Please use this identifier to cite or link to this item: https://doi.org/10.1038/srep25844
Title: Phosphoprotein network analysis of white adipose tissues unveils deregulated pathways in response to high-fat diet
Authors: Asfa, A.S
Qiu, B
Wee, S
Choi, H 
Gunaratne, J 
Tergaonkar, V 
Keywords: acetate coenzyme A ligase
ACSS2 protein, mouse
peptide
phosphoprotein
triacylglycerol
3T3-L1 cell line
animal
chemically induced
chemistry
drug effects
gene expression regulation
gene regulatory network
genetics
lipid diet
metabolism
mouse
mutation
obesity
procedures
protein protein interaction
proteomics
signal transduction
white adipose tissue
3T3-L1 Cells
Acetate-CoA Ligase
Adipose Tissue, White
Animals
Diet, High-Fat
Gene Expression Regulation
Gene Regulatory Networks
Mice
Mutation
Obesity
Peptides
Phosphoproteins
Protein Interaction Maps
Proteomics
Signal Transduction
Triglycerides
Issue Date: 2016
Publisher: Nature Publishing Group
Citation: Asfa, A.S, Qiu, B, Wee, S, Choi, H, Gunaratne, J, Tergaonkar, V (2016). Phosphoprotein network analysis of white adipose tissues unveils deregulated pathways in response to high-fat diet. Scientific Reports 6 : 25844. ScholarBank@NUS Repository. https://doi.org/10.1038/srep25844
Abstract: Despite efforts in the last decade, signaling aberrations associated with obesity remain poorly understood. To dissect molecular mechanisms that define this complex metabolic disorder, we carried out global phosphoproteomic analysis of white adipose tissue (WAT) from mice fed on low-fat diet (LFD) and high-fat diet (HFD). We quantified phosphorylation levels on 7696 peptides, and found significant differential phosphorylation levels in 282 phosphosites from 191 proteins, including various insulin-responsive proteins and metabolic enzymes involved in lipid homeostasis in response to high-fat feeding. Kinase-substrate prediction and integrated network analysis of the altered phosphoproteins revealed underlying signaling modulations during HFD-induced obesity, and suggested deregulation of lipogenic and lipolytic pathways. Mutation of the differentially-regulated novel phosphosite on cytoplasmic acetyl-coA forming enzyme ACSS2 (S263A) upon HFD-induced obesity led to accumulation of serum triglycerides and reduced insulin-responsive AKT phosphorylation as compared to wild type ACSS2, thus highlighting its role in obesity. Altogether, our study presents a comprehensive map of adipose tissue phosphoproteome in obesity and reveals many previously unknown candidate phosphorylation sites for future functional investigation.
Source Title: Scientific Reports
URI: https://scholarbank.nus.edu.sg/handle/10635/174966
ISSN: 2045-2322
DOI: 10.1038/srep25844
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