Unfolded Protein Response Pathways in Bloodstream-Form Trypanosoma brucei?

Eukaryotic Cell
Calvin TiengweJames D Bangs

Abstract

The unfolded protein response (UPR) is a stress mechanism to cope with misfolded proteins in the early secretory pathway, the hallmark being transcriptional upregulation of endoplasmic reticulum (ER) molecular chaperones such as BiP and protein disulfide isomerase. Despite the lack of transcriptional regulation and the absence of the classical UPR machinery, African trypanosomes apparently respond to persistent ER stress by a UPR-like response, including upregulation of BiP, and a related spliced leader silencing (SLS) response whereby SL RNA transcription is shut down. Initially observed by knockdown of the secretory protein translocation machinery, both responses are also induced by chemical agents known to elicit UPR in mammalian cells (H. Goldshmidt, D. Matas, A. Kabi, A. Carmi, R. Hope, S. Michaeli, PLoS Pathog 6:e1000731, 2010, http://dx.doi.org/10.1371/journal.ppat.1000731). As these findings were generated primarily in procyclic-stage trypanosomes, we have investigated both responses in pathogenic bloodstream-stage parasites. RNA interference (RNAi) silencing of the core translocon subunit Trypanosoma brucei Sec61α (TbSec61α) failed to induce either response. Interestingly, cell growth halted within 16 h of silencing, b...Continue Reading

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Citations

Oct 26, 2016·Cellular Microbiology·Calvin TiengweJames D Bangs
Oct 6, 2020·PLoS Neglected Tropical Diseases·Marco Túlio Alves da SilvaOtavio Henrique Thiemann
Dec 23, 2020·Molecular and Biochemical Parasitology·Isabella E MaudlinMark Carrington
Aug 23, 2019·Experimental Cell Research·Jana Messias SandesRegina Celia Bressan Queiroz Figueiredo
May 18, 2021·Parasitology International·Coh-Ichi Nihei, Masayuki Nakanishi

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