Mus musculus
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA535475 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR8962300_1.fastq.gz | Fastqsanger.gz | |||
| SRR8962300_2.fastq.gz | Fastqsanger.gz | |||
| SRR8962301_1.fastq.gz | Fastqsanger.gz | |||
| SRR8962301_2.fastq.gz | Fastqsanger.gz | |||
| SRR8962302_1.fastq.gz | Fastqsanger.gz |
Items per page: 5 1 - 5 of 16 |
Similar Datasets
Project description:Myopalladin (MYPN) is a striated muscle-specific protein located in the Z-line and I-band of the sarcomere as well as the nucleus. Analysis of MYPN knockout (MKO) mice showed a 48% reduction in myofiber cross-sectional area in MKO mice and a consequent reduction in isometric force generation and power output. Similarly, reduced myotube width was observed in MKO primary myoblast cultures. RNA-Seq studies revealed downregulation of serum response factor (SRF)-target genes in MKO mice, important for muscle growth and differentiation, and further studies revealed that MYPN, like its homologue PALLD, can bind and bundle filamentous actin as well as interact with MRTF-A, both major players in the regulation of the SRF pathway. Consistently, MYPN increased MRTF-A-mediated activation of SRF signaling in myogenic cells, and transduction of MKO myoblasts with constitutive active SRF rescued the reduced myotube width, demonstrating that MYPN promotes skeletal muscle growth through activation of the SRF pathway.
2020-02-24 | GSE124763 | GEO
Project description:Chemokine signaling is important for the seeding of different sites by hematopoietic stem cells during development. Serum Response Factor (SRF) controls multiple genes governing adhesion and migration, mainly by recruiting members of the Myocardin-Related Transcription Factor (MRTF) family of G-actin regulated cofactors. We used vav-iCre to inactivate MRTF-SRF signaling early during hematopoietic development. In both Srf- and Mrtf-deleted animals, hematopoiesis in fetal liver and spleen is intact, but does not become established in fetal bone marrow. Srf-null HSC/Ps (hematopoietic stem/progenitor cells) fail to effectively engraft in transplantation experiments, exhibiting normal proximal signaling responses to SDF-1, but reduced adhesiveness, F-actin assembly, and reduced motility. Srf-null HSC/Ps fail to polarise in response to SDF-1, and cannot migrate through restrictive membrane pores to SDF-1 or Scf in vitro. Mrtf-null HSC/Ps were also defective in chemotactic responses to SDF-1. MRTF-SRF signaling is thus critical for the response to chemokine signaling during hematopoietic development. Strand specific RNA sequencing (RNA-seq) in sorted WT and SRF deleted LSK cells with or without a 30 minute SDF stimulation and validation by qRT-PCR
2015-03-04 | E-GEOD-63820 | biostudies-arrayexpress
Project description:To control transcription, SRF recruits signal-regulated co-activators, the Ternary Complex Factors (TCFs) and the Myocardin-related Transcription Factors (MRTFs), which compete for a common site on its DNA-binding domain. The TCFs - SAP-1, Elk-1 and Net - are Ets proteins that link SRF activity to Ras-ERK signalling. In contrast, the two MRTFs, MRTF-A and MRTF-B, link SRF activity to Rho-actin signalling. In this novel signalling pathway, the actin-binding MRTF RPEL domain acts as a G-actin sensor, controlling MRTF nuclear accumulation in response to signal-induced depletion of the G-actin pool. Previous studies have suggested that the Ras-ERK signalling and Rho-actin pathways control specific subsets of SRF target genes. We used ChIP-seq and RNA-seq to analyse the immediate-early transcriptional response in NIH3T3 fibroblasts, using pathway-specific inhibitors to identify the contributions of Ras-ERK and Rho-actin signalling Chromatin immunoprecipitation and sequencing (ChIP-seq) in NIH3T3 fibroblast after serum stimulation in presence or absence of LatrunculinB or U0126 drugs and using antibodies against SRF, MRTF-A, MRTF-B, SAP1, ELK1, NET, Pol II, PolII S5P, PolII S2P and total H3. Validation by ChIP-PCR. Strand specific total-RNA-seq following DSN normalisation and validation by qRT-PCR from NIH3T3 stimulated by serum or Cytochalasin D in presence or absence of LatrunculinB and/or U0126 drugs.
2014-04-24 | E-GEOD-45888 | biostudies-arrayexpress
Project description:Chemokine signaling is important for the seeding of different sites by hematopoietic stem cells during development. Serum Response Factor (SRF) controls multiple genes governing adhesion and migration, mainly by recruiting members of the Myocardin-Related Transcription Factor (MRTF) family of G-actin regulated cofactors. We used vav-iCre to inactivate MRTF-SRF signaling early during hematopoietic development. In both Srf- and Mrtf-deleted animals, hematopoiesis in fetal liver and spleen is intact, but does not become established in fetal bone marrow. Srf-null HSC/Ps (hematopoietic stem/progenitor cells) fail to effectively engraft in transplantation experiments, exhibiting normal proximal signaling responses to SDF-1, but reduced adhesiveness, F-actin assembly, and reduced motility. Srf-null HSC/Ps fail to polarise in response to SDF-1, and cannot migrate through restrictive membrane pores to SDF-1 or Scf in vitro. Mrtf-null HSC/Ps were also defective in chemotactic responses to SDF-1. MRTF-SRF signaling is thus critical for the response to chemokine signaling during hematopoietic development.
2015-03-04 | GSE63820 | GEO
Project description:Myocardin-related transcription factor A (MRTF-A) in complex with the serum response factor (SRF) regulates the expression of cytoskeletal genes in response to cytoplasmic and nuclear actin dynamics. Different components of nucleoskeleton, besides nuclear actin, also regulate the activity of MRTF-A. Here we extend these studies by showing that lamina-associated polypeptide 2α (Lap2α), the nucleoplasmic isoform of Lap2, is a novel regulator, and a direct binding partner of MRTF-A. Lap2α is a nucleoplasmic protein that interacts with A-type lamins and the retinoblastoma protein (pRb) and contributes to chromatin organization. Unlike other known MRTF-A regulators, Lap2α is not required for MRTF-A nucleo-cytoplasmic shuttling; it functions within the nucleus where it binds MRTF-A directly via its unique C-terminal domain prior to MRTF-A forming the complex with chromatin and SRF. Such interaction affects MRTF-A transcriptional activity since genome-wide analysis revealed reduced binding of MRTF-A to SRF target genes in Lap2α knockout cells compared to control cells that consequently led to impaired expression of target genes. Our studies therefore add another regulatory layer to the control MRTF-A-SRF-mediated gene expression, and broaden the role of Lap2α in transcriptional regulation.
2020-12-15 | GSE159369 | GEO
Project description:Myocardin-related transcription factor A (MRTF-A) in complex with the serum response factor (SRF) regulates the expression of cytoskeletal genes in response to cytoplasmic and nuclear actin dynamics. Different components of nucleoskeleton, besides nuclear actin, also regulate the activity of MRTF-A. Here we extend these studies by showing that lamina-associated polypeptide 2α (Lap2α), the nucleoplasmic isoform of Lap2, is a novel regulator, and a direct binding partner of MRTF-A. Lap2α is a nucleoplasmic protein that interacts with A-type lamins and the retinoblastoma protein (pRb) and contributes to chromatin organization. Unlike other known MRTF-A regulators, Lap2α is not required for MRTF-A nucleo-cytoplasmic shuttling; it functions within the nucleus where it binds MRTF-A directly via its unique C-terminal domain prior to MRTF-A forming the complex with chromatin and SRF. Such interaction affects MRTF-A transcriptional activity since genome-wide analysis revealed reduced binding of MRTF-A to SRF target genes in Lap2α knockout cells compared to control cells that consequently led to impaired expression of target genes. Our studies therefore add another regulatory layer to the control MRTF-A-SRF-mediated gene expression, and broaden the role of Lap2α in transcriptional regulation.
2020-12-15 | GSE159370 | GEO
Project description:The Kruppel-like factor 5 (Klf5) regulates pluripotent stem cell self-renewal but its role in somatic stem cells is unknown. Klf5 deficient hematopoietic stem cells and progenitors (HSC/P) fail to engraft after transplantation. This HSC/P defect was associated with impaired bone marrow (BM) homing and lodging and decreased retention in BM. The Klf5Δ/Δ HSC/P homing defect associated with decreased adhesion to fibronectin and expression of membrane-bound β1/β2-integrins. In vivo inducible gain-of-function of Klf5 in HSC translated into increased HSC/P adhesion. The expression of Rab5 family members, mediators of β1/β2-integrin recycling in the early endosome, was decreased in Klf5Δ/Δ HSC/P. Klf5 binds directly to the promoter of Rab5a/b and overexpression of Rab5b rescued the expression of activated β1/β2-integrins, adhesion and BM homing of Klf5Δ/Δ HSC/P. Altogether, these data indicate that Klf5 is indispensable for adhesion, homing, lodging and retention of HSC/P in the BM through Rab5-dependent post-translational regulation of Beta1/Beta2 integrins. Differential gene expression analyses was performed with Affymetrix GeneChip Mouse 1.0 ST assay. LSK cells from KLF-/- (n=4) and wt (n=5), bred on a C57BL/6 background, was analyzed for differential gene expression using GeneSpring GX11 using student's T-test.
2013-01-30 | E-GEOD-43806 | biostudies-arrayexpress
Project description:The composition and stiffness of the extracellular matrix (ECM) environment that surrounds Multipotent mesenchymal stem cells (MSCs) stem cells dictates transcriptional programming, thereby affecting stem cell lineage decision-making. Cells sense force between themselves and their microenvironment controlling the capability of MSCs to differentiate into adipocytes, osteocytes and chondrocytes. Force sensing is transmitted by integrin receptors and their associated adhesion signalling complexes. To identify regulators of MSC force sensing we sought to catalogue MSC adhesion complex composition. Therefore we isolated integrin-associated adhesion complexes formed in MSCs plated on the ECM ligand fibronectin. We identifed proteins using mass spectrometry that define a MSC specific subset of adhesion complex proteins consisting of key linkages to the actin cytoskeleton together with integrin signalling and force sensing components.
2016-07-20 | MSV000079956 | MassIVE
Project description:To control transcription, SRF recruits signal-regulated co-activators, the Ternary Complex Factors (TCFs) and the Myocardin-related Transcription Factors (MRTFs), which compete for a common site on its DNA-binding domain. The TCFs - SAP-1, Elk-1 and Net - are Ets proteins that link SRF activity to Ras-ERK signalling. In contrast, the two MRTFs, MRTF-A and MRTF-B, link SRF activity to Rho-actin signalling. In this novel signalling pathway, the actin-binding MRTF RPEL domain acts as a G-actin sensor, controlling MRTF nuclear accumulation in response to signal-induced depletion of the G-actin pool. Previous studies have suggested that the Ras-ERK signalling and Rho-actin pathways control specific subsets of SRF target genes. We used ChIP-seq and RNA-seq to analyse the immediate-early transcriptional response in NIH3T3 fibroblasts, using pathway-specific inhibitors to identify the contributions of Ras-ERK and Rho-actin signalling
2014-04-24 | GSE45888 | GEO
Project description:Serum response factor (SRF) is a ubiquitously expressed transcription factor that is essential for brain development and function. SRF activity is controlled by two competing classes of coactivators, myocardin-related transcription factors (MRTF) and ternary complex factors, which introduce specificity into gene expression programs. Here, we explored the MRTF-mediated regulatory mechanism in mouse cortical neurons. Using gene-reporter assays and pharmacological and genetic approaches in isolated mouse cortical neurons, we found that cyclase-associated protein 1 (CAP1) repressed neuronal MRTF-SRF activity. CAP1 promoted cytosolic retention of MRTF by controlling cytosolic G-actin levels that required its helical folded domain and its CARP domain. This function of CAP1 was not redundant with that of its homolog CAP2 and was independent of cofilin1 and actin-depolymerizing factor. Deep RNA sequencing and mass spectrometry in cerebral cortex lysates from CAP1 knockout (CAP1-KO) mice supported the in vivo relevance for the CAP1-actin-MRTF-SRF signalling axis. Our study identified CAP1 as a repressor of neuronal gene expression and led to the identification of likely MRTF-SRF target genes in the developing cerebral cortex, whose dysregulation may contribute to impaired formation of neuronal networks in CAP1-KO mice. Together with our previous studies that implicated CAP1 in actin dynamics in axonal growth cones or excitatory synapses, we established CAP1 as a crucial actin regulator in neurons.
2025-01-14 | PXD051147 | Pride