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LC-MSMS analysis of immunoprecipitated JunB-FLAG from HAP1 ADO KO cells

ABSTRACT: Define the N-terminal acetylation status of human JunB in siCTRL, siNAA10 or siNAA20 treated HAP1 ADO KO cells.

INSTRUMENT(S): Orbitrap Eclipse

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Malin Lundekvam

LAB HEAD: Thomas Arnesen

PROVIDER: PXD045695 | Pride | 2024-07-03

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	1A_siCtrl_1.mzML	Mzml
	1A_siCtrl_1.mzid.gz	Mzid
	1A_siCtrl_1.raw	Raw
	1B_siCtrl_2.mzML	Mzml
	1B_siCtrl_2.mzid.gz	Mzid

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1 - 5 of 18

Publications

N-terminal cysteine acetylation and oxidation patterns may define protein stability.

Heathcote Karen C KC Keeley Thomas P TP Myllykoski Matti M Lundekvam Malin M McTiernan Nina N Akter Salma S Masson Norma N Ratcliffe Peter J PJ Arnesen Thomas T Flashman Emily E

Nature communications 20240625 1

Oxygen homeostasis is maintained in plants and animals by O2-sensing enzymes initiating adaptive responses to low O2 (hypoxia). Recently, the O2-sensitive enzyme ADO was shown to initiate degradation of target proteins RGS4/5 and IL32 via the Cysteine/Arginine N-degron pathway. ADO functions by catalysing oxidation of N-terminal cysteine residues, but despite multiple proteins in the human proteome having an N-terminal cysteine, other endogenous ADO substrates ha ...[more]

PMID: 38918375

Similar Datasets

N-terminal acetyaltion of Human JunB in yeast expressing all N-terminal acetyltransferases, no NatA enzyme or no NatB enzyne

Project description:Define the N-terminal status of overexpressed human JUNB in WT yeast strain, NAA10 Δ strain and NAA20 Δ strain.

2024-07-03 | PXD047612 | Pride

MicroRNA-15/16 Antagonizes c-Myb to Control Natural Killer Cell Maturation (c-Myb overexpression)

Project description:NK cells develop in the bone marrow and complete their maturation in peripheral organs, but the molecular events controlling maturation are incompletely understood. Utilizing an NK cell-specific miR-15/16 deficient genetic model (15aKO), we identified a critical role for miR-15/16 family microRNAs in the normal maturation of NK cells in vivo, with a specific reduction in mature CD11b+CD27- NK cells in multiple tissues. The mechanism responsible was a block in differentiation, since accelerated NK cell death was not evident, and earlier intermediates of NK cell maturation were expanded. Further, we identified Myb as a direct target of miR-15/16 in NK cells, with Myb expression increased in immature 15aKO NK cells. Following adoptive transfer, immature 15aKO NK cells exhibited defective maturation, which was rescued by ectopic miR-15/16 expression or Myb knockdown. Moreover, Myb overexpression resulted in defective NK cell maturation. Thus, miR-15/16 regulation of Myb controls the normal NK cell maturation program. KY-1 and KY-2 cell lines overexpressing c-Myb

2015-09-03 | E-GEOD-58268 | biostudies-arrayexpress

DPPA3-HIF1a axis controls colorectal cancer chemoresistance by imposing a slow cell-cycle phenotype (DNA methylation arrays)

Project description:Tumor relapse is linked to rapid chemoresistance and represents a bottleneck for cancer therapy success. Engagement of a reduced proliferation state is a non-mutational mechanism exploited by cancer cells to bypass therapy-induced cell death. Through combining pulse-chase experiments in engineered CRC cells and transcriptomic analyses, we identified DPPA3 as a master regulator of slow-cycling phenotype in CRC. We find that DPPA3 stabilizes HIF1a even in normoxia thus limiting nuclear CCNB1 levels and represses DNA replication and cell cycle programs resulting in a slow cell-cycle phenotype. Down-regulation of HIF1a partially restores a chemosensitive proliferative phenotype in DPPA3-overexpressing cancer cells. In cohorts of patient samples, we find that DPPA3 is a predictive biomarker of CRC chemotherapeutic resistance and tumor relapse. Our work demonstrates that slow-cycling cancer cells exploit a DPPA3/HIF1a axis to support tumor persistence under therapeutic stress and provides key insights on the molecular regulation of tumor cell slow-cycliness and chemoresistance. This dataset comprises DNA methylation data of SW1222 CRC cells subjected to DPPA3 overexpression for 5 days.

2023-07-30 | E-MTAB-12892 | biostudies-arrayexpress

Proteomic Analysis of Foxc1-interacting proteins in HEK293T cells

Project description:Foxc1 has been identified to participate in regulating genes expression directly by binding their promoters as well as playing various roles in signal transduction within the cells. In this study, we found that, in F9 Embryonal Carcinoma cells, Foxc1 repressed the promoter’s transcription activity by binding the region of 1Kb upstream of Transcription Start Site within Nanog promoter.To understand more functions of Foxc1, streptavidin-biotin affinity purification combined with Liquid chromatography electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS) analysis was carried out.Bioinformatic analysis identified 360 proteins which may act as Foxc1 interactors.

2021-09-09 | PXD022178 | Pride

Identification of Bacillus subtilis TerC proteins MeeF and MeeY Co-immunoprecipitated proteins

Project description:Proteins co-immunoprecipitated with C-terminal FLAG-tagged MeeF or MeeY

2023-09-26 | PXD044879 | Pride

Decoding the signalling profile of hematopoietic progenitor kinase 1 (HPK1) in innate immunity: a proteomic approach

Project description:The fine-tuned spatiotemporal response of leukocytes to external stimuli is a hallmark of the immune system. Sensing of stimuli occurs through cell surface receptors, which transmit signals into the cell. Signaling via β2 integrins, B cell, and T cell receptors involve similar pathways. However, the activation of the same signaling molecule can result in opposing cell effector functions. One such example is the hematopoietic progenitor kinase 1 (HPK1), which negatively regulates activation of B and T cells but in contrast enforces neutrophil activation upon β2 integrin receptor engagement. Whether this difference is determined by specific interacting proteins might be disclosed by decoding the binding partners of HPK1. In the adaptive immune system, the interactome of HPK1 has already been described, whereas it is unknown in innate immune cells. Therefore, we set out to identify interacting proteins of HPK1 in the myeloid system. Neutrophil-like differentiated HL-60 cells were exposed to immobilized fibrinogen and either stimulated with Mn2+ to allow β2 integrin-mediated adhesion or left unstimulated for control. Co-immunoprecipitation experiments followed by mass spectrometry led to the identification of 116 proteins interacting with HPK1 in total. Here, 58 proteins were found only in unstimulated cells and 39 proteins only in Mn2+-stimulated adherent cells. From these results we constructed the interacting network of HPK1 with signaling, cytoskeleton-associated, transmembrane, adapter, and other proteins. Taken together, our study provides comprehensive insights into the HPK1 interactome in innate immune cells paving the way to a deeper understanding of the complex signaling profile of HPK1 in leukocytes.

2022-02-10 | PXD021136 | Pride

ZC3H11A interacts with PABPN1 and alters polyadenylation of viral transcripts

Project description:Nuclear mRNA metabolism is regulated by multiple proteins, which either directly bind to RNA or form multi-protein complexes. The RNA-binding protein ZC3H11A is involved in nuclear mRNA export, and NF-κB signaling and is essential during mouse embryo development. Furthermore, previous studies have shown that ZC3H11A is important for nuclear-replicating viruses. However, detailed biochemical characterization of the ZC3H11A protein has been lacking. In this study, we established the ZC3H11A protein interactome in human and mouse cells. We demonstrate that the nuclear poly(A)-binding protein PABPN1 interacts specifically with the ZC3H11A protein and controls ZC3H11A localization into nuclear speckles. We report that ZC3H11A specifically interacts with the human adenovirus type 5 (HAdV-5) capsid mRNA in a PABPN1-dependent manner. Notably, ZC3H11A uses the same zinc finger motifs to interact with PABPN1 and mRNA, with a single zinc finger motif responsible for these functions. Further, we demonstrate that the lack of ZC3H11A alters the polyadenylation of HAdV-5 capsid mRNA. Taken together, our results suggest that the ZC3H11A protein acts as a novel regulator of polyadenylation of nuclear mRNA.

2023-10-24 | PXD042238 | Pride

Protein composition of immunoprecipitated synaptic ribbons.

Project description:The synaptic ribbon is an electron-dense structure found in hair cells and photoreceptors. The ribbon is surrounded by neurotransmitter-filled vesicles and considered to play a role in vesicle release. We generated an objective, quantitative analysis of the protein composition of the ribbon complex using a mass spectrometry-based proteomics analysis. Our use of affinity-purified ribbons and control IgG immunoprecipitations ensure that the identified proteins are indeed associated with the ribbon complex. The use of mouse tissue, where the proteome is complete, generated a comprehensive analysis of the candidates. We identified 30 proteins (comprising 56 isoforms and subunits) associated with the ribbon complex. The ribbon complex primarily comprises proteins found in conventional synapses, which we categorized into 6 functional groups: vesicle handling (38.5%), scaffold (7.3%), cytoskeletal molecules (20.6%), phosphorylation enzymes (10.6%), molecular chaperones (8.2%), and transmembrane proteins from the presynaptic membrane firmly attached to the ribbon (11.3%). The 3 CtBP isoforms represent the major protein in the ribbon whether calculated by molar amount (30%) or by mass (20%). The relatively high quantity of phosphorylation enzymes suggests a very active and regulated structure. The ribbon appears to comprise a concentrated cluster of proteins dealing with vesicle creation, retention and distribution, and consequent exocytosis.

| S-EPMC3274173 | biostudies-literature

TTC7A Localizes to Specific Regions of Chromatin

Project description:Inherited TTC7A loss of function mutations causes intestinal and immune deficiency. TTC7A is expressed in hematopoietic and epithelial cells however its cellular function remains poorly understood. In this work we provided evidence that TTC7A is an intrinsic nucleus factor. In an attempt to link the function of TTC7A in chromatin compaction, histone modifications and general transcriptional regulation we undertook to map the observed interaction of TTC7A to chromatin genome-wide by ChiP-Seq of Flag-tagged WT_TTC7A expressed in B lymphoblastoid cell lines using two anti-Flag antibodies (hereafter IP-Flag1 and IP-Flag2).

2018-10-19 | E-MTAB-5938 | biostudies-arrayexpress

RNA-seq from animals treated with RNAi against prp-8, prp-6, and prp-31

Project description:Transcriptome analysis of a population of control animals and RNAi-treated to partially inactivate genes that are homologs to human genes causing Retinitis Pigmentosa. RNA-seq analyses were performed at L3 larval stage in wild type, and smg-1(r861) mutants that have a defective Non-mediated decay pathway. RNA-seq experiments were also performed in adults glp-4(bn2) mutants that lack of germline. synchronized N2 and smg-1(r861) L1 larvae fed for 24 hours at 20 Â°C with the RNAi clones of prp-6, prp-8, prp-31 and gfp; and 5-day adult glp-4(bn2) worms grown at 25 Â°C and fed first, for 72 hours with OP50 and next, for 48 more hours with the RNAi clones of prp-8, prp-31 and gfp

2016-07-03 | E-GEOD-72952 | biostudies-arrayexpress

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