PERIODOC ACID SCHIFF (PAS)
- Known as:
- PERIODOC ACID SCHIFF (PAS)
- Catalog number:
- 113080101
- Product Quantity:
- 100 ml
- Category:
- -
- Supplier:
- emmonya
- Gene target:
- PERIODOC ACID SCHIFF (PAS)
Related genes to: PERIODOC ACID SCHIFF (PAS)
- Gene:
- ARNTL NIH gene
- Name:
- aryl hydrocarbon receptor nuclear translocator like
- Previous symbol:
- -
- Synonyms:
- MOP3, JAP3, BMAL1, PASD3, bHLHe5
- Chromosome:
- 11p15.3
- Locus Type:
- gene with protein product
- Date approved:
- 1997-11-06
- Date modifiied:
- 2017-08-18
- Gene:
- ARNTL2 NIH gene
- Name:
- aryl hydrocarbon receptor nuclear translocator like 2
- Previous symbol:
- -
- Synonyms:
- BMAL2, MOP9, CLIF, PASD9, bHLHe6
- Chromosome:
- 12p11.23
- Locus Type:
- gene with protein product
- Date approved:
- 2003-08-21
- Date modifiied:
- 2016-10-05
- Gene:
- EHD1 NIH gene
- Name:
- EH domain containing 1
- Previous symbol:
- PAST1
- Synonyms:
- H-PAST, HPAST1, FLJ42622, FLJ44618
- Chromosome:
- 11q13.1
- Locus Type:
- gene with protein product
- Date approved:
- 1999-08-11
- Date modifiied:
- 2016-10-05
- Gene:
- EHD2 NIH gene
- Name:
- EH domain containing 2
- Previous symbol:
- PAST2
- Synonyms:
- -
- Chromosome:
- 19q13.33
- Locus Type:
- gene with protein product
- Date approved:
- 2000-03-22
- Date modifiied:
- 2016-10-05
- Gene:
- EHD3 NIH gene
- Name:
- EH domain containing 3
- Previous symbol:
- PAST3
- Synonyms:
- -
- Chromosome:
- 2p23.1
- Locus Type:
- gene with protein product
- Date approved:
- 2000-03-22
- Date modifiied:
- 2016-10-05
Related products to: PERIODOC ACID SCHIFF (PAS)
Related articles to: PERIODOC ACID SCHIFF (PAS)
- Mutations in the gene encoding lamins A/C cause an array of tissue-selective diseases, with the heart being the most commonly affected organ. Despite progress in understanding the perturbations emanating from mutations, an integrative understanding of the pathogenesis underlying cardiac dysfunction remains elusive. Using a novel conditional deletion model capable of translatome profiling, we observed that cardiomyocyte-specific deletion in adult mice led to rapid cardiomyopathy with pathological remodeling. Before cardiac dysfunction, -deleted cardiomyocytes displayed nuclear abnormalities, Golgi dilation/fragmentation, and CREB3-mediated stress activation. Translatome profiling identified MED25 activation, a transcriptional cofactor that regulates Golgi stress. Autophagy is disrupted in the hearts of these mice, which can be recapitulated by disrupting the Golgi. Systemic administration of modulators of autophagy or ER stress significantly delayed cardiac dysfunction and prolonged survival. These studies support a hypothesis wherein stress responses emanating from the perinuclear space contribute to the cardiomyopathy development. - Source: PubMed
Publication date: 2024/05/08
Sikder KunalPhillips ElizabethZhong ZhijiuWang NadanSaunders JasmineMothy DavidKossenkov AndrewSchneider TimothyNichtova ZuzanaCsordas GyorgyMargulies Kenneth BChoi Jason C - Short amphipathic peptides are capable of binding to transcriptional coactivators, often targeting the same binding surfaces as native transcriptional activation domains. However, they do so with modest affinity and generally poor selectivity, limiting their utility as synthetic modulators. Here we show that incorporation of a medium-chain, branched fatty acid to the N-terminus of one such heptameric lipopeptidomimetic (LPPM-8) increases the affinity for the coactivator Med25 >20-fold (Ki >100 μM to 4 μM), rendering it an effective inhibitor of Med25 protein-protein interactions (PPIs). The lipid structure, the peptide sequence, and the C-terminal functionalization of the lipopeptidomimetic each influence the structural propensity of LPPM-8 and its effectiveness as an inhibitor. LPPM-8 engages Med25 through interaction with the H2 face of its activator interaction domain and in doing so stabilizes full-length protein in the cellular proteome. Further, genes regulated by Med25-activator PPIs are inhibited in a cell model of triple-negative breast cancer. Thus, LPPM-8 is a useful tool for studying Med25 and mediator complex biology and the results indicate that lipopeptidomimetics may be a robust source of inhibitors for activator-coactivator complexes. - Source: PubMed
Publication date: 2024/04/17
Pattelli Olivia NValdivia Estefanía MartínezBeyersdorf Matthew SRegan Clint SRivas MónicaHebert Katherine AMerajver Sofia DCierpicki TomaszMapp Anna K - Rapid metabolic responses to pathogens are essential for plant survival and depend on numerous transcription factors. Mediator is the major transcriptional co-regulator for integration and transmission of signals from transcriptional regulators to RNA polymerase II. Using four Arabidopsis Mediator mutants, med16, med18, med25 and cdk8, we studied how differences in regulation of their transcript and metabolite levels correlate to their responses to Pseudomonas syringae infection. We found that med16 and cdk8 were susceptible, while med25 showed increased resistance. Glucosinolate, phytoalexin and carbohydrate levels were reduced already before infection in med16 and cdk8, but increased in med25, which also displayed increased benzenoids levels. Early after infection, wild type plants showed reduced glucosinolate and nucleoside levels, but increases in amino acids, benzenoids, oxylipins and the phytoalexin camalexin. The Mediator mutants showed altered levels of these metabolites and in regulation of genes encoding key enzymes for their metabolism. At later stage, mutants displayed defective levels of specific amino acids, carbohydrates, lipids and jasmonates which correlated to their infection response phenotypes. Our results reveal that MED16, MED25 and CDK8 are required for a proper, coordinated transcriptional response of genes which encode enzymes involved in important metabolic pathways for Arabidopsis responses to Pseudomonas syringae infections. - Source: PubMed
Publication date: 2024/03/21
Blomberg JeanetteTasselius ViktorVergara AlexanderKaramat FazeelatImran Qari MuhammadStrand ÅsaRosvall MartinBjörklund Stefan - Familial dilated cardiomyopathy (DCM) is among the leading indications for heart transplantation. DCM alters the transcriptomic profile. The alteration or activation/silencing of physiologically operating transcripts may explain the onset and progression of this pathological state. The mediator complex (MED) plays a fundamental role in the transcription process. The aim of this study is to investigate the MED subunits, which are altered in DCM, to identify target crossroads genes. RNA sequencing allowed us to identify specific MED subunits that are altered during familial DCM, transforming into human myocardial samples. N = 13 MED subunits were upregulated and n = 7 downregulated. MED9 alone was significantly reduced in patients compared to healthy subjects (HS) (FC = -1.257; < 0.05). Interestingly, we found a short MED9 isoform (MED9s) (ENSG00000141026.6), which was upregulated when compared to the full-transcript isoform (MED9f). Motif identification analysis yielded several significant matches ( < 0.05), such as GATA4, which is downregulated in CHD. Moreover, although the protein-protein interaction network showed FOG2/ZFPM2, FOS and ID2 proteins to be the key interacting partners of GATA4, only FOG2/ZFPM2 overexpression showed an interaction score of "high confidence" ≥ 0.84. A significant change in the MED was observed during HF. For the first time, the MED9 subunit was significantly reduced between familial DCM and HS ( < 0.05), showing an increased MED9s isoform in DCM patients with respect to its full-length transcript. MED9 and GATA4 shared the same sequence motif and were involved in a network with FOG2/ZFPM2, FOS, and ID2, proteins already implicated in cardiac development. - Source: PubMed
Publication date: 2024/03/06
Franzese MonicaZanfardino MarioSoricelli AndreaCoppola AnnapaolaMaiello CiroSalvatore MarcoSchiano ConcettaNapoli Claudio - The human Mediator complex subunit MED25 binds transactivation domains (TADs) present in various cellular and viral proteins using two binding interfaces, named H1 and H2, which are found on opposite sides of its ACID domain. Here, we use and compare deep learning methods to characterize human MED25-TAD interfaces and assess the predicted models to published experimental data. For the H1 interface, AlphaFold produces predictions with high-reliability scores that agree well with experimental data, while the H2 interface predictions appear inconsistent, preventing reliable binding modes. Despite these limitations, we experimentally assess the validity of MED25 interface predictions with the viral transcriptional activators Lana-1 and IE62. AlphaFold predictions also suggest the existence of a unique hydrophobic pocket for the Arabidopsis MED25 ACID domain. - Source: PubMed
Publication date: 2024/03/04
Monté DidierLens ZoéDewitte FrédériqueVilleret VincentVerger Alexis