Trypanosomatid Pin1-type Peptidyl-Prolyl Isomerase is Cytosolic and Not Essential for Cell Proliferation
- Autores
- Erben, Esteban Daniel; Nardelli, Sheila; De Jesus, Teresa C. L.; Schenkman, Sergio; Tellez, Maria Teresa
- Año de publicación
- 2012
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Pin1-type peptidyl-prolyl cis/trans isomerases (PPIases) isomerise the peptide bond of specific phosphorylated (Ser/Thr)-Pro residues, regulating various cellular events. Previously, we reported a Pin1-type PPIase in Trypanosoma cruzi, but little is known about its function and subcellular localization. Immunofluorescence analysis revealed that in contrast with Pin1-like proteins from diverse organisms, TcPin1 mainly localized in the cytoplasm and was excluded from the nuclei. In addition, RNAi-mediated downregulation of TbPin1 in Trypanosoma brucei did not abolish cell proliferation. Using yeast two-hybrid assay, we identified a MORN domain-containing protein as putative Pin1-binding partners. These data suggest that Pin1-mediated signaling mechanism plays a different role in protozoan parasites.
Fil: Erben, Esteban Daniel. Zentrum fur Molekular Biologie Heidelberg; Alemania
Fil: Nardelli, Sheila. Universidade Federal de São Paulo. Departamento de Microbiologia, Imunologia e Parasitologia; Brasil
Fil: De Jesus, Teresa C. L.. Universidade Federal de São Paulo. Departamento de Microbiologia, Imunologia e Parasitologia; Brasil
Fil: Schenkman, Sergio. Universidade Federal de São Paulo. Departamento de Microbiologia, Imunologia e Parasitologia; Brasil
Fil: Tellez, Maria Teresa. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular; Argentina - Materia
-
Pin1-Type Peptidyl-Prolyl Isomerase
Trypansoma Cruzi - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
.jpg)
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/3974
Ver los metadatos del registro completo
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Trypanosomatid Pin1-type Peptidyl-Prolyl Isomerase is Cytosolic and Not Essential for Cell ProliferationErben, Esteban DanielNardelli, SheilaDe Jesus, Teresa C. L.Schenkman, SergioTellez, Maria TeresaPin1-Type Peptidyl-Prolyl IsomeraseTrypansoma Cruzihttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Pin1-type peptidyl-prolyl cis/trans isomerases (PPIases) isomerise the peptide bond of specific phosphorylated (Ser/Thr)-Pro residues, regulating various cellular events. Previously, we reported a Pin1-type PPIase in Trypanosoma cruzi, but little is known about its function and subcellular localization. Immunofluorescence analysis revealed that in contrast with Pin1-like proteins from diverse organisms, TcPin1 mainly localized in the cytoplasm and was excluded from the nuclei. In addition, RNAi-mediated downregulation of TbPin1 in Trypanosoma brucei did not abolish cell proliferation. Using yeast two-hybrid assay, we identified a MORN domain-containing protein as putative Pin1-binding partners. These data suggest that Pin1-mediated signaling mechanism plays a different role in protozoan parasites.Fil: Erben, Esteban Daniel. Zentrum fur Molekular Biologie Heidelberg; AlemaniaFil: Nardelli, Sheila. Universidade Federal de São Paulo. Departamento de Microbiologia, Imunologia e Parasitologia; BrasilFil: De Jesus, Teresa C. L.. Universidade Federal de São Paulo. Departamento de Microbiologia, Imunologia e Parasitologia; BrasilFil: Schenkman, Sergio. Universidade Federal de São Paulo. Departamento de Microbiologia, Imunologia e Parasitologia; BrasilFil: Tellez, Maria Teresa. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular; ArgentinaWiley2012-12-03info: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/11336/3974Erben, Esteban Daniel; Nardelli, Sheila; De Jesus, Teresa C. L.; Schenkman, Sergio; Tellez, Maria Teresa; Trypanosomatid Pin1-type Peptidyl-Prolyl Isomerase is Cytosolic and Not Essential for Cell Proliferation; Wiley; Journal of Eukaryotic Microbiology; 60; 1; 3-12-2012; 101-1051066-5234enginfo:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1111/jeu.12009/abstractinfo:eu-repo/semantics/altIdentifier/wos/http://dx.doi.org/DOI:10.1111/jeu.12009info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T12:14:11Zoai:ri.conicet.gov.ar:11336/3974instacron: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 12:14:11.344CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
| dc.title.none.fl_str_mv |
Trypanosomatid Pin1-type Peptidyl-Prolyl Isomerase is Cytosolic and Not Essential for Cell Proliferation |
| title |
Trypanosomatid Pin1-type Peptidyl-Prolyl Isomerase is Cytosolic and Not Essential for Cell Proliferation |
| spellingShingle |
Trypanosomatid Pin1-type Peptidyl-Prolyl Isomerase is Cytosolic and Not Essential for Cell Proliferation Erben, Esteban Daniel Pin1-Type Peptidyl-Prolyl Isomerase Trypansoma Cruzi |
| title_short |
Trypanosomatid Pin1-type Peptidyl-Prolyl Isomerase is Cytosolic and Not Essential for Cell Proliferation |
| title_full |
Trypanosomatid Pin1-type Peptidyl-Prolyl Isomerase is Cytosolic and Not Essential for Cell Proliferation |
| title_fullStr |
Trypanosomatid Pin1-type Peptidyl-Prolyl Isomerase is Cytosolic and Not Essential for Cell Proliferation |
| title_full_unstemmed |
Trypanosomatid Pin1-type Peptidyl-Prolyl Isomerase is Cytosolic and Not Essential for Cell Proliferation |
| title_sort |
Trypanosomatid Pin1-type Peptidyl-Prolyl Isomerase is Cytosolic and Not Essential for Cell Proliferation |
| dc.creator.none.fl_str_mv |
Erben, Esteban Daniel Nardelli, Sheila De Jesus, Teresa C. L. Schenkman, Sergio Tellez, Maria Teresa |
| author |
Erben, Esteban Daniel |
| author_facet |
Erben, Esteban Daniel Nardelli, Sheila De Jesus, Teresa C. L. Schenkman, Sergio Tellez, Maria Teresa |
| author_role |
author |
| author2 |
Nardelli, Sheila De Jesus, Teresa C. L. Schenkman, Sergio Tellez, Maria Teresa |
| author2_role |
author author author author |
| dc.subject.none.fl_str_mv |
Pin1-Type Peptidyl-Prolyl Isomerase Trypansoma Cruzi |
| topic |
Pin1-Type Peptidyl-Prolyl Isomerase Trypansoma Cruzi |
| purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
| dc.description.none.fl_txt_mv |
Pin1-type peptidyl-prolyl cis/trans isomerases (PPIases) isomerise the peptide bond of specific phosphorylated (Ser/Thr)-Pro residues, regulating various cellular events. Previously, we reported a Pin1-type PPIase in Trypanosoma cruzi, but little is known about its function and subcellular localization. Immunofluorescence analysis revealed that in contrast with Pin1-like proteins from diverse organisms, TcPin1 mainly localized in the cytoplasm and was excluded from the nuclei. In addition, RNAi-mediated downregulation of TbPin1 in Trypanosoma brucei did not abolish cell proliferation. Using yeast two-hybrid assay, we identified a MORN domain-containing protein as putative Pin1-binding partners. These data suggest that Pin1-mediated signaling mechanism plays a different role in protozoan parasites. Fil: Erben, Esteban Daniel. Zentrum fur Molekular Biologie Heidelberg; Alemania Fil: Nardelli, Sheila. Universidade Federal de São Paulo. Departamento de Microbiologia, Imunologia e Parasitologia; Brasil Fil: De Jesus, Teresa C. L.. Universidade Federal de São Paulo. Departamento de Microbiologia, Imunologia e Parasitologia; Brasil Fil: Schenkman, Sergio. Universidade Federal de São Paulo. Departamento de Microbiologia, Imunologia e Parasitologia; Brasil Fil: Tellez, Maria Teresa. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular; Argentina |
| description |
Pin1-type peptidyl-prolyl cis/trans isomerases (PPIases) isomerise the peptide bond of specific phosphorylated (Ser/Thr)-Pro residues, regulating various cellular events. Previously, we reported a Pin1-type PPIase in Trypanosoma cruzi, but little is known about its function and subcellular localization. Immunofluorescence analysis revealed that in contrast with Pin1-like proteins from diverse organisms, TcPin1 mainly localized in the cytoplasm and was excluded from the nuclei. In addition, RNAi-mediated downregulation of TbPin1 in Trypanosoma brucei did not abolish cell proliferation. Using yeast two-hybrid assay, we identified a MORN domain-containing protein as putative Pin1-binding partners. These data suggest that Pin1-mediated signaling mechanism plays a different role in protozoan parasites. |
| publishDate |
2012 |
| dc.date.none.fl_str_mv |
2012-12-03 |
| 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 |
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article |
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publishedVersion |
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http://hdl.handle.net/11336/3974 Erben, Esteban Daniel; Nardelli, Sheila; De Jesus, Teresa C. L.; Schenkman, Sergio; Tellez, Maria Teresa; Trypanosomatid Pin1-type Peptidyl-Prolyl Isomerase is Cytosolic and Not Essential for Cell Proliferation; Wiley; Journal of Eukaryotic Microbiology; 60; 1; 3-12-2012; 101-105 1066-5234 |
| url |
http://hdl.handle.net/11336/3974 |
| identifier_str_mv |
Erben, Esteban Daniel; Nardelli, Sheila; De Jesus, Teresa C. L.; Schenkman, Sergio; Tellez, Maria Teresa; Trypanosomatid Pin1-type Peptidyl-Prolyl Isomerase is Cytosolic and Not Essential for Cell Proliferation; Wiley; Journal of Eukaryotic Microbiology; 60; 1; 3-12-2012; 101-105 1066-5234 |
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eng |
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eng |
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