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. 2015 Feb 15;7(2):709–738. doi: 10.3390/v7020709

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© 2015 by the authors; licensee MDPI, Basel, Switzerland.

This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).

PMC Copyright notice

Interactions of ANK/F-box proteins are known from several poxviral species of the Avipoxvirus (AVPV) [117,122], Parapoxvirus (PPOV) [78], Orthopoxvirus (OPXV) genera [79,80,81,82,83,106,109,115,116], and also the Leporipoxvirus super-group (LSG) genera [84,101,123]. These poxviral proteins bind to Skp1 via F-box domains, and in some cases also interact with other cellular proteins or have an effect on other cellular systems, most frequently the canonical activation of NF-κB1 transcriptional regulation. Green/red underlined poxviral (PXV) proteins indicate demonstrated binding of both Skp1 and a cellular substrate. Ubiquitination (Ub) with SCF1 ligases containing a poxviral ANK/F-box has been shown in several examples: OV008, EVM002, EVM005, and EVM154; E3 ubiquitin ligases also control key parts of the NF-κB signalling via SCF-βTrCP1 and an unknown SCF that target p105 and IκBα for proteasomal degradation and processing.