Further insight into substrate recognition by USP7: structural and biochemical analysis of the HdmX and Hdm2 interactions with USP7.
Abstract
Ubiquitin-specific protease 7 (USP7) catalyzes the deubiquitination of several substrate proteins including p53 and Hdm2. We have previously shown that USP7, and more specifically its amino-terminal domain (USP7-NTD), interacts with distinct regions on p53 and Hdm2 containing P/AxxS motifs. The ability of USP7 to also deubiquitinate and control the turnover of HdmX was recently demonstrated. We utilized a combination of biochemistry and structural biology to identify which domain of USP7 interacts with HdmX as well as to identify regions of HdmX that interact with USP7. We showed that USP7-NTD recognized two of six P/AxxS motifs of HdmX ((8)AQCS(11) and (398)AHSS(401)). The crystal structure of the USP7-NTD:HdmX(AHSS) complex was determined providing the molecular basis of complex formation between USP7-NTD and the HdmX(AHSS) peptide. The HdmX peptide interacted within the same residues of USP7-NTD as previously demonstrated with p53, Hdm2, and EBNA1 peptides. We also identified an additional site on Hdm2 ((397)PSTS(400)) that interacts with USP7-NTD and determined the crystal structure of this complex. Finally, analysis of USP7-interacting peptides on filter arrays confirmed the importance of the serine residue at the fourth position for the USP7-NTD interaction and showed that phosphorylation of serines within the binding sequence prevents this interaction. These results lead to a better understanding of the mechanism of substrate recognition by USP7-NTD.
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USP7 TRAF-like domain substrates include p53, Mdm2, Mdm4, and MCM-BP.
“These substrates include the tumor suppressor p53 (Hu et al., 2006; Sheng et al., 2006), the Mdm2 E3 ubiquitin ligase (Hu et al., 2006; Sheng et al., 2006; Sarkari et al., 2010), the Mdm2 homolog Mdm4 (Sarkari et al., 2010) and mini-chromosome maintenance binding-protein MCM-BP (Jagannathan et al., 2014; Figure 1 and Table 1).”
From USP7 Is a Master Regulator of Genome Stability (2020) · cites this paper as Sarkari et al., 2010
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- Authors
- Sarkari, F., La Delfa, A., Arrowsmith, C. H., Frappier, L., Sheng, Y., & Saridakis, V.
- Affiliations
- University of Toronto (CA)
- University Health Network (CA)
- York University (CA)
- Corresponding author
- Saridakis, Vivian
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2010-10
- Volume
- 402
- Issue
- 5
- Pages
- 825-837
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2069018419
- Cited by
- 54
- References
- 33
- Citations by year
- 2026: 3 · 2025: 6 · 2024: 3 · 2023: 4 · 2021: 4 · 2020: 8 · 2019: 5 · 2018: 1 · 2017: 1 · 2016: 3 · 2015: 5 · 2014: 2 · 2013: 3 · 2012: 3
- FWCI
- 1.17
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- USP7, deubiquitination, substrate recognition, HDMX, MDM2, p53, protein-protein interaction, crystal structure, serine phosphorylation, EBNA1, ubiquitin-specific protease
- MeSH terms
- Ubiquitin-Specific Peptidase 7, Amino Acid Sequence, Binding Sites, Models, Molecular, Molecular Sequence Data, Nuclear Proteins, Phosphorylation, Protein Binding, Proto-Oncogene Proteins, Serine, Sequence Alignment, Crystallography, X-Ray, Cell Cycle Proteins, Protein Structure, Quaternary, Protein Interaction Mapping, Ubiquitin Thiolesterase, Proto-Oncogene Proteins c-mdm2
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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