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

• Verfasst von: Erben, Esteban D. [VerfasserIn]
• Verfasst von: Nardelli, Sheila C. [VerfasserIn]
• Verfasst von: Jesus, Teresa C. L. de [VerfasserIn]
• Verfasst von: Schenkman, Sergio [VerfasserIn]
• Verfasst von: Tellez‐Iñon, Maria T. [VerfasserIn]
• Titel: Trypanosomatid pin1-type peptidyl-prolyl isomerase is cytosolic and not essential for cell proliferation
• Verf.angabe: Esteban D. Erben, Sheila C. Nardelli, Teresa C.L. de Jesus, Sergio Schenkman & Maria T. Tellez‐Iñon
• Jahr: 2013
• Jahr des Originals: 2012
• Umfang: 5 S.
• Fussnoten: First published: 03 December 2012 ; Gesehen am 17.02.2021
• Titel Quelle: Enthalten in: The journal of eukaryotic microbiology
• Ort Quelle: Oxford [u.a.] : Wiley-Blackwell, 1954
• Jahr Quelle: 2013
• Band/Heft Quelle: 60(2013), 1, Seite 101-105
• ISSN Quelle: 1550-7408
• DOI: doi:10.1111/jeu.12009
• Datenträger: Online-Ressource
• Sprache: eng
• Sach-SW: MORN domain
• Sach-SW: parvulin
• Sach-SW: peptidyl-prolyl isomerase
• Sach-SW: Pin1
• Sach-SW: PPIase
• Sach-SW: Trypanosoma cruzi
• K10plus-PPN: 174849225X

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.