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Review
. 2024 Sep 2;11(4):285-296.
doi: 10.1055/s-0044-1790210. eCollection 2024 Dec.

Human Viral Oncoproteins and Ubiquitin-Proteasome System

Zahra Rafiei Atani  1   2 , Sareh Sadat Hosseini  3 , Hossein Goudarzi  4 , Ebrahim Faghihloo  4
Affiliations
Review

Human Viral Oncoproteins and Ubiquitin-Proteasome System

Zahra Rafiei Atani et al. Glob Med Genet. .

Abstract

Some human cancers worldwide may be related to human tumor viruses. Knowing, controlling, and managing the viruses that cause cancers remain a problem. Also, tumor viruses use ubiquitin-proteasome system (UPS) that can alter host cellular processes through UPS. Human tumor viruses cause persistent infections, due to their ability to infect their host cells without killing them. Tumor viruses such as Epstein-Barr virus, hepatitis C virus, hepatitis B virus, human papillomaviruses, human T cell leukemia virus, Kaposi's sarcoma-associated herpesvirus, and Merkel cell polyomavirus are associated with human malignancies. They interfere with the regulation of cell cycle and control of apoptosis, which are important for cellular functions. These viral oncoproteins bind directly or indirectly to the components of UPS, modifying cellular pathways and suppressor proteins like p53 and pRb. They can also cause progression of malignancy. In this review, we focused on how viral oncoproteins bind to the components of the UPS and how these interactions induce the degradation of cellular proteins for their survival.

Keywords: UPS; oncoprotein; proteasome; tumor virus; ubiquitin.

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Conflict of interest statement

Conflict of Interest None declared.

Figures

Fig. 1
Fig. 1
EBNA-1 associates with USP7 via binding to p53. p53 is blocked by USP7 and then degraded via proteasome.
Fig. 2
Fig. 2
EBNA-3C associates with Pim-1 and then enhances the proteasomal degradation.
Fig. 3
Fig. 3
NS5A, NS5B (binding to uba domain), and E2–P38 are degraded by proteasome.
Fig. 4
Fig. 4
HBx affects some components and then promotes hepatocyte proliferation.
Fig. 5
Fig. 5
E6 protein of α-HPV 16 binds to p53 by E6AP, then p53 is ubiquitinated and degraded by 26s proteasome, and ubiquitin are released.
Fig. 6
Fig. 6
E7 of α-HPV 16 binds to pRb by C- terminal domain. The C-terminal domain binds to S4 for inducing ATPase activity. Also, E7 binds to pRb by N-terminal domain then pRb degrades through proteasome.
Fig. 7
Fig. 7
LT-antigen binds to SCF Fbw7 and degrades through proteasome. After binding ST-antigen to SCF Fbw7 , LT-antigen can bind to pRb, then degrade it by proteasome and lead the cell to S-phase.
Fig. 8
Fig. 8
LANA protein of KSHV can bind to p53. p53 is ubiquitinated and degraded through 26S proteasome.
Fig. 9
Fig. 9
Tax protein of HTLV binds to pRb by C-terminal domain and binds to proteasome via zinc-finger-binding motifs. Afterward, pRb degrades.
See this image and copyright information in PMC

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