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Role of Selenoprotein F in Protein Folding and Secretion: Potential Involvement in Human Disease

by Bingyu Ren 1,2, Min Liu 1,3, Jiazuan Ni 3,4 and Jing Tian 1,3,4,*
1
Shenzhen Key Laboratory of Marine Biotechnology and Ecology, Department of Marine Biology, Shenzhen University, Shenzhen 518060, China
2
Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun 130022, China
3
Shenzhen Engineering Laboratory for Marine Algal Biotechnology, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen 518060, China
4
Shenzhen Key Laboratory of Microbial Genetic Engineering, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen 518060, China
*
Author to whom correspondence should be addressed.
Nutrients 2018, 10(11), 1619; https://doi.org/10.3390/nu10111619
Received: 29 September 2018 / Revised: 20 October 2018 / Accepted: 23 October 2018 / Published: 2 November 2018
(This article belongs to the Special Issue The Role of Selenium in Health and Disease)
Selenoproteins form a group of proteins of which its members contain at least one selenocysteine, and most of them serve oxidoreductase functions. Selenoprotein F (SELENOF), one of the 25 currently identified selenoproteins, is located in the endoplasmic reticulum (ER) organelle and is abundantly expressed in many tissues. It is regulated according to its selenium status, as well as by cell stress conditions. SELENOF may be functionally linked to protein folding and the secretion process in the ER. Several studies have reported positive associations between SELENOF genetic variations and several types of cancer. Also, altered expression levels of SELENOF have been found in cancer cases and neurodegenerative diseases. In this review, we summarize the current understanding of the structure, expression, and potential function of SELENOF and discuss its possible relation with various pathological processes. View Full-Text
Keywords: selenium; selenoprotein F; thiol–disulfide oxidoreductase; endoplasmic reticulum stress; protein folding quality control; single nucleotide polymorphisms selenium; selenoprotein F; thiol–disulfide oxidoreductase; endoplasmic reticulum stress; protein folding quality control; single nucleotide polymorphisms
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Ren, B.; Liu, M.; Ni, J.; Tian, J. Role of Selenoprotein F in Protein Folding and Secretion: Potential Involvement in Human Disease. Nutrients 2018, 10, 1619.

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