SFB-YEATS4 acetylation identification
Ontology highlight
ABSTRACT:
ORGANISM(S): Homo Sapiens
SUBMITTER: 
Yuanzhong Wu
PROVIDER: PXD047355 | iProX | Wed Nov 29 00:00:00 GMT 2023
REPOSITORIES: iProX
Similar Datasets
Project description:PhosphoTMT experiment on HEK293T cells transiently transfected with either SFB-TLK1, SFB-TLK2, or siRNAs targeting TLK1, TLK2, or TLK1 and TLK2. Data represents 4 biological replicates.
2025-01-02 | PXD047966 | Pride
Project description:We have performed ChIP-sequencing analysis on human FOXN2 and RFX1 target sequences in human embryonic kidney HEK293T cells stably expressing Streptavidin-S-FLAG (SFB) triple-tagged proteins. The NGS sequencing were performed on Illumina MiSeq desktop sequencer.
2015-01-01 | E-MTAB-3120 | biostudies-arrayexpress
Project description:Aim to identify the IRF1 acetylation site by KAT8 in cotransfected HEK293T cells
2022-12-05 | PXD038568 |
Project description:Histone deacetylation is involved in epigenetically mediated tumor suppressor genes silencing. The screen of genes modulated by histone acetylation in gastric cancer maycontribute to the identification of potential therapeutic targets. In this experiment we aimed to identify differentially expressed genes by comparing Trichostatin A (TSA)-treated and non-treated gastric cancer cell lines. TrichostatinA (TSA) belongs to the hydroxamic acid chemical class histone deacetylaseinhibitors, which selectively inhibit the class I and II mammalian histonedeacetylase families. As expected, TSA acetylates promoter regions, or disables corepressors, resulting in increased gene expression. The ACP02 and ACP03 gastric cancer cell lines used in this experiment were previously established by our research group from primary gastric adenocarcinomas classified as diffuse and intestinal types, respectively. Both cell lines present chromosome 8 trisomy, MYC amplification, and TP53 loss of copy. Moreover, ACP03 is able to start a tumorigenesis process in Cebus apellas.
2016-10-21 | E-MTAB-4736 | biostudies-arrayexpress
Project description:To identify acetylation-dependent posttranslational modifications (PTMs) of G6PD, site-specifically acetylated and Flag-tagged G6PD was expressed in HEK293T cells by genetically encoding the incorporation of acetylated lysine in response to an in-frame TAG stop codon. K403-acetylated G6PD (sample) and K414-acetylated G6PD (control) were co-expressed with WT Fyn kinase and a catalytically inactive mutant of Fyn (FynDN). G6PD was immunoprecipitated using anti-Flag beads before MS analysis.
2023-10-24 | PXD041775 | Pride
Project description:Pannexin 1 (Panx1) channels can be activated by alpha 1 adrenoceptor-induced pathways for the sympathetic regulation of blood pressure; however, the molecular mechanisms for this form of Panx1 channel activation remain elusive. To identify potential acetyl-lysine residue(s) of Panx1 channels that might be involved in this receptor-mediated Panx1 channel activation, we performed mass-spectrometry on Strep-tagged Panx1 proteins precipitated from the whole cell lysate of HEK293T cells after stable isotope labeling by amino acids in cell culture (SILAC). Those HEK293T cells were transiently transfected with alpha1D adrenoceptors and human Panx1-Strep, with or without phenylephrine stimulation. Equal amounts of light-labeled (control) and heavy-labeled (phenylephrine stimulated) cell lysates were pooled, and Panx1 proteins were precipitated by Strep-Tactin beads, followed by LC-MS-MS analysis. From three biological replicates, we identified a consistent, albeit modest, reduction of acetylation level at K140, following phenylephrine stimulation. Whereas the acetylation level of other lysine residues (K321, K374, K381, K409) were variable among three replicates or were unaffected by phenylephrine treatment. These results implicate Panx1 K140 as a potential regulatory site for receptor-mediated channel activation via an acetylation-deacetylation mechanism.
2021-07-16 | PXD025912 | Pride
Project description:Differences in global levels of histone acetylation occur in normal and cancer cells, although the reason cells regulate these levels has remained unclear. Here we demonstrate a role for histone acetylation in regulating intracellular pH (pHi). As pHi decreases, histones are globally deacetylated by histone deacetylases (HDACs) and the released acetate anions are co-exported with protons out of the cell by monocarboxylate transporters (MCTs), preventing further reductions in pHi. Conversely, global histone acetylation increases at more alkaline pHi, such as when resting cells are induced to proliferate. Inhibition of HDACs or MCTs decreases acetate export and lowers pHi, particularly compromising pHi maintenance in acidic environments. Global deacetylation at low pH is reflected at a genomic level by decreased abundance and extensive redistribution of acetylation at promoters and intergenic regions. Thus acetylation of chromatin functions as a rheostat to regulate pHi with important implications for therapeutic use of HDAC inhibitors. To investigate the redistribution of H4K16ac throughout the genome upon treatment at pH 6.5
2012-11-04 | E-GEOD-40114 | biostudies-arrayexpress
Project description:The incubation of a 10,000 member PNA-encoded peptide library with cells over-expressing the alpha(v)beta(3) and alpha(v)beta(5) integrins (D54) or CCR6 (HEK293T-CCR6) followed by microarray analysis allowed detailed information on the interaction between peptide-ligands and cell surface receptors to be extracted. This allowed the identification of new cell specific ligands for alpha(v)beta(3) and alpha(v)beta(5) integrins and CCR6 and offers an approach to ligand discovery that allows the comparative, competitive and simultaneous analysis of different cell types for the identification of differences in surface-receptor ligands and/or receptor expression between cell types.
2011-08-10 | E-MEXP-3103 | biostudies-arrayexpress
Project description:DNA derived from the genetic material of pathogens or from cellular DNA damage provides a molecular pattern that can be sensed by pattern-recognition receptors of the mammalian innate immune system. In recent years, the cyclic GMP-AMP synthase (cGAS) protein has been characterized as a primary cytosolic DNA sensor during infection with bacteria, DNA viruses, or retroviruses. While the role of cGAS in downstream immune signaling through STING-TBK1-IRF3 proteins is well-defined, regulatory mechanisms of cGAS activity, such as through post-translational modifications (PTMs), are still an active area of research. Here, we report a comprehensive characterization of cGAS phosphorylations and acetylations in three different cell types. Data-dependent proteomic analyses of immunoaffinity purified cGAS was performed in HEK293T cells under control and DNA-challenged conditions (N = 3 each) and human fibroblasts (HFF) cells under control and HSV-1 infected conditions (N = 4 each) to generate candidate cGAS PTM sites. Using parallel reaction monitoring, a total of 11 PTMs (4 phosphorylations and 7 acetylations) were validated in HEK293T, HFF, and THP-1 cells. Of these, 3 phosphorylations and 5 acetylations have not been previously identified. The functions of these modifications were by generating a series of mutants and measuring cGAS-dependent apoptotic and immune signaling activities.
2020-05-11 | PXD017109 | Pride
Project description:Study hypothesis: We hypothesise that the reduced risk of colorectal cancer through increased fibre intake is mediated in part through changes in global protein acetylation.
Primary outcome(s): Altered faecal short chain fatty acid (SCFA) production.
In the cross-sectional arm there is a single sampling timepoint and all primary and secondary measures are made at this point. For the intervention arm sampling is performed at baseline and after 8 weeks of intervention.
| 2425832 | ecrin-mdr-crc