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

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 character...

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Autores principales: 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.
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Publicado: 2011
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_0950382X_v79_n1_p50_Schoijet
https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_0950382X_v79_n1_p50_Schoijet_oai
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spelling I28-R145-paper_0950382X_v79_n1_p50_Schoijet_oai2024-08-16 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. 2011 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. application/pdf http://hdl.handle.net/20.500.12110/paper_0950382X_v79_n1_p50_Schoijet info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar Mol. Microbiol. 2011;79(1):50-62 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 Defining the role of a FYVE domain in the localization and activity of a cAMP phosphodiesterase implicated in osmoregulation in Trypanosoma cruzi info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_0950382X_v79_n1_p50_Schoijet_oai
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-145
collection Repositorio Digital de la Universidad de Buenos Aires (UBA)
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
spellingShingle 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
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.
Defining the role of a FYVE domain in the localization and activity of a cAMP phosphodiesterase implicated in osmoregulation in Trypanosoma cruzi
topic_facet 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
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.
format Artículo
Artículo
publishedVersion
author 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_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_sort Schoijet, A.C.
title Defining the role of a FYVE domain in the localization and activity of a cAMP phosphodiesterase implicated in osmoregulation in 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
publishDate 2011
url http://hdl.handle.net/20.500.12110/paper_0950382X_v79_n1_p50_Schoijet
https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_0950382X_v79_n1_p50_Schoijet_oai
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