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Title: Bile Acid Signal-induced Phosphorylation of Small Heterodimer Partner by Protein Kinase C;#950; Is Critical for Epigenomic Regulation of Liver Metabolic Genes

Authors:
; ; ; ; ; ; ; ;  [1];  [2];  [2]
  1. (UIUC)
  2. (
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
National Institutes of Health (NIH)
OSTI Identifier:
1123974
Resource Type:
Journal Article
Resource Relation:
Journal Name: J. Biol. Chem.; Journal Volume: 288; Journal Issue: (32) ; 08, 2013
Country of Publication:
United States
Language:
ENGLISH

Citation Formats

Seok, Sunmi, Kanamaluru, Deepthi, Xiao, Zhen, Ryerson, Daniel, Choi, Sung-E, Suino-Powell, Kelly, Xu, H. Eric, Veenstra, Timothy D., Kemper, Jongsook Kim, Van Andel), and SAIC). Bile Acid Signal-induced Phosphorylation of Small Heterodimer Partner by Protein Kinase C;#950; Is Critical for Epigenomic Regulation of Liver Metabolic Genes. United States: N. p., 2014. Web. doi:10.1074/jbc.M113.452037.
Seok, Sunmi, Kanamaluru, Deepthi, Xiao, Zhen, Ryerson, Daniel, Choi, Sung-E, Suino-Powell, Kelly, Xu, H. Eric, Veenstra, Timothy D., Kemper, Jongsook Kim, Van Andel), & SAIC). Bile Acid Signal-induced Phosphorylation of Small Heterodimer Partner by Protein Kinase C;#950; Is Critical for Epigenomic Regulation of Liver Metabolic Genes. United States. doi:10.1074/jbc.M113.452037.
Seok, Sunmi, Kanamaluru, Deepthi, Xiao, Zhen, Ryerson, Daniel, Choi, Sung-E, Suino-Powell, Kelly, Xu, H. Eric, Veenstra, Timothy D., Kemper, Jongsook Kim, Van Andel), and SAIC). Wed . "Bile Acid Signal-induced Phosphorylation of Small Heterodimer Partner by Protein Kinase C;#950; Is Critical for Epigenomic Regulation of Liver Metabolic Genes". United States. doi:10.1074/jbc.M113.452037.
@article{osti_1123974,
title = {Bile Acid Signal-induced Phosphorylation of Small Heterodimer Partner by Protein Kinase C;#950; Is Critical for Epigenomic Regulation of Liver Metabolic Genes},
author = {Seok, Sunmi and Kanamaluru, Deepthi and Xiao, Zhen and Ryerson, Daniel and Choi, Sung-E and Suino-Powell, Kelly and Xu, H. Eric and Veenstra, Timothy D. and Kemper, Jongsook Kim and Van Andel) and SAIC)},
abstractNote = {},
doi = {10.1074/jbc.M113.452037},
journal = {J. Biol. Chem.},
number = (32) ; 08, 2013,
volume = 288,
place = {United States},
year = {Wed Mar 19 00:00:00 EDT 2014},
month = {Wed Mar 19 00:00:00 EDT 2014}
}
  • Calcium/calmodulin-dependent protein kinase (CCaMK) has been shown to play an important role in abscisic acid (ABA)-induced antioxidant defense and enhance the tolerance of plants to drought stress. However, its downstream molecular events are poorly understood. Here, we identify a NAC transcription factor, ZmNAC84, in maize, which physically interacts with ZmCCaMK in vitro and in vivo. ZmNAC84 display a partially overlapping expression pattern with ZmCCaMK after ABA treatment and H 2O 2 is required for ABA-induced ZmNAC84 expression. Functional analysis reveals that ZmNAC84 is essential for ABA-induced antioxidant defense in a ZmCCaMK-dependent manner. Furthermore, ZmCCaMK directly phosphorylates S113 of ZmNAC84 inmore » vitro, and S113 is essential for the ABA-induced stimulation of antioxidant defense by ZmCCaMK. Moreover, overexpression of ZmNAC84 in tobacco can improve drought tolerance, and alleviate drought-induced oxidative damage of transgenic plants. These results define a mechanism for ZmCCaMK function in ABA-induced antioxidant defense, where ABA-produced H 2O 2 first induces expression of ZmCCaMK and ZmNAC84 and activates ZmCCaMK, and subsequently the activated ZmCCaMK phosphorylates ZmNAC84 at S113, thereby inducing antioxidant defense by activating downstream genes.« less
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