Submembraneous microtubule cytoskeleton: regulation of ATPases by interaction with acetylated tubulin

Autores
Arce, Carlos Angel; Casale, Cesar Horacio; Barra, Hector
Año de publicación
2008
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The ATP-hydrolysing enzymes (Na+,K+)-, H+- and Ca2+-ATPase are integral membrane proteins that play important roles in the exchange of ions and nutrients between the exterior and interior of cells, and are involved in signal transduction pathways. Activity of these ATPases is regulated by several specific effectors. Here, we review the regulation of these P-type ATPases by a common effector, acetylated tubulin, which interacts with them and inhibits their enzyme activity. The presence of an acetyl group on Lys40 of a-tubulin is a requirement for the interaction. Stimulation of enzyme activity by different effectors involves the dissociation of tubulin ⁄ATPase complexes. In cultured cells, acetylated tubulin associated with ATPase appears to be a constituent of microtubules. Stabilization of microtubules by taxol blocks association ⁄ dissociation of the complex. Membrane ATPases may function as anchorage sites for microtubules.
Fil: Arce, Carlos Angel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Casale, Cesar Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Biología Molecular; Argentina
Fil: Barra, Hector. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Materia
Na,K-ATPase
Tubulin
Membrane
PMCA
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:11336/242250
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/242250
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Submembraneous microtubule cytoskeleton: regulation of ATPases by interaction with acetylated tubulinArce, Carlos AngelCasale, Cesar HoracioBarra, HectorNa,K-ATPaseTubulinMembranePMCAhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1The ATP-hydrolysing enzymes (Na+,K+)-, H+- and Ca2+-ATPase are integral membrane proteins that play important roles in the exchange of ions and nutrients between the exterior and interior of cells, and are involved in signal transduction pathways. Activity of these ATPases is regulated by several specific effectors. Here, we review the regulation of these P-type ATPases by a common effector, acetylated tubulin, which interacts with them and inhibits their enzyme activity. The presence of an acetyl group on Lys40 of a-tubulin is a requirement for the interaction. Stimulation of enzyme activity by different effectors involves the dissociation of tubulin ⁄ATPase complexes. In cultured cells, acetylated tubulin associated with ATPase appears to be a constituent of microtubules. Stabilization of microtubules by taxol blocks association ⁄ dissociation of the complex. Membrane ATPases may function as anchorage sites for microtubules.Fil: Arce, Carlos Angel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaFil: Casale, Cesar Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Biología Molecular; ArgentinaFil: Barra, Hector. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaWiley Blackwell Publishing, Inc2008-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/242250Arce, Carlos Angel; Casale, Cesar Horacio; Barra, Hector; Submembraneous microtubule cytoskeleton: regulation of ATPases by interaction with acetylated tubulin; Wiley Blackwell Publishing, Inc; Febs Journal; 275; 19; 9-2008; 4664-46741742-464XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://febs.onlinelibrary.wiley.com/doi/10.1111/j.1742-4658.2008.06615.xinfo:eu-repo/semantics/altIdentifier/doi/10.1111/j.1742-4658.2008.06615.xinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:08:00Zoai:ri.conicet.gov.ar:11336/242250instacron: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 10:08:00.426CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Submembraneous microtubule cytoskeleton: regulation of ATPases by interaction with acetylated tubulin
title Submembraneous microtubule cytoskeleton: regulation of ATPases by interaction with acetylated tubulin
spellingShingle Submembraneous microtubule cytoskeleton: regulation of ATPases by interaction with acetylated tubulin
Arce, Carlos Angel
Na,K-ATPase
Tubulin
Membrane
PMCA
title_short Submembraneous microtubule cytoskeleton: regulation of ATPases by interaction with acetylated tubulin
title_full Submembraneous microtubule cytoskeleton: regulation of ATPases by interaction with acetylated tubulin
title_fullStr Submembraneous microtubule cytoskeleton: regulation of ATPases by interaction with acetylated tubulin
title_full_unstemmed Submembraneous microtubule cytoskeleton: regulation of ATPases by interaction with acetylated tubulin
title_sort Submembraneous microtubule cytoskeleton: regulation of ATPases by interaction with acetylated tubulin
dc.creator.none.fl_str_mv Arce, Carlos Angel
Casale, Cesar Horacio
Barra, Hector
author Arce, Carlos Angel
author_facet Arce, Carlos Angel
Casale, Cesar Horacio
Barra, Hector
author_role author
author2 Casale, Cesar Horacio
Barra, Hector
author2_role author
author
dc.subject.none.fl_str_mv Na,K-ATPase
Tubulin
Membrane
PMCA
topic Na,K-ATPase
Tubulin
Membrane
PMCA
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The ATP-hydrolysing enzymes (Na+,K+)-, H+- and Ca2+-ATPase are integral membrane proteins that play important roles in the exchange of ions and nutrients between the exterior and interior of cells, and are involved in signal transduction pathways. Activity of these ATPases is regulated by several specific effectors. Here, we review the regulation of these P-type ATPases by a common effector, acetylated tubulin, which interacts with them and inhibits their enzyme activity. The presence of an acetyl group on Lys40 of a-tubulin is a requirement for the interaction. Stimulation of enzyme activity by different effectors involves the dissociation of tubulin ⁄ATPase complexes. In cultured cells, acetylated tubulin associated with ATPase appears to be a constituent of microtubules. Stabilization of microtubules by taxol blocks association ⁄ dissociation of the complex. Membrane ATPases may function as anchorage sites for microtubules.
Fil: Arce, Carlos Angel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Casale, Cesar Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Biología Molecular; Argentina
Fil: Barra, Hector. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
description The ATP-hydrolysing enzymes (Na+,K+)-, H+- and Ca2+-ATPase are integral membrane proteins that play important roles in the exchange of ions and nutrients between the exterior and interior of cells, and are involved in signal transduction pathways. Activity of these ATPases is regulated by several specific effectors. Here, we review the regulation of these P-type ATPases by a common effector, acetylated tubulin, which interacts with them and inhibits their enzyme activity. The presence of an acetyl group on Lys40 of a-tubulin is a requirement for the interaction. Stimulation of enzyme activity by different effectors involves the dissociation of tubulin ⁄ATPase complexes. In cultured cells, acetylated tubulin associated with ATPase appears to be a constituent of microtubules. Stabilization of microtubules by taxol blocks association ⁄ dissociation of the complex. Membrane ATPases may function as anchorage sites for microtubules.
publishDate 2008
dc.date.none.fl_str_mv 2008-09
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/11336/242250
Arce, Carlos Angel; Casale, Cesar Horacio; Barra, Hector; Submembraneous microtubule cytoskeleton: regulation of ATPases by interaction with acetylated tubulin; Wiley Blackwell Publishing, Inc; Febs Journal; 275; 19; 9-2008; 4664-4674
1742-464X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/242250
identifier_str_mv Arce, Carlos Angel; Casale, Cesar Horacio; Barra, Hector; Submembraneous microtubule cytoskeleton: regulation of ATPases by interaction with acetylated tubulin; Wiley Blackwell Publishing, Inc; Febs Journal; 275; 19; 9-2008; 4664-4674
1742-464X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://febs.onlinelibrary.wiley.com/doi/10.1111/j.1742-4658.2008.06615.x
info:eu-repo/semantics/altIdentifier/doi/10.1111/j.1742-4658.2008.06615.x
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
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
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score 13.13397

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