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

Date
2013-01-01Author
Erben, Esteban D.
Nardelli, Sheila C. [UNIFESP]
Jesus, Teresa C. L. de [UNIFESP]
Schenkman, Sergio [UNIFESP]
Tellez-Inon, Maria T.
Type
ArtigoISSN
1066-5234Is part of
Journal of Eukaryotic MicrobiologyDOI
10.1111/jeu.12009Metadata
Show full item recordAbstract
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.
Citation
Journal of Eukaryotic Microbiology. Hoboken: Wiley-Blackwell, v. 60, n. 1, p. 101-105, 2013.Sponsorship
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)
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