skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: New insights into the posttranslational regulation of human cytosolic thioredoxin by S-palmitoylation

Abstract

High level of palmitate is associated with metabolic disorders. We recently showed that enhanced level of S-palmitoylated cytosolic thioredoxin (Trx1) in mouse liver was new characteristic feature of insulin resistance. However, our understanding of the effect of S-palmitoylation on Trx1 is limited, and the tissue specificity of Trx1 S-palmitoylation is unclear. Here we show that S-palmitoylation also occurs at Cys73 of Trx1 in living endothelial cells, and the level of S-palmitoylated Trx1 undergoes regulation by insulin signaling. Trx1 prefers thiol-thioester exchange with palmitoyl-CoA to acetyl-CoA. S-palmitoylation alters conformation or secondary structure of Trx1, as well as decreases the ability of Trx1 to transfer electrons from thioredoxin reductase to S-nitrosylated protein–tyrosine phosphatase 1B and S-nitroso-glutathione. Our results demonstrate that S-palmitoylation is an important post-translational modification of human Trx1. - Highlights: • S-palmitoylation occurs at Cys73 of Trx1 in living endothelial cells. • Insulin signaling may regulate level of S-palmitoylated Trx1 in the cells. • S-palmitoylation plays significant effects on Trx1 structure and functions.

Authors:
;
Publication Date:
OSTI Identifier:
22462048
Resource Type:
Journal Article
Journal Name:
Biochemical and Biophysical Research Communications
Additional Journal Information:
Journal Volume: 460; Journal Issue: 4; Other Information: Copyright (c) 2015 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0006-291X
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ANIMAL TISSUES; ELECTRON TRANSFER; GLUCOSAMINE; GLUTATHIONE; HUMAN POPULATIONS; HYDROXYLAMINE; INSULIN; LIGASES; LIVER; MICE; MODIFICATIONS; SIGNALS; SPECIFICITY; THIOLS; TYROSINE

Citation Formats

Xu, Zhiyu, and Zhong, Liangwei, E-mail: liazho@ucas.ac.cn. New insights into the posttranslational regulation of human cytosolic thioredoxin by S-palmitoylation. United States: N. p., 2015. Web. doi:10.1016/J.BBRC.2015.03.132.
Xu, Zhiyu, & Zhong, Liangwei, E-mail: liazho@ucas.ac.cn. New insights into the posttranslational regulation of human cytosolic thioredoxin by S-palmitoylation. United States. doi:10.1016/J.BBRC.2015.03.132.
Xu, Zhiyu, and Zhong, Liangwei, E-mail: liazho@ucas.ac.cn. Fri . "New insights into the posttranslational regulation of human cytosolic thioredoxin by S-palmitoylation". United States. doi:10.1016/J.BBRC.2015.03.132.
@article{osti_22462048,
title = {New insights into the posttranslational regulation of human cytosolic thioredoxin by S-palmitoylation},
author = {Xu, Zhiyu and Zhong, Liangwei, E-mail: liazho@ucas.ac.cn},
abstractNote = {High level of palmitate is associated with metabolic disorders. We recently showed that enhanced level of S-palmitoylated cytosolic thioredoxin (Trx1) in mouse liver was new characteristic feature of insulin resistance. However, our understanding of the effect of S-palmitoylation on Trx1 is limited, and the tissue specificity of Trx1 S-palmitoylation is unclear. Here we show that S-palmitoylation also occurs at Cys73 of Trx1 in living endothelial cells, and the level of S-palmitoylated Trx1 undergoes regulation by insulin signaling. Trx1 prefers thiol-thioester exchange with palmitoyl-CoA to acetyl-CoA. S-palmitoylation alters conformation or secondary structure of Trx1, as well as decreases the ability of Trx1 to transfer electrons from thioredoxin reductase to S-nitrosylated protein–tyrosine phosphatase 1B and S-nitroso-glutathione. Our results demonstrate that S-palmitoylation is an important post-translational modification of human Trx1. - Highlights: • S-palmitoylation occurs at Cys73 of Trx1 in living endothelial cells. • Insulin signaling may regulate level of S-palmitoylated Trx1 in the cells. • S-palmitoylation plays significant effects on Trx1 structure and functions.},
doi = {10.1016/J.BBRC.2015.03.132},
journal = {Biochemical and Biophysical Research Communications},
issn = {0006-291X},
number = 4,
volume = 460,
place = {United States},
year = {2015},
month = {5}
}