Defining the role of a FYVE domain in the localization and activity of a cAMP phosphodiesterase implicated in osmoregulation in Trypanosoma cruzi

Autores
Schoijet, A.C.; Miranda, K.; Medeiros, L.C.S.; De Souza, W.; Flawiá, M.M.; Torres, H.N.; Pignataro, O.P.; Docampo, R.; Alonso, G.D.
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Intracellular levels of cyclic nucleotide second messengers are regulated predominantly by a large superfamily of phosphodiesterases (PDEs). Trypanosoma cruzi, the causative agent of Chagas disease, encodes four different PDE families. One of these PDEs, T. cruzi PDE C2 (TcrPDEC2) has been characterized as a FYVE domain containing protein. Here, we report a novel role for TcrPDEC2 in osmoregulation in T. cruzi and reveal the relevance of its FYVE domain. Our data show that treatment of epimastigotes with TcrPDEC2 inhibitors improves their regulatory volume decrease, whereas cells overexpressing this enzyme are unaffected by the same inhibitors. Consistent with these results, TcrPDEC2 localizes to the contractile vacuole complex, showing strong labelling in the region corresponding to the spongiome. Furthermore, transgenic parasites overexpressing a truncated version of TcrPDEC2 without the FYVE domain show a failure in its targeting to the contractile vacuole complex and a marked decrease in PDE activity, supporting the importance of this domain to the localization and activity of TcrPDEC2. Taking together, the results here presented are consistent with the importance of the cyclic AMP signalling pathway in regulatory volume decrease and implicate TcrPDEC2 as a specifically localized PDE involved in osmoregulation in T. cruzi. © 2010 Blackwell Publishing Ltd.
Fil:Schoijet, A.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Flawiá, M.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Torres, H.N. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Pignataro, O.P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Alonso, G.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fuente
Mol. Microbiol. 2011;79(1):50-62
Materia
cyclic AMP phosphodiesterase
article
cell vacuole
controlled study
enzyme activity
epimastigote
gene overexpression
immunofluorescence microscopy
nonhuman
osmoregulation
priority journal
protein binding
protein domain
protein localization
radioimmunoassay
signal transduction
transgene
Trypanosoma cruzi
3',5'-Cyclic-AMP Phosphodiesterases
Enzyme Inhibitors
Gene Expression
Microscopy, Immunoelectron
Protein Structure, Tertiary
Trypanosoma cruzi
Vacuoles
Water-Electrolyte Balance
Trypanosoma cruzi
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/2.5/ar
Repositorio
Biblioteca Digital (UBA-FCEN)
Institución
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
OAI Identificador
paperaa:paper_0950382X_v79_n1_p50_Schoijet
Acceder
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oai_identifier_str paperaa:paper_0950382X_v79_n1_p50_Schoijet
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling Defining the role of a FYVE domain in the localization and activity of a cAMP phosphodiesterase implicated in osmoregulation in Trypanosoma cruziSchoijet, A.C.Miranda, K.Medeiros, L.C.S.De Souza, W.Flawiá, M.M.Torres, H.N.Pignataro, O.P.Docampo, R.Alonso, G.D.cyclic AMP phosphodiesterasearticlecell vacuolecontrolled studyenzyme activityepimastigotegene overexpressionimmunofluorescence microscopynonhumanosmoregulationpriority journalprotein bindingprotein domainprotein localizationradioimmunoassaysignal transductiontransgeneTrypanosoma cruzi3',5'-Cyclic-AMP PhosphodiesterasesEnzyme InhibitorsGene ExpressionMicroscopy, ImmunoelectronProtein Structure, TertiaryTrypanosoma cruziVacuolesWater-Electrolyte BalanceTrypanosoma cruziIntracellular levels of cyclic nucleotide second messengers are regulated predominantly by a large superfamily of phosphodiesterases (PDEs). Trypanosoma cruzi, the causative agent of Chagas disease, encodes four different PDE families. One of these PDEs, T. cruzi PDE C2 (TcrPDEC2) has been characterized as a FYVE domain containing protein. Here, we report a novel role for TcrPDEC2 in osmoregulation in T. cruzi and reveal the relevance of its FYVE domain. Our data show that treatment of epimastigotes with TcrPDEC2 inhibitors improves their regulatory volume decrease, whereas cells overexpressing this enzyme are unaffected by the same inhibitors. Consistent with these results, TcrPDEC2 localizes to the contractile vacuole complex, showing strong labelling in the region corresponding to the spongiome. Furthermore, transgenic parasites overexpressing a truncated version of TcrPDEC2 without the FYVE domain show a failure in its targeting to the contractile vacuole complex and a marked decrease in PDE activity, supporting the importance of this domain to the localization and activity of TcrPDEC2. Taking together, the results here presented are consistent with the importance of the cyclic AMP signalling pathway in regulatory volume decrease and implicate TcrPDEC2 as a specifically localized PDE involved in osmoregulation in T. cruzi. © 2010 Blackwell Publishing Ltd.Fil:Schoijet, A.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Flawiá, M.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Torres, H.N. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Pignataro, O.P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Alonso, G.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.2011info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12110/paper_0950382X_v79_n1_p50_SchoijetMol. Microbiol. 2011;79(1):50-62reponame:Biblioteca Digital (UBA-FCEN)instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesinstacron:UBA-FCENenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/ar2025-09-04T09:48:48Zpaperaa:paper_0950382X_v79_n1_p50_SchoijetInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-09-04 09:48:49.64Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
dc.title.none.fl_str_mv Defining the role of a FYVE domain in the localization and activity of a cAMP phosphodiesterase implicated in osmoregulation in Trypanosoma cruzi
title Defining the role of a FYVE domain in the localization and activity of a cAMP phosphodiesterase implicated in osmoregulation in Trypanosoma cruzi
spellingShingle Defining the role of a FYVE domain in the localization and activity of a cAMP phosphodiesterase implicated in osmoregulation in Trypanosoma cruzi
Schoijet, A.C.
cyclic AMP phosphodiesterase
article
cell vacuole
controlled study
enzyme activity
epimastigote
gene overexpression
immunofluorescence microscopy
nonhuman
osmoregulation
priority journal
protein binding
protein domain
protein localization
radioimmunoassay
signal transduction
transgene
Trypanosoma cruzi
3',5'-Cyclic-AMP Phosphodiesterases
Enzyme Inhibitors
Gene Expression
Microscopy, Immunoelectron
Protein Structure, Tertiary
Trypanosoma cruzi
Vacuoles
Water-Electrolyte Balance
Trypanosoma cruzi
title_short Defining the role of a FYVE domain in the localization and activity of a cAMP phosphodiesterase implicated in osmoregulation in Trypanosoma cruzi
title_full Defining the role of a FYVE domain in the localization and activity of a cAMP phosphodiesterase implicated in osmoregulation in Trypanosoma cruzi
title_fullStr Defining the role of a FYVE domain in the localization and activity of a cAMP phosphodiesterase implicated in osmoregulation in Trypanosoma cruzi
title_full_unstemmed Defining the role of a FYVE domain in the localization and activity of a cAMP phosphodiesterase implicated in osmoregulation in Trypanosoma cruzi
title_sort Defining the role of a FYVE domain in the localization and activity of a cAMP phosphodiesterase implicated in osmoregulation in Trypanosoma cruzi
dc.creator.none.fl_str_mv Schoijet, A.C.
Miranda, K.
Medeiros, L.C.S.
De Souza, W.
Flawiá, M.M.
Torres, H.N.
Pignataro, O.P.
Docampo, R.
Alonso, G.D.
author Schoijet, A.C.
author_facet Schoijet, A.C.
Miranda, K.
Medeiros, L.C.S.
De Souza, W.
Flawiá, M.M.
Torres, H.N.
Pignataro, O.P.
Docampo, R.
Alonso, G.D.
author_role author
author2 Miranda, K.
Medeiros, L.C.S.
De Souza, W.
Flawiá, M.M.
Torres, H.N.
Pignataro, O.P.
Docampo, R.
Alonso, G.D.
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv cyclic AMP phosphodiesterase
article
cell vacuole
controlled study
enzyme activity
epimastigote
gene overexpression
immunofluorescence microscopy
nonhuman
osmoregulation
priority journal
protein binding
protein domain
protein localization
radioimmunoassay
signal transduction
transgene
Trypanosoma cruzi
3',5'-Cyclic-AMP Phosphodiesterases
Enzyme Inhibitors
Gene Expression
Microscopy, Immunoelectron
Protein Structure, Tertiary
Trypanosoma cruzi
Vacuoles
Water-Electrolyte Balance
Trypanosoma cruzi
topic cyclic AMP phosphodiesterase
article
cell vacuole
controlled study
enzyme activity
epimastigote
gene overexpression
immunofluorescence microscopy
nonhuman
osmoregulation
priority journal
protein binding
protein domain
protein localization
radioimmunoassay
signal transduction
transgene
Trypanosoma cruzi
3',5'-Cyclic-AMP Phosphodiesterases
Enzyme Inhibitors
Gene Expression
Microscopy, Immunoelectron
Protein Structure, Tertiary
Trypanosoma cruzi
Vacuoles
Water-Electrolyte Balance
Trypanosoma cruzi
dc.description.none.fl_txt_mv Intracellular levels of cyclic nucleotide second messengers are regulated predominantly by a large superfamily of phosphodiesterases (PDEs). Trypanosoma cruzi, the causative agent of Chagas disease, encodes four different PDE families. One of these PDEs, T. cruzi PDE C2 (TcrPDEC2) has been characterized as a FYVE domain containing protein. Here, we report a novel role for TcrPDEC2 in osmoregulation in T. cruzi and reveal the relevance of its FYVE domain. Our data show that treatment of epimastigotes with TcrPDEC2 inhibitors improves their regulatory volume decrease, whereas cells overexpressing this enzyme are unaffected by the same inhibitors. Consistent with these results, TcrPDEC2 localizes to the contractile vacuole complex, showing strong labelling in the region corresponding to the spongiome. Furthermore, transgenic parasites overexpressing a truncated version of TcrPDEC2 without the FYVE domain show a failure in its targeting to the contractile vacuole complex and a marked decrease in PDE activity, supporting the importance of this domain to the localization and activity of TcrPDEC2. Taking together, the results here presented are consistent with the importance of the cyclic AMP signalling pathway in regulatory volume decrease and implicate TcrPDEC2 as a specifically localized PDE involved in osmoregulation in T. cruzi. © 2010 Blackwell Publishing Ltd.
Fil:Schoijet, A.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Flawiá, M.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Torres, H.N. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Pignataro, O.P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Alonso, G.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
description Intracellular levels of cyclic nucleotide second messengers are regulated predominantly by a large superfamily of phosphodiesterases (PDEs). Trypanosoma cruzi, the causative agent of Chagas disease, encodes four different PDE families. One of these PDEs, T. cruzi PDE C2 (TcrPDEC2) has been characterized as a FYVE domain containing protein. Here, we report a novel role for TcrPDEC2 in osmoregulation in T. cruzi and reveal the relevance of its FYVE domain. Our data show that treatment of epimastigotes with TcrPDEC2 inhibitors improves their regulatory volume decrease, whereas cells overexpressing this enzyme are unaffected by the same inhibitors. Consistent with these results, TcrPDEC2 localizes to the contractile vacuole complex, showing strong labelling in the region corresponding to the spongiome. Furthermore, transgenic parasites overexpressing a truncated version of TcrPDEC2 without the FYVE domain show a failure in its targeting to the contractile vacuole complex and a marked decrease in PDE activity, supporting the importance of this domain to the localization and activity of TcrPDEC2. Taking together, the results here presented are consistent with the importance of the cyclic AMP signalling pathway in regulatory volume decrease and implicate TcrPDEC2 as a specifically localized PDE involved in osmoregulation in T. cruzi. © 2010 Blackwell Publishing Ltd.
publishDate 2011
dc.date.none.fl_str_mv 2011
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/20.500.12110/paper_0950382X_v79_n1_p50_Schoijet
url http://hdl.handle.net/20.500.12110/paper_0950382X_v79_n1_p50_Schoijet
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/2.5/ar
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/2.5/ar
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv Mol. Microbiol. 2011;79(1):50-62
reponame:Biblioteca Digital (UBA-FCEN)
instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron:UBA-FCEN
reponame_str Biblioteca Digital (UBA-FCEN)
collection Biblioteca Digital (UBA-FCEN)
instname_str Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron_str UBA-FCEN
institution UBA-FCEN
repository.name.fl_str_mv Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
repository.mail.fl_str_mv ana@bl.fcen.uba.ar
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