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Cited by 163Ubiquitin and proteasome pathwaysCancer-related Molecular PathwaysProtein Degradation and Inhibitors

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Emerging insights into HAUSP (USP7) in physiology, cancer and other diseases.

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Bhattacharya, Seemana, Chakraborty, Dipankar, Basu, Malini, Ghosh, Mrinal K·2018·Signal Transduction and Targeted Therapy
DOI 10.1038/s41392-018-0012-yPMC PMC6023882
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Abstract

Herpesvirus-associated ubiquitin-specific protease (HAUSP) is a USP family deubiquitinase. HAUSP is a protein of immense biological importance as it is involved in several cellular processes, including host-virus interactions, oncogenesis and tumor suppression, DNA damage and repair processes, DNA dynamics and epigenetic modulations, regulation of gene expression and protein function, spatio-temporal distribution, and immune functions. Since its discovery in the late 1990s as a protein interacting with a herpes virus regulatory protein, extensive studies have assessed its complex roles in p53-MDM2-related networks, identified numerous additional interacting partners, and elucidated the different roles of HAUSP in the context of cancer, development, and metabolic and neurological pathologies. Recent analyses have provided new insights into its biochemical and functional dynamics. In this review, we provide a comprehensive account of our current knowledge about emerging insights into HAUSP in physiology and diseases, which shed light on fundamental biological questions and promise to provide a potential target for therapeutic intervention.

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Fig. 1 Mode of action of ubiquitin ligases and deubiquitinases for maintenance of the cellular protein pool. Pictorial representation of the 26s proteasomal degradation pathway where a series of ubiquitin ligases (E1, E2, E3) sequentially polyubiqutinate proteins for degradation. Deubiqutinases (DUBs) remove ubiquitin from proteins for their activation or escape from degradation. Altogether, these pathways maintain cellular homeostasis by regulating cellular protein pool
Fig. 1 Mode of action of ubiquitin ligases and deubiquitinases for maintenance of the cellular protein pool. Pictorial representation of the 26s proteasomal degradation pathway where a series of ubiquitin ligases (E1, E2, E3) sequentially polyubiqutinate proteins for degradation. Deubiqutinases (DUBs) remove ubiquitin from proteins for their activation or escape from degradation. Altogether, these pathways maintain cellular homeostasis by regulating cellular protein poolCC BY · PubMed Central
Fig. 2 The HAUSP timeline: 20 years of research. A schematic representation of the 20 years of research on HAUSP from its discovery to the current findings and the relevant discoveries in different phases
Fig. 2 The HAUSP timeline: 20 years of research. A schematic representation of the 20 years of research on HAUSP from its discovery to the current findings and the relevant discoveries in different phasesCC BY · PubMed Central
Fig. 3 Domain structure of HAUSP. a Pictorial representation of HAUSP demonstrating the different domains and binding sites for major interacting partners. b Predictive representation of the complete HAUSP structure (by superimposing pdb structures 4yoc, 5fwi, and 2f1z) with domains representing their respective binding partners ICP0, p53, and EBNA1
Fig. 3 Domain structure of HAUSP. a Pictorial representation of HAUSP demonstrating the different domains and binding sites for major interacting partners. b Predictive representation of the complete HAUSP structure (by superimposing pdb structures 4yoc, 5fwi, and 2f1z) with domains representing their respective binding partners ICP0, p53, and EBNA1CC BY · PubMed Central
Fig. 4 Role of USP7/HAUSP in multiple cellular events. Figure depicts involvement of USP7/HAUSP in multiple cellular events (a Viral-protein association; b DNA damage response; c Epigenetic functions; d Hypoxia; e Immune functions; and f Endosomal functions)
Fig. 4 Role of USP7/HAUSP in multiple cellular events. Figure depicts involvement of USP7/HAUSP in multiple cellular events (a Viral-protein association; b DNA damage response; c Epigenetic functions; d Hypoxia; e Immune functions; and f Endosomal functions)CC BY · PubMed Central
Fig. 5 Major interacting partners/substrates of USP7/HAUSP. Figure presents various crucial interacting oncoproteins and tumor suppressors of USP7/HAUSP with various post-translational modifications (phosphorylation, ubiquitination, deubiquitination, etc.)
Fig. 5 Major interacting partners/substrates of USP7/HAUSP. Figure presents various crucial interacting oncoproteins and tumor suppressors of USP7/HAUSP with various post-translational modifications (phosphorylation, ubiquitination, deubiquitination, etc.)CC BY · PubMed Central
Fig. 6 Regulation of HAUSP. A pictorial representation of the different modes of HAUSP regulation (a Transcriptional and b Post-translational)
Fig. 6 Regulation of HAUSP. A pictorial representation of the different modes of HAUSP regulation (a Transcriptional and b Post-translational)CC BY · PubMed Central
Fig. 7 Structures and IC50 values of potential HAUSP inhibitors. A diagrammatic representation of the chemical structures of potential inhibitors of HAUSP with their reported IC50 values
Fig. 7 Structures and IC50 values of potential HAUSP inhibitors. A diagrammatic representation of the chemical structures of potential inhibitors of HAUSP with their reported IC50 valuesCC BY · PubMed Central

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Metadata

Authors
Bhattacharya, S., Chakraborty, D., Basu, M., & Ghosh, M. K.
Affiliations
  • Indian Institute of Chemical Biology (IN)
  • Surendranath College (IN)
Corresponding author
Ghosh, Mrinal K
ORCID
Venue
Signal Transduction and Targeted Therapy
Publisher
Springer Science and Business Media LLC
Published
2018-06-29
Volume
3
Issue
1
Pages
17-17
ISSN
2059-3635 (ISSN-L)
DOI
10.1038/s41392-018-0012-y
PMC
PMC6023882
OpenAlex
W2809511392
Cited by
162
References
114
Citations by year
2026: 8 · 2025: 27 · 2024: 16 · 2023: 23 · 2022: 29 · 2021: 15 · 2020: 26 · 2019: 16 · 2018: 1
FWCI
5.34
Type
journal article
Language
en
Open access
Licence
Locations
  • Signal Transduction and Targeted Therapy (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
Funders
  • Department of Biotechnology, Ministry of Science and Technology, India
  • Department of Science and Technology, Ministry of Science and Technology, India (SR/NM/NS-1058/2015)
  • Council of Scientific and Industrial Research, India
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
  • Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
Keywords
USP7, deubiquitinase, host-virus interaction, herpesvirus, carcinogenesis, tumor suppression, DNA damage and repair, epigenetic regulation, gene expression regulation, immune function, metabolic disorders, neurological disorders, therapeutic target

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