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Trypanosomatid pin1-type peptidyl-prolyl isomerase is cytosolic and not essential for cell proliferation

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 localizat...

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Bibliographische Detailangaben
Hauptverfasser: Erben, Esteban D. (VerfasserIn) , Nardelli, Sheila C. (VerfasserIn) , Jesus, Teresa C. L. de (VerfasserIn) , Schenkman, Sergio (VerfasserIn) , Tellez‐Iñon, Maria T. (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 2013
In: The journal of eukaryotic microbiology
Year: 2012, Jahrgang: 60, Heft: 1, Pages: 101-105
ISSN:1550-7408
DOI:https://doi.org/10.1111/jeu.12009
Online-Zugang:Verlag, lizenzpflichtig, Volltext: https://doi.org/https://doi.org/10.1111/jeu.12009
Verlag, lizenzpflichtig, Volltext: https://onlinelibrary.wiley.com/doi/abs/10.1111/jeu.12009
Volltext
Verfasserangaben:Esteban D. Erben, Sheila C. Nardelli, Teresa C.L. de Jesus, Sergio Schenkman & Maria T. Tellez‐Iñon
Beschreibung
Zusammenfassung: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.
Beschreibung:First published: 03 December 2012
Gesehen am 17.02.2021
Beschreibung:Online Resource
ISSN:1550-7408
DOI:https://doi.org/10.1111/jeu.12009

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