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High MED1 expression is associated with metastasis in breast Cancer.
maintenance of the cancer cell state is dependent on recruitment of Mediator and Cohesin through FOXA and master transcription factors
co-expression of PPARgamma and TRAP220 represents a biomarker for good prognosis in colorectal cancer patients
Data suggest that mediator complex subunit 1 (Med1/TRAP220) is a target for checkpoint kinase 2 (Chk2)-mediated phosphorylation and may play a role in cellular DNA damage responses by mediating proper induction of gene transcription upon DNA damage.
In a cohort of youth at risk for bipolar disorder, pathway analysis showed an enrichment of the glucocorticoid receptor (GR) pathway with the genes MED1, HSPA1L, GTF2A1 and TAF15, which might underlie the previously reported role of stress response in the risk for bipolar disorder in vulnerable populations.
modulation of ESR1-MED1 interactions by cAMP signaling plays a critical role in human decidualization.
Our data indicate that MED1 serves as a key mediator in ARv567es induced gene expression
Results show that miR-1 is downregulated in osteosarcoma cells but both of its targets Med1 and Med31 were overexpressed suggesting that MiR-1 plays an important role on the proliferation of osteosarcoma cells through regulation of Med1 and Med31.
MED1 is required for optimal PRDM16-induced Ucp1 expression
no association between SCZ and the SNPs of VDR, suggesting that VDR is not a major gene for SCZ in Chinese Han population. However, our data indicate a potential involvement of VDR SNPs in the susceptibility of risperidone-treated patients to MetS
hyperactivated ERK and/or AKT signaling pathways promoted MED1 overexpression in prostate cancer cells.
These results demonstrate a role for MED1 in mediating resistance to the pure anti-estrogen fulvestrant both in vitro and in vivo.
multiple modes of the GATA1-MED1 axis may help to fine-tune GATA1 function during GATA1-mediated homeostasis events.
Data concluded that those of VDR ff genotype may be regarded as "low responders" to vitamin D intake in terms of response of circulating 25(OH)D and certain inflammatory biomarkers.
MiR-205 is an epigenetically regulated tumor suppressor that targets MED1.
MED1 is recruited to the HER2 gene and required for its expression.
Med1 (also known as PBP/RB18A/TRAP220/DRIP205) is a component of the human TRAP/Mediator complex that plays an important role in the transcriptional control of various genes
functional communications between the MED1 subunit and the MED24-containing submodule that mediate estrogen receptor functions and growth of both normal mammary epithelial cells and breast carcinoma cells.
Studies indicate that the activation domain of p53 (p53AD) binds directly to the MED17 subunit of Mediator, whereas the p53 C-terminal domain (p53CTD) binds the MED1 subunit.
These results suggest that Mediator structural shifts induced by activator binding help stably orient pol II prior to transcription initiation within the human mediator-RNA polymerase II-TFIIF assembly.
B-cell conditional deficient mice for the Med1 subunit display robust somatic hypermutation.
Data, including data from studies using cells from transgenic/knockout mice, suggest that Med1 plays role in enamel formation; Med1 induces Alpl via stimulation of Notch1 signaling by forming Notch1-RBP-Jk complex on Alpl promoter. (Med1 = mediator complex subunit 1; Alpl = alkaline phosphatase, liver-bone-kidney; Notch1 = Notch gene homolog 1; RBP-Jk = kappa J region recombining binding protein suppressor of hairless)
MED1 in macrophages has an antiatherosclerotic role via PPARgamma-regulated transactivation.
Cardiomyocyte-specific ablation of Med1 causes lethal dilated cardiomyopathy in mice.
Med1 deletion disrupted cardiac mitochondrial and metabolic gene expression patterns
Med1 and Med12, two subunits of the mediator complex implicated in transcription initiation and long-range enhancer/promoter loop formation, are dynamically recruited to the IgH locus enhancers.
We conclude that MED1 regulates the temporal progression of primary spermatocytes through meiosis, with its absence resulting in abbreviated pre-leptotene, leptotene, and zygotene stages, and a prolonged pachytene stage.
These results demonstrate that Med1 is a master regulator in adult stem cells to govern epithelial cell fate
The novel function of MED1 in keratinocytes.
PRDM16 deficiency in BAT reduces MED1 binding at PRDM16 target sites and causes a fundamental change in chromatin architecture at key brown fat-selective genes
Collectively, these observations strongly suggest that MED1 has an important affect on mitochondrial function.
Clk2 phosphorylation of PGC-1alpha disrupts its interaction with Mediator subunit 1, which leads to a suppression of PGC-1alpha activation of peroxisome proliferator-activated receptor alpha target genes in fatty acid oxidation and ketogenesis.
Med1 phosphorylation by its association with AMPK regulates liver cell proliferation and fatty acid oxidation, most likely as a downstream effector of PPARalpha and AMPK
Tshb gene transcription was attenuated in MED1 mutant mice in which the nuclear receptor-binding ability of MED1 was specifically disrupted.
Med1 is a context-dependent GATA-1 coregulator that also exerts specialized functions in erythroid cells to control GATA-1-independent, cell-type-specific genes.
MED1 has roles in maintaining quiescence of keratinocytes and preventing depletion of the follicular stem cells.
Hyperlipidemia in MED1(deltaLiv) mice in response to fasting is due to the accumulation of VLDL, which suggests that MED1 plays a pivotal role in the regulation of plasma triglyceride and cholesterol levels.
Med1 is implicated in adipogenesis, lipid metabolic and biosynthetic processes, glucose metabolism, and mitochondrial metabolic pathways
The activation of gene transcription is a multistep process that is triggered by factors that recognize transcriptional enhancer sites in DNA. These factors work with co-activators to direct transcriptional initiation by the RNA polymerase II apparatus. The protein encoded by this gene is a subunit of the CRSP (cofactor required for SP1 activation) complex, which, along with TFIID, is required for efficient activation by SP1. This protein is also a component of other multisubunit complexes e.g. thyroid hormone receptor-(TR-) associated proteins which interact with TR and facilitate TR function on DNA templates in conjunction with initiation factors and cofactors. It also regulates p53-dependent apoptosis and it is essential for adipogenesis. This protein is known to have the ability to self-oligomerize.
, PPAR binding protein
, PPAR-binding protein
, PPARG binding protein
, TR-interacting protein 2
, activator-recruited cofactor 205 kDa component
, mediator of RNA polymerase II transcription subunit 1
, p53 regulatory protein RB18A
, peroxisome proliferator-activated receptor-binding protein
, thyroid hormone receptor-associated protein complex 220 kDa component
, thyroid hormone receptor-associated protein complex component TRAP220
, thyroid receptor interacting protein 2
, thyroid receptor-interacting protein 2
, vitamin D receptor-interacting protein 230 kD
, vitamin D receptor-interacting protein complex component DRIP205
, mediator complex subunit 1
, peroxisome proliferator-activated receptor binding protein
, membrane component, chromosome 17, surface marker 2
, Ppar binding protein
, peroxisome proliferator activated receptor binding protein