Trypanosomatid Pin1-Type Peptidyl-Prolyl Isomerase Is Cytosolic and Not Essential for Cell Proliferation

Trypanosomatid Pin1-Type Peptidyl-Prolyl Isomerase Is Cytosolic and Not Essential for Cell Proliferation

Author Erben, Esteban D. Google Scholar
Nardelli, Sheila C. Autor UNIFESP Google Scholar
Jesus, Teresa C. L. de Autor UNIFESP Google Scholar
Schenkman, Sergio Autor UNIFESP Google Scholar
Tellez-Inon, Maria T. Google Scholar
Institution INGEBI CONICET
Universidade Federal de São Paulo (UNIFESP)
Abstract 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.
Keywords MORN domain
parvulin
peptidyl-prolyl isomerase
Pin1
PPIase
Trypanosoma cruzi
Language English
Sponsor Consejo Nacional de Investigaciones Cientificas y Tecnicas (CONICET, Argentina)
Agencia Nacional de Promocion Cientifica y Tecnologica (ANPCyT, Argentina)
Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
Date 2013-01-01
Published in Journal of Eukaryotic Microbiology. Hoboken: Wiley-Blackwell, v. 60, n. 1, p. 101-105, 2013.
ISSN 1066-5234 (Sherpa/Romeo, impact factor)
Publisher Wiley-Blackwell
Extent 101-105
Origin http://dx.doi.org/10.1111/jeu.12009
Access rights Closed access
Type Article
Web of Science ID WOS:000313122500012
URI http://repositorio.unifesp.br/handle/11600/35837

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