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HSP70-driven molecular response to the proteasome machinery inhibition is a vulnerability in cancer

ABSTRACT: Cell lines indicated in the file names were either treated with carfilzomib (C) at concentrations near the IC50 of proteasome activity in each cell line for 24h, or with DMSO (D) as a control, in biological duplicates.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture, Embryonic Stem Cell

SUBMITTER: Jacek Wisniewski

LAB HEAD: Jacek R Wisniewski

PROVIDER: PXD025364 | Pride | 2025-10-29

REPOSITORIES: Pride

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			Action	DRS
	20180411_QX8_JRW_SA_L_KK54.raw	Raw
	20180411_QX8_JRW_SA_L_KK55.raw	Raw
	20180411_QX8_JRW_SA_L_KK56.raw	Raw
	20180411_QX8_JRW_SA_L_KK57.raw	Raw
	20180411_QX8_JRW_SA_L_KK58.raw	Raw

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HSP70-driven molecular response to the proteasome machinery inhibition is a vulnerability in cancer

Project description:Two human primary fibroblast cell lines indicated in the file names were either treated with carfilzomib (C) at the concentrations near the IC50 of proteasome activity (10nM) for 24h, or with DMSO (D) as a control, in biological duplicates (numbers 1-2).

2025-10-29 | PXD027840 | Pride

HSP70-driven molecular response to the proteasome machinery inhibition is a vulnerability in cancer

Project description:In this study we employed a label-free global proteomics approach, with a sensitivity of over 10k quantified proteins per sample, to determine contributions of different compensatory mechanisms upon the proteasome inhibition with carfilzomib - in cells of multiple myeloma, normal fibroblasts and cancers of lung, colon and pancreas. We identified several responding pathways, while the main HSP70 family stress inducible molecular chaperones HSPA1A and HSPA1B (often addressed jointly as HSPA1A/B or simply “Hsp70”, due to nearly identical protein sequences) were the most universal proteasome inhibition responders in proteomes of all the studied cell types. Further overlap of differential proteomics with RNA-seq analysis obtained at the same condions (DMSO control vs carfilzomib treatment) and a subsequent validation showed that the proteasome inhibition-dependent induction of HSPA1A/B and other chaperone proteins in cancer cells is in fact transcription-driven.

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Mutant p53, mutant KRAS and hyperactive CMYC downstream proteomic programs in lung, colon and pancreatic cancer cell lines

Project description:Human cancer cell lines indicated in the file names, with stably overexpressed Cas9 nuclease, were transfected with (C) control sgRNA or (P) TP53-specific sgRNA, (K) KRAS-specific sgRNA or (M) CMYC-specific sgRNA. Each experiment was done by transfection of sgRNA pair - control (C) or causing a NHEJ-mediated knock-out of the target genes (P, K or M). Samples for proteomics were collected 48h post sgRNA transfection without selection, in three biological replicates each (indicated with numbers 1-3). In cell lines with three activated oncogenes, three separate oncogene-targeting transfections were carried out.

2024-10-17 | PXD037398 | Pride

Multi-omics analysis of BCG macrophage activation

Project description:THP-1-derived macrophages were infected with M. bovis BCG. Separately, proteomic analysis was performed on histones (file names containing IKP) and the total proteome (file names containing JMI).

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Fyn- and Abl-driven interactome and post-translational modifications of DCBLD1 and DCBLD2

Project description:Three related datasets are included, all from immunoprecipitations of FLAG-tagged DCBLD1 and DCBLD2 (human) from 293 cells. Letters at the end of file names denote regions of each gel lave from highest (“A”) to lowest (“B”-X) molecular weight. File names containing “SILAC” are part of a dataset composed of 3 biological replicates (“T1”,”T2”,”T3” in file name) run of 10% or 15% gels (“10” or “15” in file name). DCBLD1 or DCBLD2 were immunoprecipitated from cells alone (light SILAC condition) or with Fyn/Abl (heavy SILAC condition). “Mock”, “Fyn” alone, or “Abl” alone in file names denote control immunoprecipitates, in which the light condition was a mock transfection and the heavy was either a mock or had Fyn/Abl expressed alone. Trypsin was used as the proteolytic enzyme. File names beginning with “Label_free” are part of datasets from LC-MS/MS analysis of DCBLD1 or DCBLD2 immunoprecipitates from 293 lysates. Prior to LC-MS/MS analysis, immunoprecipitates were digested with trypsin and GluC. Only DCBLD1 and DCBLD2 protein bands were analyzed via LC-MS/MS. File names containing “zebrafish” are part of datasets from LC-MS/MS analysis of DCBLD2 immunoprecipitates from 293 extracts that were then incubated with zebrafish extracts. These datasets include tryptic peptides from both human and zebrafish proteins.

2020-08-07 | PXD017723 | Pride

Proteomics data of Escherichia phage vB_EcoS-EE09 isolated from wastewater treatment plant effluent and its infected and non-infected host E. coli DSM613

Project description:This dataset was created to (i) compare the protein expression of E. coli DSM613 cells infected and uninfected with phage vB_EcoS-EE09 and (ii) detect structural proteins of phage vB_EcoS-EE09. Thus, this set provides proteomic data of three setups: 1. Uninfected E. coli DSM613 (file names [file ID]: 04_22A [F40]; 13_ecolicontrol_01 [F13]; 14_ecolicontrol_02 [F14]) 2. E. coli DSM613 infected with phage vB_EcoS-EE09 (file names [file ID]: 02_13A [F39]; 27_ecoliinfected_01 [F27]; 28_ecoliinfected_02 [F28]) 3. Cell-free phage lysate of phage vB_EcoS-EE09 (sample name: 01_EE09)

2023-11-13 | PXD046455 | Pride

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Sequences that influence mRNA trans splicing and polyadenylation in trypanosoma brucei.

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2022-04-29 | E-MTAB-11628 | biostudies-arrayexpress

Proteomic Response of Cupriavidus metallidurans CH34 to gold stress

Project description:Proteomic response of Cupriavidus metallidurans CH34 to gold stress as in comparison to copper stress and control. Please note that 25Au in gel file names is a typo and should read 50Au.

2016-10-26 | PXD005034 | Pride

A simple method for developing lysine targeted covalent protein reagents

Project description:In this project we developed phosphopeptides functionalized with methacrylate ester warheads installed on a cysteine residue, which bind covalently to the protein 14-3-3 sigma. We prepared complexes of the purified protein with the peptides and used trypsin digestion and LC-MSMS to elucidate the binding site of the peptides, by comparison of compound-treated complexes to DMSO-treated protein and observing the disappearance on non-modified peptides. The file names are based on internal names used for the project and are distinct from the names given to the peptides in the final publication. Names are as follows: 4IEA - peptide 3 in the final publication 128C - peptide 8 in the final publication 132C - peptide 11 in the final publication

2024-01-26 | PXD044257 | Pride

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