c-Abl Phosphorylates Hdmx and Regulates Its Interaction with p53
Open accessAbstract
Upon exposure to DNA damage the p53 tumor suppressor is accumulated and activated to stall cellular growth. For this to occur, p53 must be relieved from its major inhibitors, Mdm2 (Hdm2 in humans) and Mdmx (Mdm4; Hdmx in humans). A key mechanism controlling this relief is the post-translational modifications of p53 and its inhibitors. We have previously demonstrated that the stress-activated tyrosine kinase, c-Abl, contributes to the relief of p53 from Hdm2. Because Hdmx is the major inhibitor of p53 activity, the additional possibility that c-Abl protects p53 through targeting Hdmx was explored in this study. c-Abl was found to interact with and to phosphorylate Hdmx. This phosphorylation was enhanced in response to DNA damage. Importantly, we mapped the sites of phosphorylation to the p53 binding domain of Hdmx. One of these phosphorylations, on tyrosine 99, inhibited Hdmx interaction with p53. This inhibition is consistent with the predicted role of this residue in the interaction with p53 based on the crystal structure of the interaction site. Our results show that c-Abl not only targets Hdm2, but also Hdmx, which together contribute to p53 activation in response to DNA damage.
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DNA damage-induced phosphorylation of N-terminal residues of Mdm2 at Ser17 by DNA-PK or of Mdmx at Tyr99 by c-abl has been reported to disrupt binding to p53 in vitro.
“DNA damage-induced phosphorylation of N-terminal residues of Mdm2 at Ser17 by DNA-PK [52] or Mdmx at Tyr99 by c-abl [53] have been reported to disrupt binding to p53 in vitro.”
From The p53 orchestra: Mdm2 and Mdmx set the tone (2010) · cites this paper as [53]
Following genotoxic stress, DNA-PK phosphorylates Ser17 of MDM2 and ABL phosphorylates Tyr99 of MDMX, leading to dissociation of p53 from its negative regulators.
“Following genotoxic stress, DNA-dependent protein kinase (DNA-PK) phosphorylates Ser17 of MDM2 (Ref. 35), and ABL (also known as ABL1) phosphorylates Tyr99 of MDMX36. In each case, this leads to the dissociation of p53 from its negative regulators.”
From MDM2, MDMX and p53 in oncogenesis and cancer therapy (2013) · cites this paper as [36]
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- Authors
- Zuckerman, V., Lenos, K., Popowicz, G. M., Silberman, I., Grossman, T., Marine, J.-C., Holak, T. A., Jochemsen, A. G., & Haupt, Y.
- Affiliations
- Hebrew University of Jerusalem (IL)
- Leiden University Medical Center (NL)
- Max Planck Society (DE)
- Ghent University (BE)
- Corresponding author
- Haupt, Ygal
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2009-02
- Volume
- 284
- Issue
- 6
- Pages
- 4031-4039
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2054085388
- Cited by
- 68
- References
- 47
- Citations by year
- 2025: 2 · 2024: 2 · 2022: 2 · 2020: 3 · 2019: 2 · 2018: 3 · 2017: 5 · 2016: 5 · 2015: 10 · 2014: 6 · 2013: 9 · 2012: 4
- FWCI
- 2.64
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Ghent University Academic Bibliography (Ghent University) (submittedVersion)
- Max Planck Institute for Plasma Physics (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 › DNA Repair Mechanisms
- Keywords
- c-Abl, HDMX, MDM4, p53, tyrosine phosphorylation, p53 activation, DNA damage response, p53 inhibitors, protein-protein interaction, post-translational modification
- MeSH terms
- DNA Damage, Humans, Nuclear Proteins, Peptide Mapping, Phosphorylation, Protein Processing, Post-Translational, Proto-Oncogene Proteins, Tumor Suppressor Protein p53, Proto-Oncogene Proteins c-abl, Protein Structure, Tertiary, Cell Cycle Proteins, Catalytic Domain, Cell Line, Tumor, Proto-Oncogene Proteins c-mdm2
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