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Data show that protein phosphatase-2A (PP2A) was upregulated in lung adenocarcinoma cell lines that were transfected with midline 1 E3 ubiquitin-protein ligase (MID1)-siRNA, suggesting MID1 negatively regulates PP2A in lung adenocarcinoma.
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identified four miRNAs, miR-19, miR-340, miR-374 and miR-542 that bind to the 3'-UTR of the MID1 mRNA. These miRNAs not only regulate MID1 expression but also mTOR signaling and translation of disease associated mRNAs and could therefore serve as potential drugs for future therapy development
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Our data reveal a novel role for MID1 and for atypical ubiquitination in balancing BRAF35 presence, and likely its activity, within nuclear and cytoplasmic compartments
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P151L MID1 mutation is associated with X-linked Opitz Syndrome.
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the coiled-coil and COS domain (CC-COS) bind to microtubules, demonstrating for the first time that MID1 can directly associate with the microtubules
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Osx is upregulated in patients with Ossification of the posterior longitudinal ligament.
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A130T/V mutations within the MID1 zinc-binding Bbox1 domain affects protein folding.
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MID1 catalyzes the ubiquitination of protein phosphatase 2A and mutations within its Bbox1 domain disrupt polyubiquitination of alpha4 but not of PP2Ac in X-linked Opitz syndrome.
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TRAIL regulates MID1 and TSLP, inflammation, fibrosis, smooth muscle hypertrophy, and expression of inflammatory effector chemokines and cytokines in experimental eosinophilic esophagitis.
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These studies provide insight into the mechanism by which mutations observed in X-linked Opitz G syndrome affect the structure and function of the MID1 Bbox1 domain
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A familial c.1102C>T (p.R368X) mutation in the MID1 gene, is reported.
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Results revealed S422 as a novel phosphorylation site of Osx and GSK-3b played an important role in regulating the protein stability and transactivational activity of Osx.
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Fu ubiquitination and cleavage is one of the key elements connecting the MID1-PP2A protein complex with GLI3 activity control
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Promotion of AR, in addition to enhancement of the Akt-, NFkappaB-, and Hh-pathways by sustained MID1-upregulation during androgen deprivation therapy provides a powerful proliferative scenario for PCa progression into castration resistance
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In prostate cancer cells the inhibitory effect of metformin was mimicked by disruption of MID1 translational regulator complex.
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Two patients with underdeveloped arcuate fasciculus had novel, nonsynonymous variants in MID1 and EN2 genes regulating axon guidance pathway.
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for the first time within the MID1 gene, a complex rearrangement composed of two deletions, an inversion and a small insertion that may suggest the involvement of concurrent non-homologous mechanisms in the generation of the observed structural variant.
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expanded CAG repeats bind to a translation regulatory protein complex containing MID1, protein phosphatase 2A and 40S ribosomal S6 kinase.
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found that MID1 was upregulated in primary human bronchial epithelial cells
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Protein phosphatase 2A (PP2A)-specific ubiquitin ligase MID1 is a sequence-dependent regulator of translation efficiency controlling 3-phosphoinositide-dependent protein kinase-1 (PDPK-1).
