ArticleCell cycle (Georgetown, Tex.)2015
The alternative translated MDMX(p60) isoform regulates MDM2 activity.
Article in Cell cycle (Georgetown, Tex.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 8 citations in OpenAlex.
- Cryptic in vitro ubiquitin ligase activity of HDMX towards p53 is probably regulated by an induced fit mechanism.Bioscience reports · 2022Article
- MDM4 alternative splicing and implication in MDM4 targeted cancer therapies.American journal of cancer research · 2021Review
- Mdm2 and MdmX RING Domains Play Distinct Roles in the Regulation of p53 Responses: A Comparative Study of Mdm2 and MdmX RING Domains in U2OS Cells.International journal of molecular sciences · 2020Article
- The long and the short of it: the MDM4 tail so far.Journal of molecular cell biology · 2019Review
- p53 promotes its own polyubiquitination by enhancing the HDM2 and HDMX interaction.Protein science : a publication of the Protein Society · 2018Article
- p53 binds the mdmx mRNA and controls its translation.Oncogene · 2017Article
- Where does transcription start? 5'-RACE adapted to next-generation sequencing.Nucleic acids research · 2016Article
- DNA methylation: conducting the orchestra from exposure to phenotype?Clinical epigenetics · 2016Review
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Isoforms derived from alternative splicing, mRNA translation initiation or promoter usage extend the functional repertoire of the p53, p63 and p73 genes family and of their regulators MDM2 and MDMX. Here we show cap-independent translation of an N-terminal truncated isoform of hMDMX, hMDMX(p60), which is initiated at the 7th AUG codon downstream of the initiation site for full length hMDMX(FL) at position +384. hMDMX(p60) lacks the p53 binding motif but retains the RING domain and interacts with hMDM2 and hMDMX(FL). hMDMX(p60) shows higher affinity for hMDM2, as compared to hMDMX(FL). In vitro data reveal a positive cooperative interaction between hMDMX(p60) and hMDM2 and in cellulo data show that low levels of hMDMX(p60) promote degradation of hMDM2 whereas higher levels stabilize hMDM2 and prevent hMDM2-mediated degradation of hMDMX(FL). These results describe a novel alternatively translated hMDMX isoform that exhibits unique regulatory activity toward hMDM2 autoubiquitination. The data illustrate how the N-terminus of hMDMX regulates its C-terminal RING domain and the hMDM2 activity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.