Tubulin–Na + , K + ‐ATPase interaction: Involvement in enzymatic regulation and cellular function

Autores
Santander, Verónica Silvin; Campetelli, Alexis Nazareno; Monesterolo, Noelia Edith; Rivelli Antonelli, Juan Franco; Nigra, Ayelén Denise; Arce, Carlos Angel; Casale, Cesar Horacio
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
A new function for tubulin was described by our laboratory: acetylated tubulin forms a complex with Na+,K+-ATPase (NKA) and inhibits its activity. This process was shown to be a regulatory factor of physiological importance in cultured cells, human erythrocytes and several rat tissues. Formation of the acetylated tubulin/NKA complex is reversible. We demonstrated that in cultured cells, high concentrations of glucose induce translocation of acetylated tubulin from cytoplasm to plasma membrane with a consequent inhibition of NKA activity. This effect is reversed by adding glutamate, which is co-transported to the cell with Na+. Another post-translational modification of tubulin, detyrosinated tubulin, is also involved in the regulation of NKA activity: it enhances the NKA inhibition induced by acetylated tubulin. Manipulation of the content of these modifications of tubulin could work as a new strategy to maintain homeostasis of Na+ and K+, and to regulate a variety of functions in which NKA is involved, such as osmotic fragility and deformability of human erythrocytes. The results summarized in this review show that the interaction between tubulin and NKA plays an important role in cellular physiology, both in the regulation of Na+/K+ homeostasis and in the rheological properties of the cells, which is mechanically different from other roles reported up to now.
Fil: Santander, Verónica Silvin. 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: Campetelli, Alexis Nazareno. Universidad Nacional de Rio Cuarto. Facultad de Cs.exactas Fisicoquimicas y Naturales. Instituto de Biotecnologia Ambiental y Salud. - Consejo Nacional de Investigaciones Cientificas y Tecnicas. Centro Cientifico Tecnologico Conicet - Cordoba. Instituto de Biotecnologia Ambiental y Salud.; Argentina
Fil: Monesterolo, Noelia Edith. Universidad Nacional de Rio Cuarto. Facultad de Cs.exactas Fisicoquimicas y Naturales. Instituto de Biotecnologia Ambiental y Salud. - Consejo Nacional de Investigaciones Cientificas y Tecnicas. Centro Cientifico Tecnologico Conicet - Cordoba. Instituto de Biotecnologia Ambiental y Salud.; Argentina
Fil: Rivelli Antonelli, Juan Franco. Universidad Nacional de Rio Cuarto. Facultad de Cs.exactas Fisicoquimicas y Naturales. Instituto de Biotecnologia Ambiental y Salud. - Consejo Nacional de Investigaciones Cientificas y Tecnicas. Centro Cientifico Tecnologico Conicet - Cordoba. Instituto de Biotecnologia Ambiental y Salud.; Argentina
Fil: Nigra, Ayelén Denise. 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: 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. Universidad Nacional de Rio Cuarto. Facultad de Cs.exactas Fisicoquimicas y Naturales. Instituto de Biotecnologia Ambiental y Salud. - Consejo Nacional de Investigaciones Cientificas y Tecnicas. Centro Cientifico Tecnologico Conicet - Cordoba. Instituto de Biotecnologia Ambiental y Salud.; Argentina
Materia
NA, K-ATPASE
TUBULIN
INTERACTION
REGULATION
MEMBRANES
ERYTHROCYTES
HOMEOSTASIS
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:11336/104408
Acceder
id CONICETDig_c53227e14d0319ef6a42db255f2472aa
oai_identifier_str oai:ri.conicet.gov.ar:11336/104408
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Tubulin–Na + , K + ‐ATPase interaction: Involvement in enzymatic regulation and cellular functionSantander, Verónica SilvinCampetelli, Alexis NazarenoMonesterolo, Noelia EdithRivelli Antonelli, Juan FrancoNigra, Ayelén DeniseArce, Carlos AngelCasale, Cesar HoracioNA, K-ATPASETUBULININTERACTIONREGULATIONMEMBRANESERYTHROCYTESHOMEOSTASIShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1A new function for tubulin was described by our laboratory: acetylated tubulin forms a complex with Na+,K+-ATPase (NKA) and inhibits its activity. This process was shown to be a regulatory factor of physiological importance in cultured cells, human erythrocytes and several rat tissues. Formation of the acetylated tubulin/NKA complex is reversible. We demonstrated that in cultured cells, high concentrations of glucose induce translocation of acetylated tubulin from cytoplasm to plasma membrane with a consequent inhibition of NKA activity. This effect is reversed by adding glutamate, which is co-transported to the cell with Na+. Another post-translational modification of tubulin, detyrosinated tubulin, is also involved in the regulation of NKA activity: it enhances the NKA inhibition induced by acetylated tubulin. Manipulation of the content of these modifications of tubulin could work as a new strategy to maintain homeostasis of Na+ and K+, and to regulate a variety of functions in which NKA is involved, such as osmotic fragility and deformability of human erythrocytes. The results summarized in this review show that the interaction between tubulin and NKA plays an important role in cellular physiology, both in the regulation of Na+/K+ homeostasis and in the rheological properties of the cells, which is mechanically different from other roles reported up to now.Fil: Santander, Verónica Silvin. 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: Campetelli, Alexis Nazareno. Universidad Nacional de Rio Cuarto. Facultad de Cs.exactas Fisicoquimicas y Naturales. Instituto de Biotecnologia Ambiental y Salud. - Consejo Nacional de Investigaciones Cientificas y Tecnicas. Centro Cientifico Tecnologico Conicet - Cordoba. Instituto de Biotecnologia Ambiental y Salud.; ArgentinaFil: Monesterolo, Noelia Edith. Universidad Nacional de Rio Cuarto. Facultad de Cs.exactas Fisicoquimicas y Naturales. Instituto de Biotecnologia Ambiental y Salud. - Consejo Nacional de Investigaciones Cientificas y Tecnicas. Centro Cientifico Tecnologico Conicet - Cordoba. Instituto de Biotecnologia Ambiental y Salud.; ArgentinaFil: Rivelli Antonelli, Juan Franco. Universidad Nacional de Rio Cuarto. Facultad de Cs.exactas Fisicoquimicas y Naturales. Instituto de Biotecnologia Ambiental y Salud. - Consejo Nacional de Investigaciones Cientificas y Tecnicas. Centro Cientifico Tecnologico Conicet - Cordoba. Instituto de Biotecnologia Ambiental y Salud.; ArgentinaFil: Nigra, Ayelén Denise. 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: 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. Universidad Nacional de Rio Cuarto. Facultad de Cs.exactas Fisicoquimicas y Naturales. Instituto de Biotecnologia Ambiental y Salud. - Consejo Nacional de Investigaciones Cientificas y Tecnicas. Centro Cientifico Tecnologico Conicet - Cordoba. Instituto de Biotecnologia Ambiental y Salud.; ArgentinaWiley-liss, Div John Wiley & Sons Inc2018-10-30info: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/11336/104408Santander, Verónica Silvin; Campetelli, Alexis Nazareno; Monesterolo, Noelia Edith; Rivelli Antonelli, Juan Franco; Nigra, Ayelén Denise; et al.; Tubulin–Na + , K + ‐ATPase interaction: Involvement in enzymatic regulation and cellular function; Wiley-liss, Div John Wiley & Sons Inc; Journal of Cellular Physiology; 234; 6; 30-10-2018; 7752-77630021-95411097-4652CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://doi.wiley.com/10.1002/jcp.27610info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pubmed/30378111info:eu-repo/semantics/altIdentifier/doi/10.1002/jcp.27610info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1002/jcp.27610info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T12:13:59Zoai:ri.conicet.gov.ar:11336/104408instacron: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:34982025-10-22 12:14:00.072CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Tubulin–Na + , K + ‐ATPase interaction: Involvement in enzymatic regulation and cellular function
title Tubulin–Na + , K + ‐ATPase interaction: Involvement in enzymatic regulation and cellular function
spellingShingle Tubulin–Na + , K + ‐ATPase interaction: Involvement in enzymatic regulation and cellular function
Santander, Verónica Silvin
NA, K-ATPASE
TUBULIN
INTERACTION
REGULATION
MEMBRANES
ERYTHROCYTES
HOMEOSTASIS
title_short Tubulin–Na + , K + ‐ATPase interaction: Involvement in enzymatic regulation and cellular function
title_full Tubulin–Na + , K + ‐ATPase interaction: Involvement in enzymatic regulation and cellular function
title_fullStr Tubulin–Na + , K + ‐ATPase interaction: Involvement in enzymatic regulation and cellular function
title_full_unstemmed Tubulin–Na + , K + ‐ATPase interaction: Involvement in enzymatic regulation and cellular function
title_sort Tubulin–Na + , K + ‐ATPase interaction: Involvement in enzymatic regulation and cellular function
dc.creator.none.fl_str_mv Santander, Verónica Silvin
Campetelli, Alexis Nazareno
Monesterolo, Noelia Edith
Rivelli Antonelli, Juan Franco
Nigra, Ayelén Denise
Arce, Carlos Angel
Casale, Cesar Horacio
author Santander, Verónica Silvin
author_facet Santander, Verónica Silvin
Campetelli, Alexis Nazareno
Monesterolo, Noelia Edith
Rivelli Antonelli, Juan Franco
Nigra, Ayelén Denise
Arce, Carlos Angel
Casale, Cesar Horacio
author_role author
author2 Campetelli, Alexis Nazareno
Monesterolo, Noelia Edith
Rivelli Antonelli, Juan Franco
Nigra, Ayelén Denise
Arce, Carlos Angel
Casale, Cesar Horacio
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv NA, K-ATPASE
TUBULIN
INTERACTION
REGULATION
MEMBRANES
ERYTHROCYTES
HOMEOSTASIS
topic NA, K-ATPASE
TUBULIN
INTERACTION
REGULATION
MEMBRANES
ERYTHROCYTES
HOMEOSTASIS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv A new function for tubulin was described by our laboratory: acetylated tubulin forms a complex with Na+,K+-ATPase (NKA) and inhibits its activity. This process was shown to be a regulatory factor of physiological importance in cultured cells, human erythrocytes and several rat tissues. Formation of the acetylated tubulin/NKA complex is reversible. We demonstrated that in cultured cells, high concentrations of glucose induce translocation of acetylated tubulin from cytoplasm to plasma membrane with a consequent inhibition of NKA activity. This effect is reversed by adding glutamate, which is co-transported to the cell with Na+. Another post-translational modification of tubulin, detyrosinated tubulin, is also involved in the regulation of NKA activity: it enhances the NKA inhibition induced by acetylated tubulin. Manipulation of the content of these modifications of tubulin could work as a new strategy to maintain homeostasis of Na+ and K+, and to regulate a variety of functions in which NKA is involved, such as osmotic fragility and deformability of human erythrocytes. The results summarized in this review show that the interaction between tubulin and NKA plays an important role in cellular physiology, both in the regulation of Na+/K+ homeostasis and in the rheological properties of the cells, which is mechanically different from other roles reported up to now.
Fil: Santander, Verónica Silvin. 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: Campetelli, Alexis Nazareno. Universidad Nacional de Rio Cuarto. Facultad de Cs.exactas Fisicoquimicas y Naturales. Instituto de Biotecnologia Ambiental y Salud. - Consejo Nacional de Investigaciones Cientificas y Tecnicas. Centro Cientifico Tecnologico Conicet - Cordoba. Instituto de Biotecnologia Ambiental y Salud.; Argentina
Fil: Monesterolo, Noelia Edith. Universidad Nacional de Rio Cuarto. Facultad de Cs.exactas Fisicoquimicas y Naturales. Instituto de Biotecnologia Ambiental y Salud. - Consejo Nacional de Investigaciones Cientificas y Tecnicas. Centro Cientifico Tecnologico Conicet - Cordoba. Instituto de Biotecnologia Ambiental y Salud.; Argentina
Fil: Rivelli Antonelli, Juan Franco. Universidad Nacional de Rio Cuarto. Facultad de Cs.exactas Fisicoquimicas y Naturales. Instituto de Biotecnologia Ambiental y Salud. - Consejo Nacional de Investigaciones Cientificas y Tecnicas. Centro Cientifico Tecnologico Conicet - Cordoba. Instituto de Biotecnologia Ambiental y Salud.; Argentina
Fil: Nigra, Ayelén Denise. 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: 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. Universidad Nacional de Rio Cuarto. Facultad de Cs.exactas Fisicoquimicas y Naturales. Instituto de Biotecnologia Ambiental y Salud. - Consejo Nacional de Investigaciones Cientificas y Tecnicas. Centro Cientifico Tecnologico Conicet - Cordoba. Instituto de Biotecnologia Ambiental y Salud.; Argentina
description A new function for tubulin was described by our laboratory: acetylated tubulin forms a complex with Na+,K+-ATPase (NKA) and inhibits its activity. This process was shown to be a regulatory factor of physiological importance in cultured cells, human erythrocytes and several rat tissues. Formation of the acetylated tubulin/NKA complex is reversible. We demonstrated that in cultured cells, high concentrations of glucose induce translocation of acetylated tubulin from cytoplasm to plasma membrane with a consequent inhibition of NKA activity. This effect is reversed by adding glutamate, which is co-transported to the cell with Na+. Another post-translational modification of tubulin, detyrosinated tubulin, is also involved in the regulation of NKA activity: it enhances the NKA inhibition induced by acetylated tubulin. Manipulation of the content of these modifications of tubulin could work as a new strategy to maintain homeostasis of Na+ and K+, and to regulate a variety of functions in which NKA is involved, such as osmotic fragility and deformability of human erythrocytes. The results summarized in this review show that the interaction between tubulin and NKA plays an important role in cellular physiology, both in the regulation of Na+/K+ homeostasis and in the rheological properties of the cells, which is mechanically different from other roles reported up to now.
publishDate 2018
dc.date.none.fl_str_mv 2018-10-30
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/11336/104408
Santander, Verónica Silvin; Campetelli, Alexis Nazareno; Monesterolo, Noelia Edith; Rivelli Antonelli, Juan Franco; Nigra, Ayelén Denise; et al.; Tubulin–Na + , K + ‐ATPase interaction: Involvement in enzymatic regulation and cellular function; Wiley-liss, Div John Wiley & Sons Inc; Journal of Cellular Physiology; 234; 6; 30-10-2018; 7752-7763
0021-9541
1097-4652
CONICET Digital
CONICET
url http://hdl.handle.net/11336/104408
identifier_str_mv Santander, Verónica Silvin; Campetelli, Alexis Nazareno; Monesterolo, Noelia Edith; Rivelli Antonelli, Juan Franco; Nigra, Ayelén Denise; et al.; Tubulin–Na + , K + ‐ATPase interaction: Involvement in enzymatic regulation and cellular function; Wiley-liss, Div John Wiley & Sons Inc; Journal of Cellular Physiology; 234; 6; 30-10-2018; 7752-7763
0021-9541
1097-4652
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://doi.wiley.com/10.1002/jcp.27610
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pubmed/30378111
info:eu-repo/semantics/altIdentifier/doi/10.1002/jcp.27610
info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1002/jcp.27610
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-liss, Div John Wiley & Sons Inc
publisher.none.fl_str_mv Wiley-liss, Div John Wiley & Sons 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 12.982451

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