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Viral Interactions with PDZ Domain-Containing Proteins—An Oncogenic Trait?

James, Claire, Roberts, Sally·2016·Pathogens
DOI 10.3390/pathogens5010008PMC PMC4810129
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Abstract

Many of the human viruses with oncogenic capabilities, either in their natural host or in experimental systems (hepatitis B and C, human T cell leukaemia virus type 1, Kaposi sarcoma herpesvirus, human immunodeficiency virus, high-risk human papillomaviruses and adenovirus type 9), encode in their limited genome the ability to target cellular proteins containing PSD95/ DLG/ZO-1 (PDZ) interaction modules. In many cases (but not always), the viruses have evolved to bind the PDZ domains using the same short linear peptide motifs found in host protein-PDZ interactions, and in some cases regulate the interactions in a similar fashion by phosphorylation. What is striking is that the diverse viruses target a common subset of PDZ proteins that are intimately involved in controlling cell polarity and the structure and function of intercellular junctions, including tight junctions. Cell polarity is fundamental to the control of cell proliferation and cell survival and disruption of polarity and the signal transduction pathways involved is a key event in tumourigenesis. This review focuses on the oncogenic viruses and the role of targeting PDZ proteins in the virus life cycle and the contribution of virus-PDZ protein interactions to virus-mediated oncogenesis. We highlight how many of the viral associations with PDZ proteins lead to deregulation of PI3K/AKT signalling, benefitting virus replication but as a consequence also contributing to oncogenesis.

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Figure 1 Oncogenic viruses target a common subset of PDZ proteins. Cellular proteins targeted by the viruses are often components of the polarity complexes Crumbs, Par and Scribble that regulate apico-basal polarity and the formation of intercellular junctions including tight, adherens and gap junctions. The virus proteins that target components of the different complexes are given. ¶These viral proteins do not target the PDZ proteins using a classical PBM. §HPV E6 forms a complex with DLG1 and Cx43 to disturb trafficking. Adapted from Javier R. T., Rice, A. P. 2011 [55].
Figure 1 Oncogenic viruses target a common subset of PDZ proteins. Cellular proteins targeted by the viruses are often components of the polarity complexes Crumbs, Par and Scribble that regulate apico-basal polarity and the formation of intercellular junctions including tight, adherens and gap junctions. The virus proteins that target components of the different complexes are given. ¶These viral proteins do not target the PDZ proteins using a classical PBM. §HPV E6 forms a complex with DLG1 and Cx43 to disturb trafficking. Adapted from Javier R. T., Rice, A. P. 2011 [55].CC BY · PubMed Central
Figure 2 The effects of virus mediated targeting of PDZ proteins often converge on the PI3K/AKT signal transduction pathway. A schematic of the PI3K/AKT pathway showing the PDZ proteins involved that are targets of the viral proteins. PDZ proteins are identified by black outline. PIP2 and PIP3 are phosphoinositides. The reader should refer to the text for a fuller explanation of the effects of the virus proteins on the signalling pathway.
Figure 2 The effects of virus mediated targeting of PDZ proteins often converge on the PI3K/AKT signal transduction pathway. A schematic of the PI3K/AKT pathway showing the PDZ proteins involved that are targets of the viral proteins. PDZ proteins are identified by black outline. PIP2 and PIP3 are phosphoinositides. The reader should refer to the text for a fuller explanation of the effects of the virus proteins on the signalling pathway.CC BY · PubMed Central

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Cited by

Metadata

Authors
James, C., & Roberts, S.
Venue
Pathogens
Publisher
MDPI AG
Published
2016-01-18
Volume
5
Issue
1
Pages
8
ISSN
2076-0817
DOI
10.3390/pathogens5010008
PMC
PMC4810129
Cited by
83
References
5
Language
en
Licence
creativecommons.org/licenses/by/4.0/ (vor)

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