Dataset Information

Phosphoproteomics of Human ACHN cells by estrogen

ABSTRACT: To find out the potential targets in response to estrogen treatment on ACHN cell, a human renal cell carcinoma (RCC) cell line. Since estrogen can repress ACHN growth in a partly estrogen receptor-dependent manner, it is possible that phosphorylation state in ACHN cells is regulated.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell, Cell Culture

DISEASE(S): Renal Cell Carcinoma

SUBMITTER: Wei-Chi Ku

LAB HEAD: Wei-Chi Ku

PROVIDER: PXD001962 | Pride | 2016-04-26

REPOSITORIES: Pride

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Publications

Dual Roles of 17-β Estradiol in Estrogen Receptor-dependent Growth Inhibition in Renal Cell Carcinoma.

Chen Kuo-Chiang KC Lin Chih-Ming CM Huang Chi-Jung CJ Chen Shao-Kuan SK Wu Sheng-Tang ST Chiang Han-Sun HS Ku Wei-Chi WC

Cancer genomics & proteomics 20160501 3

<h4>Background</h4>It has been proposed that 17-β-estradiol (E2) activates estrogen receptor and inhibits renal cell carcinoma (RCC) growth. In the present study we explored the role of E2 and ER in the regulation of RCC growth.<h4>Materials and methods</h4>The RCC cell line ACHN was treated by E2 combining with E2 antagonist Fulvestrant or ER knockdown, and cell growth was monitored. Quantitative phosphoproteomics was applied to study the E2 regulated non-genomic phosphorylation changes. Wester ...[more]

PMID: 27107064

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Project description:Protein phosphorylation regulated by plant hormone is involved in the coordination of fundamental plant development. Brassinosteroids (BRs), a group of phytohormones, regulated phosphorylation dynamics remains to be delineated in plants. In this study, we performed a mass spectrometry (MS)-based phosphoproteomics to conduct a global and dynamic phosphoproteome profiling across five time points of BR treatment in the period between 5 minutes and 12 hours. MS coupling with phosphopeptide enrichment techniques has become the powerful tool for profiling protein phosphorylation. However, MS-based methods tend to have data consistency and coverage issues. To address these issues, bioinformatics approaches were used to complement the non-detected proteins and recover the dynamics of phosphorylation events. A total of 1,104 unique phosphorylated peptides from 739 unique phosphoproteins were identified. The time-dependent gene ontology (GO) analysis shows the transition of biological processes from signaling transduction to morphogenesis and stress response. The protein-protein interaction analysis found most of identified phosphoproteins have strongly connections with known BR signaling components. The analysis by using Motif-X was performed to identify 15 enriched motifs, 11 of which correspond to 6 known kinase families. To uncover the dynamic activities of kinases, the enriched motifs were combined with phosphorylation profiles and revealed that the substrates of casein kinase 2 and mitogen-activated protein kinase were significantly phosphorylated and dephosphorylated at initial time of BR treatment, respectively. The time-dependent kinase-substrate interaction networks were constructed and showed many substrates are the downstream of other signalings, such as auxin and ABA signalings. Comparing BR responsive phosphoproteome and gene expression data, we found most of phosphorylation changes were not led by gene expression changes. Our results suggested BR signaling not only induces gene expression, but also change protein activation by phosphorylation via various kinases. Through a large-scale dynamic profile of phosphoproteome coupling bioinformatics, a complicated kinase-centered network related to BR-regulated growth was deciphered. The phosphoproteins and phosphosites identified from our study provide a useful dataset for revealing signaling networks of BR regulation, and also expanded our knowledge of protein phosphorylation modification in plants as well as further deal to solve the plant growth problems.

Dataset Information

Phosphoproteomics of Human ACHN cells by estrogen

Publications

Dual Roles of 17-β Estradiol in Estrogen Receptor-dependent Growth Inhibition in Renal Cell Carcinoma.

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