Review
doi: 10.1016/s0962-8924(02)00005-3.
PHD domains and E3 ubiquitin ligases: viruses make the connection
Affiliations
- PMID: 12480335
- DOI: 10.1016/s0962-8924(02)00005-3
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Review
PHD domains and E3 ubiquitin ligases: viruses make the connection
Trends Cell Biol.
2003 Jan.
Abstract
PHD domains constitute a widely distributed subfamily of zinc fingers whose biochemical functions have been unclear until now. Recently, several PHD-containing viral proteins have been identified that promote immune evasion by downregulating proteins that govern immune recognition. Studies show that these viral regulators lead to ubiquitination of their targets by functioning as E3 ubiquitin ligases -- an activity that requires the PHD motif. These are the first examples linking the PHD domain to E3 activity, but the recent discovery of PHD-dependent E3 activity in the cellular kinase MEKK1 and the close structural relation of PHD domains to RING fingers hint that many other PHD proteins might share this activity.
Comment in
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No evidence for PHD fingers as ubiquitin ligases.Trends Cell Biol. 2003 Jun;13(6):285-7; author reply 287-8. doi: 10.1016/s0962-8924(03)00102-8. Trends Cell Biol. 2003. PMID: 12791292 No abstract available.
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