Cited by 651Cancer-related Molecular PathwaysHeat shock proteins researchUbiquitin and proteasome pathways

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MDMX: a novel p53‐binding protein with some functional properties of MDM2.

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Shvarts, A., Steegenga, W. T., Riteco, N., van Laar, T., Dekker, P., Bazuine, M., van Ham, R. C., van der Houven van Oordt, W., Hateboer, G., van der Eb, A. J., Jochemsen, A. G.·1996·The EMBO Journal

DOI 10.1002/j.1460-2075.1996.tb00919.xPMC PMC452278

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Abstract

Here we report the isolation of a cDNA encoding a new p53-associating protein. This new protein has been called MDMX on the basis of its structural similarity to MDM2, which is especially notable in the p53-binding domain. In addition, the putative metal binding domains in the C-terminal part of MDM2 are completely conserved in MDMX. The middle part of the MDMX and MDM2 proteins shows a low degree of conservation. We can show by co-immunoprecipitation that the MDMX protein interacts specifically with p53 in vivo. This interaction probably occurs with the N-terminal part of p53, because the activity of the transcription activation domain of p53 was inhibited by co-transfection of MDMX. Northern blotting showed that MDMX, like MDM2, is expressed in all tissues tested, and that several mRNAs for MDMX can be detected. Interestingly, the level of MDMX mRNA is unchanged after UV irradiation, in contrast to MDM2 transcription. This observation suggests that MDMX may be a differently regulated modifier of p53 activity in comparison with MDM2. Our study indicates that at least one additional member of the MDM protein family exists which can modulate p53 function.

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Authors: Shvarts, A., Steegenga, W. T., Riteco, N., van Laar, T., Dekker, P., Bazuine, M., van Ham, R. C., van der Houven van Oordt, W., Hateboer, G., van der Eb, A. J., & Jochemsen, A. G.
Affiliations: Leiden University (NL)
ORCID: Steegenga, W. T.
Dekker, P.
Jochemsen, A. G.
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 1996-10-01
Volume: 15
Issue: 19
Pages: 5349-5357
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1002/j.1460-2075.1996.tb00919.x
PMC: PMC452278
OpenAlex: W1592021885
Cited by: 648
References: 59
Citations by year: 2026: 14 · 2025: 13 · 2024: 14 · 2023: 23 · 2022: 26 · 2021: 20 · 2020: 26 · 2019: 21 · 2018: 19 · 2017: 24 · 2016: 39 · 2015: 16 · 2014: 40 · 2013: 25 · 2012: 36
FWCI: 4.05
Type: journal article
Language: en
Open access: green
europepmc.org
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: The EMBO Journal (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Data Archiving and Networked Services (DANS) (submittedVersion)
Topics: Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Keywords: MDMX, MDM2, p53, p53-binding protein, protein-protein interaction, metal-binding domain, p53 regulation, cDNA cloning
MeSH terms: Amino Acid Sequence, Animals, Base Sequence, Cell Line, Cloning, Molecular, Humans, Molecular Sequence Data, Nuclear Proteins, Organ Specificity, Protein Binding, Proto-Oncogene Proteins, Recombinant Fusion Proteins, RNA, Messenger, Transcription, Genetic, Transfection, Ultraviolet Rays, Transcriptional Activation, Tumor Suppressor Protein p53, Sequence Homology, Amino Acid, Sequence Analysis, DNA, DNA, Complementary, Mice, Proto-Oncogene Proteins c-mdm2

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MDMX: a novel p53‐binding protein with some functional properties of MDM2.

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