Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Transcriptional, post-transcriptional, and post-translational mechanisms rewrite the tubulin code during cardiac hypertrophy and failure

ABSTRACT: mouse alpha- and beta- tubulin isoform characterization of hypertrophied hearts after 4 days of phenylephrine (PE) or isoproterenol (Iso) induction

INSTRUMENT(S): Q Exactive

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Heart

SUBMITTER: Benjamin Prosser

LAB HEAD: Benjamin L. Prosser

PROVIDER: PXD031797 | Pride | 2022-05-20

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	20201126-QPRC-SP-346_Con01.raw	Raw
	20201126-QPRC-SP-346_Con02.raw	Raw
	20201126-QPRC-SP-346_Con03.raw	Raw
	20201126-QPRC-SP-346_Con04.raw	Raw
	20201126-QPRC-SP-346_Con05.raw	Raw

Items per page:

1 - 5 of 21

Publications

Transcriptional, Post-Transcriptional, and Post-Translational Mechanisms Rewrite the Tubulin Code During Cardiac Hypertrophy and Failure.

Phyo Sai Aung SA Uchida Keita K Chen Christina Yingxian CY Caporizzo Matthew A MA Bedi Kenneth K Griffin Joanna J Margulies Kenneth K Prosser Benjamin L BL

Frontiers in cell and developmental biology 20220401

A proliferated and post-translationally modified microtubule network underlies cellular growth in cardiac hypertrophy and contributes to contractile dysfunction in heart failure. Yet how the heart achieves this modified network is poorly understood. Determining how the "tubulin code"-the permutations of tubulin isoforms and post-translational modifications-is rewritten upon cardiac stress may provide new targets to modulate cardiac remodeling. Further, while tubulin can autoregulate its own expr ...[more]

PMID: 35433678

Similar Datasets

Transcription profiling by array of Rattus norvegicus cardiomyocytes to investigate the effects of 30 or 60 min phenylephrine exposure on gene expression

Project description:Rat neonatal cardiomyocytes were exposed to 100 uM phenylephrine for 0, 30 or 60 mins

2013-01-16 | E-MEXP-3678 | biostudies-arrayexpress

Acetylation level of Pannexin 1 lysine residues following alpha 1 adrenoceptor activation

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

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

CLIP-seq to identify transcriptome-wide TDP-43-RNA binding sites in 293HEK FlipIn cells

Project description:This experiment identified transcriptome-wide TDP-43-RNA binding sites in 293 Hek FlipIn cells. The TDP-43 variant submitted here have varying specificity in binding and deviate from the WT TDP-43 binding pattern in dependence of their reduced propensity to phase separate.

2022-03-16 | E-MTAB-9436 | biostudies-arrayexpress

Correlation between STAT3 binding presence and gene expression levels in subtypes of diffuse large B cell lymphoma

Project description:This SuperSeries is composed of the SubSeries listed below. Refer to individual Series

2013-12-16 | E-GEOD-50724 | biostudies-arrayexpress

A splicing-dependent transcriptional checkpoint associated with pre-spliceosome formation

Project description:There is good evidence for functional interactions between splicing and transcription in eukaryotes, but how and why these processes are coupled remain unknown. Prp5 is an RNA-stimulated ATPase required for pre-spliceosome formation in yeast. We demonstrate through in vivo RNA labelling that, in addition to a splicing defect, the prp5-1 mutation causes a defect in the transcription of intron-containing genes. We present chromatin immunoprecipitation evidence for a transcriptional elongation defect in which RNA polymerase that is phosphorylated at serine 5 of the largest subunit’s heptad repeat accumulates over introns, and that this defect requires the U2 snRNP-associated Cus2p. A similar accumulation of polymerase was observed when pre-spliceosome formation was blocked by a mutation in U2 snRNA. These results indicate the existence of a transcriptional elongation checkpoint that is associated with pre-spliceosome formation during co-transcriptional spliceosome assembly. We propose a role for Cus2p as a potential checkpoint factor in transcription. Examining the Pol II profile in MT strain and WT strain

2014-02-19 | E-GEOD-53647 | biostudies-arrayexpress

EZH2-mediated H3K27me3 targets transcriptional circuits of neuronal differentiation ChIP-seq

Project description:Our work describes novel roles for EZH2 in the specification of cortical neurons. Previous reports established the current model of EZH2-mediated control of neuronal progenitors differentiation through the regulation of their proliferation and developmental transitions. We built on these findings and studied the role of EZH2 in post-mitotic glutamatergic neurons differentiated from embryonic stem cells, a particularly relevant cell type where the impact of its regulation has thus far remained elusive. Briefly, our key results can be summarized as follows: 1. The conditional deletion of EZH2 at the moment of cell cycle exit in neural progenitors allowed us to study the role of EZH2 selectively in post-mitotic glutamatergic neurons. 2. Time course transcriptomic and epigenomic analyses of H3K27me3 in absence of EZH2 revealed a significant dysregulation of transcriptional networks affecting synaptic plasticity, in particular long term depression. 3. These analyses also revealed potential novel roles of EZH2 in controlling the regulation between the glutamatergic signature and the GABAergic one, suggesting a mechanism entailing failure of Prdm13 repression, a histone methyltransferase with a known role in determining GABAergic neurons specification.

2022-03-28 | E-MTAB-11363 | biostudies-arrayexpress

Post-translational modification profiling of Saccharomyces cerevisiae histone methylation enzymes uncovers regulation by upstream signalling pathways

Project description:Histone methylation is central to the regulation of eukaryotic transcription. In Saccharomyces cerevisiae, it is controlled by a system of four methyltransferases (Set1p, Set2p, Set5p, and Dot1p) and four demethylases (Jhd1p, Jhd2p, Rph1p, and Gis1p). While the histone targets for these enzymes are well characterised, the connection of the enzymes with the intracellular signalling network and thus their regulation is poorly understood, in yeast and in all other eukaryotes. Here we report the detailed characterisation of the eight S. cerevisiae enzymes, and show that they carry a total of 75 phosphorylation sites, 93 acetylation sites, and two ubiquitination sites. All enzymes are subject to phosphorylation, although demethylases Jhd1p and Jhd2p contained one and five sites respectively whereas other enzymes carried 14 to 36 sites. Phosphorylation was absent or under-represented on catalytic and other domains but strongly enriched for regions of disorder on methyltransferases, suggesting a role in the modulation of protein-protein interactions. We show that a phosphorylation cluster within an acidic and intrinsically disordered N-terminal region of methyltransferase Set2p regulates H3K36 methylation levels in vivo, thus supporting the functional relevance of disordered phosphosites. While most kinases upstream of the yeast histone methylation enzymes remain unknown, we model the possible connections between the signalling network and the histone-based gene regulatory system and propose an integrated regulatory structure. Our results provide a foundation for future, detailed exploration of the role of specific kinases and phosphosites in the regulation of histone methylation.

2020-12-15 | PXD021214 | Pride

BRD4 dynamics reveal novel acrosome-dependent chromatin reorganization during post-meiotic mammalian sperm development

Project description:During the post-meiotic phase of spermatogenesis, transcription is progressively repressed as the nuclei of haploid spermatids are compacted through a dramatic chromatin reorganization involving hyper-acetylation and replacement of most histones with sperm-specific protamines. Although BRDT has been shown to function in transcription as well as histone removal in post-meiotic spermatids, it is unknown whether other BET family proteins play a role. Immunofluorescence of mouse testes revealed BRD4 in a complete ring around the nuclei of spermatids containing hyper-acetylated histones. The BRD4 ring lies directly adjacent to the acroplaxome, or the cytoskeletal base of the acrosome, and does not form in acrosomal mutant mice. ChIP sequencing in round spermatids revealed enrichment of BRD4 and acetylated histone H3 and H4 at the promoters of active genes. GO Term analysis showed that BRD4 and BRDT bind to distinct subsets of spermatogenesis-specific genes. Association of BRD4 with Cyclin T1 decreases as spermatogenesis progresses despite a persistence of association with acetylated H4. Moreover, acetylated histones are removed from the condensing spermatid nucleus in a wave following the progressing acrosome. These data provide evidence for an interesting mechanism in which BRD4 and perhaps acetylated histones are removed from the spermatid genome via the progressing acrosome as transcription is repressed. Single replicates each of Brd4, H3K9me3, H3K9ac, H4K5ac, H4K8ac, H4K12ac, H4K16ac, H4Kac (pan-acetyl antibody), and input in mouse round spermatid cells; input is used to control for local sonication efficiency bias.

2015-03-06 | E-GEOD-56526 | biostudies-arrayexpress

Whole genome mapping of STAT3 binding sites in the two major subtypes of diffuse large B cell lymphoma

Project description:The goal of this study is to identify the effect of the transcription factor STAT3 in the two major subtypes of diffuse large B cell lymphoma (DLBCL). STAT3 is a signal transducer that, when dysregulated, becomes a powerful oncogene found in many human cancers, including DLBCL. DLBCL is the most common form of non-Hodgkin’s lymphoma and has two major subtypes: germinal center B-cell-like (GCB) and activated B-cell-like (ABC). When compared to the GCB form, ABC lymphomas respond much more poorly to current therapies and often exhibit overexpression or overactivation of STAT3. To investigate how STAT3 might contribute to this aggressive phenotype, we have used ChIP-Seq to identify STAT3 binding sites in 8 DLBCL cell lines (4 GCB subtype, 4 ABC) that are derived from patient tumors. 10,337 distinct STAT3 binding regions are occupied in at least two of the eight cell lines. One third (n = 3524) are differentially bound by STAT3 between the two subtypes (FDR < 0.05). More BRs are strongly bound in ABC than in GCB: 44% of differentially bound BRs (n = 1550) show more STAT3 binding in GCB, while 56% (n = 1974) are more strongly bound in ABC. Identification and comparison of STAT3 transcription factor binding sites in 8 cell lines that represent the 2 subtypes of DLBCL. 4 cell lines are subtyped as ABC and 4 are subtyped as GCB. 2-9 replicates and 1 input control are present for each cell line. (Cell line OCI-Ly19 was not included in the final analysis because RNA-Seq showed that its gene expression clustered in between the subtypes, probably due to its EBV+ status. However, its peak calls were used in intermediate steps of the analysis pipeline. Its sequencing runs have been included for completeness.)

2013-12-16 | E-GEOD-50723 | biostudies-arrayexpress

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data