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Genes 2018, 9(3), 160; https://doi.org/10.3390/genes9030160

Caenorhabditis elegans BRICHOS Domain–Containing Protein C09F5.1 Maintains Thermotolerance and Decreases Cytotoxicity of Aβ42 by Activating the UPR

1
Department of Life Science, Sogang University, Seoul 04107, Korea
2
LG Household & Health Care, Daejeon 34114, Korea
3
Department of Medicine, Biomedical Research Institute, Seoul National University Hospital, Seoul 03080, Korea
4
Amorepacific R&D Center, Yongin 17074, Korea
5
Department of Chemical Engineering, Hankyung National University, Anseong 17579, Korea
*
Author to whom correspondence should be addressed.
Received: 11 December 2017 / Revised: 5 March 2018 / Accepted: 9 March 2018 / Published: 13 March 2018
(This article belongs to the Section Molecular Genetics and Genomics)
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Abstract

Caenorhabditis elegans C09F5.1 is a nematode-specific gene that encodes a type II transmembrane protein containing the BRICHOS domain. The gene was isolated as a heat-sensitive mutant, but the function of the protein remained unclear. We examined the expression pattern and subcellular localization of C09F5.1 as well as its roles in thermotolerance and chaperone function. Expression of C09F5.1 under heat shock conditions was induced in a heat shock factor 1 (HSF-1)–dependent manner. However, under normal growth conditions, most cells types exposed to mechanical stimuli expressed C09F5.1. Knockdown of C09F5.1 expression or deletion of the N-terminal domain decreased thermotolerance. The BRICHOS domain of C09F5.1 did not exhibit chaperone function unlike those of other proteins containing this domain, but the domain was essential for the proper subcellular localization of the protein. Intact C09F5.1 was localized to the Golgi body, but the N-terminal domain of C09F5.1 (C09F5.1-NTD) was retained in the ER. C09F5.1-NTD delayed paralysis by beta-amyloid (1-42) protein (Aβ42) in Alzheimer’s disease model worms (CL4176) and activated the unfolded protein response (UPR) by interacting with Aβ42. An intrinsically disordered region (IDR) located at the N-terminus of C09F5.1 may be responsible for the chaperone function of C09F5.1-NTD. Taken together, the data suggest that C09F5.1 triggers the UPR by interacting with abnormal proteins. View Full-Text
Keywords: BRICHOS domain; thermotolerance; chaperone; beta-amyloid (1-42); unfolded protein response BRICHOS domain; thermotolerance; chaperone; beta-amyloid (1-42); unfolded protein response
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Song, M.; Song, K.; Kim, S.; Lee, J.; Hwang, S.; Han, C. Caenorhabditis elegans BRICHOS Domain–Containing Protein C09F5.1 Maintains Thermotolerance and Decreases Cytotoxicity of Aβ42 by Activating the UPR. Genes 2018, 9, 160.

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