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SILAC quantification of proteins in the control and UFBP1-expressing MGC803 cells

ABSTRACT: In this project, we used SILAC quantitative proteomics to identify proteins that are differentially regulated by UFM1-binding and PCI domain-containing protein 1 (UFBP1, also called DDRGK domain-containing protein 1 or DDRGK1) in a gastric cancer cell line. The aim of this study is to discover the proteins that are responsible for the biological function of UFBP1.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Stomach, Gastric Cancer Cell Line

DISEASE(S): Stomach Carcinoma

SUBMITTER: Dan Li

LAB HEAD: Guoqiang Xu

PROVIDER: PXD013590 | Pride | 2021-02-15

REPOSITORIES: Pride

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			Action	DRS
	SILACBiologicalreplicate1-Fraction1.raw	Raw
	SILACBiologicalreplicate1-Fraction10.raw	Raw
	SILACBiologicalreplicate1-Fraction11.raw	Raw
	SILACBiologicalreplicate1-Fraction12.raw	Raw
	SILACBiologicalreplicate1-Fraction13.raw	Raw

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Publications

UFBP1, a key component in ufmylation, enhances drug sensitivity by promoting proteasomal degradation of oxidative stress-response transcription factor Nrf2.

Hu Zhanhong Z Wang Xiaohui X Li Dan D Cao Lindong L Cui Hongxia H Xu Guoqiang G

Oncogene 20201120 3

The key component in the UFM1 conjugation system, UFM1-binding and PCI domain-containing protein 1 (UFBP1), regulates many biological processes. Recently it has been shown that low UFBP1 protein level is associated with the worse outcome of gastric cancer patients. However, how it responses to the sensitivity of gastric cancer to chemotherapy drugs and the underlying molecular mechanism remain elusive. Here, we discovered that high UFBP1 expression increases the progression-free survival of adva ...[more]

PMID: 33219317

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Transcriptomic and proteomic profiling of KEAP1 disrupted and sulforaphane treated human breast epithelial cells

Project description:Sulforaphane (SFN), an isothiocyanate found in cruciferous vegetables, is a potent inhibitor of experimental mammary carcinogenesis and may be an effective, safe chemopreventive agent for use in humans. SFN acts in part on the Keap1/Nrf2 pathway to regulate a battery of cytoprotective genes. In this study transcriptomic and proteomic changes in the estrogen receptor negative, non tumorigenic human breast epithelial MCF10A cell line were analyzed following SFN treatment or KEAP1 knockdown with siRNA using microarray and stable isotopic labeling with amino acids in culture (SILAC), respectively. Changes in selected transcripts and proteins were confirmed by PCR and Western blot in MCF10A and MCF12A cells. There was strong correlation between the transcriptomic and proteomic responses in both the SFN treatment (R=0.679, P<0.05) and KEAP1 knockdown (R=0.853, P<0.05) experiments. Common pathways for SFN treatment and KEAP1 knockdown were xenobiotic metabolism and antioxidants, glutathione metabolism, carbohydrate metabolism and NADH/NADPH regeneration. Moreover, these pathways were most prominent in both the transcriptomic and proteomic analyses. The aldo-keto reductase family members, AKR1B10, AKR1C1, AKR1C2 and AKR1C3, as well as NQO1 and ALDH3A1, were highly upregulated at both the transcriptomic and proteomic level. Collectively, these studies served to identify potential biomarkers that can be used in clinical trials to investigate the initial pharmacodynamic action of SFN in the breast. MCF10A cells were treated with SFN or had KEAP1 knocked down by siRNA.

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Project description:The Z-disc is a protein-rich structure critically important for myofibril development and integrity. Since a role of the Z-disc for signal integration and transduction was recently suggested, its precise phosphorylation landscape warranted in-depth analysis. We therefore established a site-resolved protein phosphorylation map of the Z-disc in skeletal myocytes and found that it is a phosphorylation hotspot in living cells, underscoring its functions in signalling and disease-related processes. In an exemplary fashion, we analysed the actin-binding multi-adaptor protein filamin C (FLNc), which is essential for Z-disc assembly and maintenance, and found that PKC phosphorylation at distinct serine residues in its hinge 2 region prevents its cleavage at an adjacent tyrosine residue by calpain 1. With this quantitative in vivo kinase assay, we show that the phosphorylation site S2625 in mouse FLNc is significantly down-regulated upon treatment of C2C12 myotubes with the PKCα inhibitor Gö6976.

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Saccharomyces cerevisiae mutant strain with R1158 strain background: Fold change after doxycycline treatment

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Identification of immunoglobulin switch (S) region binding proteins by insertional ChIP (iChIP)

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