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Proximity biotinylation of NCI-H226 cells by EGFR-FabID

ABSTRACT: NCI-H226 cells were pretreated with DMSO or gefitinib and unstimulated or stimulated with EGF. Then AGIA-FabID or EGFR-FabID were added to the cells in three biological replicates. Cell lysates were subjected to methanol-chloroform precipitation and digested with trypsin. Biotinylated peptides were purified by Tamavidin 2-REV and identified by LC-MS/MS analysis.

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Hidetaka Kosako

PROVIDER: PXD039451 | JPOST Repository | Tue Nov 14 00:00:00 GMT 2023

REPOSITORIES: jPOST

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			Action	DRS
	169_Yamada_1_AGIAiD_DMSO_Tama_FusionIT.raw	Raw
	171_Yamada_3_AGIAiD_DMSO_EGF_Tama_FusionIT.raw	Raw
	173_Yamada_5_AGIAiD_Gefitinib_EGF_Tama_FusionIT.raw	Raw
	175_Yamada_7_EGFR_FabID_DMSO_Tama_FusionIT.raw	Raw
	177_Yamada_9_EGFR_FabID_DMSO_EGF_Tama_FusionIT.raw	Raw

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Publications

Proximity extracellular protein-protein interaction analysis of EGFR using AirID-conjugated fragment of antigen binding.

Yamada Kohdai K Shioya Ryouhei R Nishino Kohei K Furihata Hirotake H Hijikata Atsushi A Kaneko Mika K MK Kato Yukinari Y Shirai Tsuyoshi T Kosako Hidetaka H Sawasaki Tatsuya T

Nature communications 20231214 1

Receptor proteins, such as epidermal growth factor receptor (EGFR), interact with other proteins in the extracellular region of the cell membrane to drive intracellular signalling. Therefore, analysis of extracellular protein-protein interactions (exPPIs) is important for understanding the biological function of receptor proteins. Here, we present an approach using a proximity biotinylation enzyme (AirID) fusion fragment of antigen binding (FabID) to analyse the proximity exPPIs of EGFR. AirID w ...[more]

PMID: 38097606

Similar Datasets

Proximity biotinylation of A431 cells by EGFR-FabID

Project description:A431 cells were pretreated with DMSO or gefitinib and unstimulated or stimulated with EGF. Then AGIA-FabID or EGFR-FabID were added to the cells in three biological replicates. Cell lysates were subjected to methanol-chloroform precipitation and digested with trypsin. Biotinylated peptides were purified by Tamavidin 2-REV and identified by LC-MS/MS analysis.

2023-11-14 | PXD039450 | JPOST Repository

Proximity biotinylation of A431 cells with gefitinib alone treatment by EGFR-FabID

Project description:A431cells were pretreated with DMSO or gefitinib. Then AGIA-FabID or EGFR-FabID were added to the cells in three biological replicates. Cell lysates were subjected to methanol-chloroform precipitation and digested with trypsin. Biotinylated peptides were purified by Tamavidin 2-REV and identified by LC-MS/MS analysis.

2023-11-14 | PXD043526 | JPOST Repository

Proximity biotinylation of NCI-H226 cells with gefitinib alone treatment by EGFR-FabID

Project description:NCI-H226 cells were pretreated with DMSO or gefitinib. Then AGIA-FabID or EGFR-FabID were added to the cells in three biological replicates. Cell lysates were subjected to methanol-chloroform precipitation and digested with trypsin. Biotinylated peptides were purified by Tamavidin 2-REV and identified by LC-MS/MS analysis.

2023-11-14 | PXD043527 | JPOST Repository

Proximity biotinylation of Expi293F cells overexpressing EGFR by EGFR-FabID

Project description:Expi293F cells were transfected with pcDNA3.1-EGFR and treated with AGIA-FabID or EGFR-FabID in three biological replicates. Cell lysates were subjected to methanol-chloroform precipitation and digested with trypsin. Biotinylated peptides were purified by Tamavidin 2-REV and identified by LC-MS/MS analysis.

2023-11-14 | PXD039449 | JPOST Repository

Proximity biotinylation of Expi293F cells stably expressing EGFR by EGFR-FabID

Project description:Expi293F cells stably expressing EGFR were treated with AGIA-FabID or EGFR-FabID in three biological replicates. Cell lysates were subjected to methanol-chloroform precipitation and digested with trypsin. Biotinylated peptides were purified by Tamavidin 2-REV and identified by LC-MS/MS analysis.

2023-11-14 | PXD043525 | JPOST Repository

Transcription profiling of Human Endometrial Cancer Cells treated with EGF or gefitinib to investigate gene regulation of EGFR Isoforms.

Project description:Microarrays were used to analyze differential gene expression and to help determine the efficacy of Iressa (gefitinib), a tyrosine kinase inhibitor, on endometrial cancer cells. Type I Ishikawa H and type II Hec50co endometrial carcinoma cells both express EGFR and sEGFR, but differ markedly in their responsiveness to the EGFR inhibitor gefitinib. This difference is paralleled by differences in the expression of sEGFR and EGFR, as well as in their transcriptional response following treatment with either EGFor gefitinib. The small cluster of differently regulated genes reported here in these type I vs. type II endometrial cancer-derived cell lines may identify candidate biomarkers useful for predicting sensitivity to EGFR blockade. Type I (Ishikawa H cells) and type II (Hec50co) derived endometrial carcinomas, were dosed with either EGF(epidermal growth factor) or Iressa (gefitinib) for 12 or 24 hours and gene expression was examined.

2010-03-23 | E-GEOD-20854 | biostudies-arrayexpress

Time-course gene expression profiles of gefitinib-sensitive or -resistant lung adenocarcinoma cells stimulated with EGF, in the presence or absence of gefitinib, EGF receptor tyrosine kinase-specific inhibitor

Project description:Gefitinib, an epidermal growth factor receptor (EGFR) tyrosine kinase inhibitor (TKI), induces substantial clinical responses for non-small cell lung cancer (NSCLC) cells harboring EGFR activating mutations, but most of them invariably develop resistance. By generating a gefitinib resistance (PC9GR) from a human NSCLC-derived drug sensitive cell line (PC9), we studied differences of transcription dynamics between them by the aid of a computational decoupling of hidden regulatory signals from time course gene expression profiles. Given a collection of transcription factors (TFs) and their regulatory targets, the method captured temporally-synchronized shifts in evolving expression of target genes sharing each TF regulatory unit, and drew underlying regulatory signals. The analysis identified sterol regulatory element binding protein 1 (SREBP-1) as a key regulatory agent that facilitates the maintenance of drug tolerance, involving transcription controls of a G1-specific cyclin dependent kinase inhibitor whose expression was specifically elevated in PC9, but in turn, reduced in PC9GR Gefitinib-resistance cell line (PC9GR) was established derived from lung adenocarcinoma cell line PC9. PC9 cells and PC9GR cells were treated with the four different conditions, control (No treatment), EGF-treatment, gefitinib-treatment, and both gefitinib and EGF-treatment. In each condition, the gene expression was measured at 26 time points during 24 hrs.

2014-01-01 | E-GEOD-34228 | biostudies-arrayexpress

Human colon cancer cell lines: NT(untreated) vs EGF, Cetuximab and Gefitinib treatments

Project description:Gene Expression Profiling of HT-29 and Caco-2 colon cancer cell lines untreated compared with EGF, Cetuximab, Gefitinib,EGF plus Cetuximab and EGF plus gefitinib treatments. Keywords: Gene Expression Profiling

2007-09-12 | GSE8967 | GEO

Phosphoproteomics of TrkA and TrkB signaling in SH-SY5Y neuroblastoma cells

Project description:Human neuroblastoma cells (SH-SY5Y) were engineered to have stable expression of either TrkA (NTRK1) or TrkB (NTRK2) receptors. The cells were pretreated with 0.5 μM Trametinib, 2.5 μM Gefitinib, and combination of 0.25 μM Trametinib and 1.25 μM Gefitinib. Stimulation of TrkA and TrkB-expressing SH-SY5Y cells was carried out 30 minutes following inhibitor addition, using 100 ng/mL of recombinant NGF (#450-01) and BDNF (#450-02), respectively (both from Peprotech). The stimulated and unstimulated controls are included.

2022-04-13 | PXD028943 | Pride

DNA Modifications Enabling Proximity Biotinylation.

Project description:Advances in peroxidase and biotin ligase-mediated signal amplification have enabled high-resolution subcellular mapping of endogenous RNA localization and protein-protein interactions. Application of these technologies has been limited to RNA and proteins because of the reactive groups required for biotinylation in each context. Here we report several novel methods for proximity biotinylation of exogenous oligodeoxyribonucleotides by application of well-established and convenient enzymatic tools. We describe approaches using simple and efficient conjugation chemistries to modify deoxyribonucleotides with "antennae" that react with phenoxy radicals or biotinoyl-5'-adenylate. In addition, we report chemical details of a previously undescribed adduct between tryptophan and a phenoxy radical group. These developments have potential application in the selection of exogenous nucleic acids capable of unaided entry into living cells.

| S-EPMC10119920 | biostudies-literature

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