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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2011
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0950382X_v79_n1_p50_Schoijet http://hdl.handle.net/20.500.12110/paper_0950382X_v79_n1_p50_Schoijet |
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paper:paper_0950382X_v79_n1_p50_Schoijet2023-06-08T15:54:26Z Defining the role of a FYVE domain in the localization and activity of a cAMP phosphodiesterase implicated in osmoregulation in Trypanosoma cruzi Schoijet, Alejandra Cecilia Flawiá, Mirtha María Torres, Héctor Norberto Pignataro, Omar Pedro Alonso, Guillermo Daniel 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 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. 2011 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0950382X_v79_n1_p50_Schoijet http://hdl.handle.net/20.500.12110/paper_0950382X_v79_n1_p50_Schoijet |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (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, Alejandra Cecilia Flawiá, Mirtha María Torres, Héctor Norberto Pignataro, Omar Pedro Alonso, Guillermo Daniel 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. |
| author |
Schoijet, Alejandra Cecilia Flawiá, Mirtha María Torres, Héctor Norberto Pignataro, Omar Pedro Alonso, Guillermo Daniel |
| author_facet |
Schoijet, Alejandra Cecilia Flawiá, Mirtha María Torres, Héctor Norberto Pignataro, Omar Pedro Alonso, Guillermo Daniel |
| author_sort |
Schoijet, Alejandra Cecilia |
| 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 |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0950382X_v79_n1_p50_Schoijet http://hdl.handle.net/20.500.12110/paper_0950382X_v79_n1_p50_Schoijet |
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