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Updated: May 28, 2026

Phosphoproteomic Strategy for Profiling Osmotic Stress Signaling in Arabidopsis
Published on: June 25, 2020
Identification of novel signaling components in genistein-regulated signaling pathways by quantitative
Guang-Rong Yan1, Xing-Feng Yin, Chuan-Le Xiao
1Institute of Life and Health Engineering, and National Engineering and Research Center for Genetic Medicine, Jinan University, Guangzhou 510632, China. tgryan@jnu.edu.cn
Abstract:
Isolated from soybeans, genistein is an isoflavonoid that exhibits anti-carcinogenic effects. Genistein could induce G2/M arrest and apoptosis of various cancer cells in vivo and in vitro. Although ERK1/2, AKT, p90RSK and NFκB were previously found to be regulated by genistein, most of signaling components in genistein-inhibited signaling pathways were still unknown. Here, we used SILAC quantitative phosphoproteomics to globally identify the phosphoproteins and their regulatory sites in signaling pathways mediated by genistein. We detected 1177 phosphorylation sites on 635 unique proteins; among them, 320 phosphorylation sites on 222 unique phosphopeptides representing 215 non-redundant proteins were modulated at least 1.5-folds by genistein. Apart from ERK1/2, PI3K, p90RSK, Bad and topoisomerase that are known genistein-regulated effectors, many novel phosphoproteins were identified for the first time to be involved in genistein-regulated signal transduction networks. They mainly include 9 receptors, 5 signal adaptors, 13 protein kinases, 2 protein phosphatase regulatory subunits, and 14 transcription regulators. Several of these phosphoproteins have been proven to be involved in G2/M arrest or apoptosis such as GPCRs, DCC, NCK1, TNK2, BTK, TP53BP1, BCLAF, MAX and MAG. This dataset provides valuable insights into the cancer-related phosphorylation signaling pathways regulated by genistein.
Insights
Genistein, a soy isoflavonoid, shows anti-cancer effects by inducing cell cycle arrest and apoptosis. This study identifies novel phosphoproteins involved in genistein
Area of Science:
- Molecular Biology
- Cancer Research
- Biochemistry
Background:
- Genistein, an isoflavonoid from soybeans, demonstrates anti-carcinogenic properties.
- It is known to induce G2/M arrest and apoptosis in cancer cells.
- While some signaling pathways (ERK1/2, AKT, p90RSK, NFκB) are known to be affected by genistein, most components remain unidentified.
Purpose of the Study:
- To globally identify phosphoproteins and their regulatory sites in genistein-mediated signaling pathways.
- To uncover novel signaling components involved in genistein's anti-cancer mechanisms.
Main Methods:
- Utilized SILAC (Stable Isotope Labeling by Amino acids in Cell culture) quantitative phosphoproteomics.
- Analyzed global phosphoprotein profiles to identify genistein-modulated sites.
Main Results:
- Identified 1177 phosphorylation sites on 635 unique proteins.
- Detected 320 phosphorylation sites (on 215 proteins) modulated by at least 1.5-fold by genistein.
- Discovered novel phosphoproteins, including receptors, adaptors, kinases, phosphatase regulators, and transcription regulators, involved in genistein signaling.
Conclusions:
- This study provides a comprehensive dataset of genistein-regulated phosphoproteins.
- Identified novel signaling molecules, such as GPCRs, DCC, NCK1, and TP53BP1, implicated in G2/M arrest and apoptosis.
- Offers valuable insights into the molecular mechanisms underlying genistein's anti-cancer effects.
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