Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Acetylation site mapping on TULP3

ABSTRACT: Fig. 2B: Semi-quantitative acetylation level on TULP3 in the presence of either empty pcDNA 3.1(+), Myc-p300, FLAG-PCAF or FLAG-GCN5 following immunoprecipitation.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Olivier Julien Basil Hubbard

PROVIDER: MSV000086358 | MassIVE | Thu Oct 22 10:29:00 BST 2020

REPOSITORIES: MassIVE

ACCESS DATA

Json Xml

Publications

A conserved acetylation switch enables pharmacological control of tubby-like protein stability.

Kerek Evan M EM Yoon Kevin H KH Luo Shu Y SY Chen Jerry J Valencia Robert R Julien Olivier O Waskiewicz Andrew J AJ Hubbard Basil P BP

The Journal of biological chemistry 20201123

Tubby-like proteins (TULPs) are characterized by a conserved C-terminal domain that binds phosphoinositides. Collectively, mammalian TULP1-4 proteins play essential roles in intracellular transport, cell differentiation, signaling, and motility. Yet, little is known about how the function of these proteins is regulated in cells. Here, we present the protein-protein interaction network of TULP3, a protein that is responsible for the trafficking of G-protein-coupled receptors to cilia and whose ab ...[more]

PMID: 33187986

Similar Datasets

In-vitro acetylation assay of TULP3

Project description:Fig. S1D: An in-vitro assay that identified the acetylation sites on recombinant TULP3 with the addition of recombinant human p300.

2020-10-20 | MSV000086340 | MassIVE

Histone exchange and histone H4 acetylation in wild-type and SET2 deletion yeast strains

Project description:ChIP-on chip assays to measure the change in histone exchange or histone acetylation over the yeast genome, in a SET2 deleted strain compared to the wild-type control. ChIP of Flag and Acetylated H4 from wild-type and SET2 deleted cells were normalized to the Myc enrichment.

2012-07-25 | GSE28096 | GEO

Epigenetic mechanisms to propagate histone acetylation by p300/CBP

Project description:Histone acetylation is important for the activation of gene transcription but little is known about its direct ‘read/write’ mechanisms. Here, we report cryo-electron microscopy structures in which a p300/CBP multidomain monomer recognizes histone H4 N-terminal tail (NT) acetylation (ac) in a nucleosome and acetylates non-H4 histone NTs within the same nucleosome. p300/CBP not only recognized H4NTac via the bromodomain pocket responsible for ‘reading’, but also interacted with the DNA minor grooves via the outside of that pocket. This directed the catalytic center of p300/CBP to one of the non-H4 histone NTs. The primary target that p300 ‘writes’ by ‘reading’ H4NTac was H2BNT, and H2BNTac promoted H2A-H2B dissociation from the nucleosome. We propose a model in which p300/CBP ‘replicates’ histone NT acetylation within the H3-H4 tetramer to inherit epigenetic storage, and ‘transcribes’ it from the H3-H4 tetramer to the H2B-H2A dimers to activate context-dependent gene transcription through local nucleosome destabilization.

2023-05-08 | PXD040835 | Pride

H4K16 acetylation marks active genes and enhancers of embryonic stem cells, but does not alter chromatin compaction (I) [ChIP-Seq]

Project description:We report that acetylation of H4K16 is a new marker of active enhancers and that some enhancers are marked by H3K4me1, MOF and H4K16ac but not by acetylated H3K27 or p300, suggesting that they are novel p300-independent regulatory elements. ChIP-seq for H4K16 acetylation in undifferentiated ES cells, and cells after 3 days of retinoic acid differentiation, along with MNase digested input for both samples

2013-08-23 | E-GEOD-43102 | biostudies-arrayexpress

Targeting P300/CBP reveals discrete regulation of transcription and chromatin accessibility by histone acetylation [singlecellseq]

Project description:To test the long-standing paradigm directly linking histone acetylation with chromatin decompaction and transcriptional output, we used integrated epigenomic and transcriptomic analyses following acute inhibition of major cellular lysine acetyltransferases P300 and CBP. We discovered that P300/CBP inhibition dynamically perturbs acetylation kinetics and dramatically suppresses core-transcriptional networks in the absence of changes to chromatin accessibility. CRISPR/Cas9 screening identified NCOR1 and HDAC3 transcriptional co-repressors as the principle antagonists of P300/CBP by counteracting acetylation turnover kinetics. Finally, deacetylation of H3K27 provides nucleation sites for reciprocal methylation switching, a feature that can be exploited therapeutically by concomitant KDM6A and P300 inhibition. Overall, this study indicates that the steady-state histone acetylation-methylation equilibrium functions as a molecular rheostat governing cellular transcription that is amenable to therapeutic exploitation as an anti-cancer regimen.

2021-05-11 | GSE173811 | GEO

Targeting P300/CBP reveals discrete regulation of transcription and chromatin accessibility by histone acetylation [ChIPseq]

2021-05-11 | GSE173775 | GEO

Targeting P300/CBP reveals discrete regulation of transcription and chromatin accessibility by histone acetylation [CRISPR]

2021-05-11 | GSE173772 | GEO

Targeting P300/CBP reveals discrete regulation of transcription and chromatin accessibility by histone acetylation [ATACseq]

2021-05-11 | GSE174272 | GEO

Targeting P300/CBP reveals discrete regulation of transcription and chromatin accessibility by histone acetylation [TTseq]

2021-05-11 | GSE174267 | GEO

Targeting P300/CBP reveals discrete regulation of transcription and chromatin accessibility by histone acetylation [RNAseq]

2021-05-11 | GSE174266 | GEO