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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/3974
Acceder
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network_name_str CONICET Digital (CONICET)
spelling 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 Técnicas2025-09-29T10:41:35Zoai: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:34982025-09-29 10:41:35.569CONICET 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
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv 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
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1111/jeu.12009/abstract
info:eu-repo/semantics/altIdentifier/wos/http://dx.doi.org/DOI:10.1111/jeu.12009
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
publisher.none.fl_str_mv Wiley
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 13.070432

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