SR) Ca2+ stores activates store-operated channels (SOCs) composed of canonical transient receptor potential (TRPC) 1 proteins in vascular smooth muscle cells (VSMCs), which contribute to important cellular functions. We have previously shown that PKC is obligatory for activation of TRPC1 SOCs in VSMCs, and the present study investigates if the classic phosphoinositol signaling pathway involving Gaq-mediated PLC activity is responsible for driving PKCdependent channel gating. The G-protein inhibitor GDPb-S, anti-Gaq antibodies, the PLC inhibitor U73122, and the PKC inhibitor GF109203X all inhibited activation of TRPC1 SOCs, and U73122 and GF109203X also reduced storeoperated PKC-dependent phosphorylation of TRPC1 proteins. Three distinct SR Ca2+ store-depleting agents, 1,2-bis(2-aminophenoxy)ethane-N,N,N9,N9-tetraacetic acid acetoxymethyl ester, cyclopiazonic acid, and N,N,N9,N9- tetrakis(2-pyridylmethyl)ethane-1,2-diamineed,induced translocations of the fluorescent biosensor GFP-PLCd1-PH from the cell membrane to the cytosol, which were inhibited by U73122. Knockdown of PLCb1 with small hairpin RNA reduced both store-operated PLC activity and stimulation of TRPC1 SOCs. Immunoprecipitation studies and proximity ligation assays revealed that store depletion induced interactions between TRPC1 and Gaq, and TRPC1 and PLCb1. We propose a novel activationmechanism forTRPC1 SOCs in VSMCs, in which store depletion induces formation of TRPC1-Gaq-PLCb1 complexes that lead to PKC stimulation and channel gating.—Shi, J., Miralles, F., Birnbaumer, L., Large, W. A., Albert, A. P. Store depletion induces Gaqmediated PLCb1 activity to stimulate TRPC1 channels in vascular smooth muscle cells
Fil: Shi, Jian. Vascular Biology Research Centre; Reino Unido
Fil: Miralles, Francesc. Vascular Biology Research Centre; Reino Unido. University of London; Reino Unido
Fil: Birnbaumer, Lutz. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. National Institute of Environmental Health Sciences; Estados Unidos
Fil: Large, William A.. Vascular Biology Research Centre; Reino Unido
Fil: Albert, Anthony P.. Vascular Biology Research Centre; Reino Unido
Materia
Electrophysiology
Plc Activity
Ca2+ Signaling
Phosphoinositol Signaling
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/47664
Acceder
id CONICETDig_dc3b2d972a2b27bdc917a098fd713071
oai_identifier_str oai:ri.conicet.gov.ar:11336/47664
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Store-operated interactions between plasmalemmal STIM1 and TRPC1 proteins stimulate PLCβ1 to induce TRPC1 channel activation in vascular smooth muscle cellsShi, JianMiralles, FrancescBirnbaumer, LutzLarge, William A.Albert, Anthony P.ElectrophysiologyPlc ActivityCa2+ SignalingPhosphoinositol Signalinghttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Depletion of sarcoplasmic reticulum (SR) Ca2+ stores activates store-operated channels (SOCs) composed of canonical transient receptor potential (TRPC) 1 proteins in vascular smooth muscle cells (VSMCs), which contribute to important cellular functions. We have previously shown that PKC is obligatory for activation of TRPC1 SOCs in VSMCs, and the present study investigates if the classic phosphoinositol signaling pathway involving Gaq-mediated PLC activity is responsible for driving PKCdependent channel gating. The G-protein inhibitor GDPb-S, anti-Gaq antibodies, the PLC inhibitor U73122, and the PKC inhibitor GF109203X all inhibited activation of TRPC1 SOCs, and U73122 and GF109203X also reduced storeoperated PKC-dependent phosphorylation of TRPC1 proteins. Three distinct SR Ca2+ store-depleting agents, 1,2-bis(2-aminophenoxy)ethane-N,N,N9,N9-tetraacetic acid acetoxymethyl ester, cyclopiazonic acid, and N,N,N9,N9- tetrakis(2-pyridylmethyl)ethane-1,2-diamineed,induced translocations of the fluorescent biosensor GFP-PLCd1-PH from the cell membrane to the cytosol, which were inhibited by U73122. Knockdown of PLCb1 with small hairpin RNA reduced both store-operated PLC activity and stimulation of TRPC1 SOCs. Immunoprecipitation studies and proximity ligation assays revealed that store depletion induced interactions between TRPC1 and Gaq, and TRPC1 and PLCb1. We propose a novel activationmechanism forTRPC1 SOCs in VSMCs, in which store depletion induces formation of TRPC1-Gaq-PLCb1 complexes that lead to PKC stimulation and channel gating.—Shi, J., Miralles, F., Birnbaumer, L., Large, W. A., Albert, A. P. Store depletion induces Gaqmediated PLCb1 activity to stimulate TRPC1 channels in vascular smooth muscle cellsFil: Shi, Jian. Vascular Biology Research Centre; Reino UnidoFil: Miralles, Francesc. Vascular Biology Research Centre; Reino Unido. University of London; Reino UnidoFil: Birnbaumer, Lutz. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. National Institute of Environmental Health Sciences; Estados UnidosFil: Large, William A.. Vascular Biology Research Centre; Reino UnidoFil: Albert, Anthony P.. Vascular Biology Research Centre; Reino UnidoWiley Blackwell Publishing, Inc2017-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/47664Shi, Jian; Miralles, Francesc; Birnbaumer, Lutz; Large, William A.; Albert, Anthony P.; Store-operated interactions between plasmalemmal STIM1 and TRPC1 proteins stimulate PLCβ1 to induce TRPC1 channel activation in vascular smooth muscle cells; Wiley Blackwell Publishing, Inc; The Journal Of Physiology; 595; 4; 2-2017; 1039-10580022-3751CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1113/JP273302info:eu-repo/semantics/altIdentifier/url/https://physoc.onlinelibrary.wiley.com/doi/abs/10.1113/JP273302info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:49:07Zoai:ri.conicet.gov.ar:11336/47664instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 09:49:07.393CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Store-operated interactions between plasmalemmal STIM1 and TRPC1 proteins stimulate PLCβ1 to induce TRPC1 channel activation in vascular smooth muscle cells
title Store-operated interactions between plasmalemmal STIM1 and TRPC1 proteins stimulate PLCβ1 to induce TRPC1 channel activation in vascular smooth muscle cells
spellingShingle Store-operated interactions between plasmalemmal STIM1 and TRPC1 proteins stimulate PLCβ1 to induce TRPC1 channel activation in vascular smooth muscle cells
Shi, Jian
Electrophysiology
Plc Activity
Ca2+ Signaling
Phosphoinositol Signaling
title_short Store-operated interactions between plasmalemmal STIM1 and TRPC1 proteins stimulate PLCβ1 to induce TRPC1 channel activation in vascular smooth muscle cells
title_full Store-operated interactions between plasmalemmal STIM1 and TRPC1 proteins stimulate PLCβ1 to induce TRPC1 channel activation in vascular smooth muscle cells
title_fullStr Store-operated interactions between plasmalemmal STIM1 and TRPC1 proteins stimulate PLCβ1 to induce TRPC1 channel activation in vascular smooth muscle cells
title_full_unstemmed Store-operated interactions between plasmalemmal STIM1 and TRPC1 proteins stimulate PLCβ1 to induce TRPC1 channel activation in vascular smooth muscle cells
title_sort Store-operated interactions between plasmalemmal STIM1 and TRPC1 proteins stimulate PLCβ1 to induce TRPC1 channel activation in vascular smooth muscle cells
dc.creator.none.fl_str_mv Shi, Jian
Miralles, Francesc
Birnbaumer, Lutz
Large, William A.
Albert, Anthony P.
author Shi, Jian
author_facet Shi, Jian
Miralles, Francesc
Birnbaumer, Lutz
Large, William A.
Albert, Anthony P.
author_role author
author2 Miralles, Francesc
Birnbaumer, Lutz
Large, William A.
Albert, Anthony P.
author2_role author
author
author
author
dc.subject.none.fl_str_mv Electrophysiology
Plc Activity
Ca2+ Signaling
Phosphoinositol Signaling
topic Electrophysiology
Plc Activity
Ca2+ Signaling
Phosphoinositol Signaling
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Depletion of sarcoplasmic reticulum (SR) Ca2+ stores activates store-operated channels (SOCs) composed of canonical transient receptor potential (TRPC) 1 proteins in vascular smooth muscle cells (VSMCs), which contribute to important cellular functions. We have previously shown that PKC is obligatory for activation of TRPC1 SOCs in VSMCs, and the present study investigates if the classic phosphoinositol signaling pathway involving Gaq-mediated PLC activity is responsible for driving PKCdependent channel gating. The G-protein inhibitor GDPb-S, anti-Gaq antibodies, the PLC inhibitor U73122, and the PKC inhibitor GF109203X all inhibited activation of TRPC1 SOCs, and U73122 and GF109203X also reduced storeoperated PKC-dependent phosphorylation of TRPC1 proteins. Three distinct SR Ca2+ store-depleting agents, 1,2-bis(2-aminophenoxy)ethane-N,N,N9,N9-tetraacetic acid acetoxymethyl ester, cyclopiazonic acid, and N,N,N9,N9- tetrakis(2-pyridylmethyl)ethane-1,2-diamineed,induced translocations of the fluorescent biosensor GFP-PLCd1-PH from the cell membrane to the cytosol, which were inhibited by U73122. Knockdown of PLCb1 with small hairpin RNA reduced both store-operated PLC activity and stimulation of TRPC1 SOCs. Immunoprecipitation studies and proximity ligation assays revealed that store depletion induced interactions between TRPC1 and Gaq, and TRPC1 and PLCb1. We propose a novel activationmechanism forTRPC1 SOCs in VSMCs, in which store depletion induces formation of TRPC1-Gaq-PLCb1 complexes that lead to PKC stimulation and channel gating.—Shi, J., Miralles, F., Birnbaumer, L., Large, W. A., Albert, A. P. Store depletion induces Gaqmediated PLCb1 activity to stimulate TRPC1 channels in vascular smooth muscle cells
Fil: Shi, Jian. Vascular Biology Research Centre; Reino Unido
Fil: Miralles, Francesc. Vascular Biology Research Centre; Reino Unido. University of London; Reino Unido
Fil: Birnbaumer, Lutz. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. National Institute of Environmental Health Sciences; Estados Unidos
Fil: Large, William A.. Vascular Biology Research Centre; Reino Unido
Fil: Albert, Anthony P.. Vascular Biology Research Centre; Reino Unido
description Depletion of sarcoplasmic reticulum (SR) Ca2+ stores activates store-operated channels (SOCs) composed of canonical transient receptor potential (TRPC) 1 proteins in vascular smooth muscle cells (VSMCs), which contribute to important cellular functions. We have previously shown that PKC is obligatory for activation of TRPC1 SOCs in VSMCs, and the present study investigates if the classic phosphoinositol signaling pathway involving Gaq-mediated PLC activity is responsible for driving PKCdependent channel gating. The G-protein inhibitor GDPb-S, anti-Gaq antibodies, the PLC inhibitor U73122, and the PKC inhibitor GF109203X all inhibited activation of TRPC1 SOCs, and U73122 and GF109203X also reduced storeoperated PKC-dependent phosphorylation of TRPC1 proteins. Three distinct SR Ca2+ store-depleting agents, 1,2-bis(2-aminophenoxy)ethane-N,N,N9,N9-tetraacetic acid acetoxymethyl ester, cyclopiazonic acid, and N,N,N9,N9- tetrakis(2-pyridylmethyl)ethane-1,2-diamineed,induced translocations of the fluorescent biosensor GFP-PLCd1-PH from the cell membrane to the cytosol, which were inhibited by U73122. Knockdown of PLCb1 with small hairpin RNA reduced both store-operated PLC activity and stimulation of TRPC1 SOCs. Immunoprecipitation studies and proximity ligation assays revealed that store depletion induced interactions between TRPC1 and Gaq, and TRPC1 and PLCb1. We propose a novel activationmechanism forTRPC1 SOCs in VSMCs, in which store depletion induces formation of TRPC1-Gaq-PLCb1 complexes that lead to PKC stimulation and channel gating.—Shi, J., Miralles, F., Birnbaumer, L., Large, W. A., Albert, A. P. Store depletion induces Gaqmediated PLCb1 activity to stimulate TRPC1 channels in vascular smooth muscle cells
publishDate 2017
dc.date.none.fl_str_mv 2017-02
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/47664
Shi, Jian; Miralles, Francesc; Birnbaumer, Lutz; Large, William A.; Albert, Anthony P.; Store-operated interactions between plasmalemmal STIM1 and TRPC1 proteins stimulate PLCβ1 to induce TRPC1 channel activation in vascular smooth muscle cells; Wiley Blackwell Publishing, Inc; The Journal Of Physiology; 595; 4; 2-2017; 1039-1058
0022-3751
CONICET Digital
CONICET
url http://hdl.handle.net/11336/47664
identifier_str_mv Shi, Jian; Miralles, Francesc; Birnbaumer, Lutz; Large, William A.; Albert, Anthony P.; Store-operated interactions between plasmalemmal STIM1 and TRPC1 proteins stimulate PLCβ1 to induce TRPC1 channel activation in vascular smooth muscle cells; Wiley Blackwell Publishing, Inc; The Journal Of Physiology; 595; 4; 2-2017; 1039-1058
0022-3751
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1113/JP273302
info:eu-repo/semantics/altIdentifier/url/https://physoc.onlinelibrary.wiley.com/doi/abs/10.1113/JP273302
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1842268954525958144
score 13.13397

Publicaciones similares