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Saribas AS , Coric P , Hamazaspyan A , Davis W , Axman R , White MK , Abou-Gharbia M , Childers W , Condra JH , Bouaziz S , Safak M
Emerging From the Unknown: Structural and Functional Features of Agnoprotein of Polyomaviruses
J Cell Physiol. 2016 Oct;231(10) :2115-27
PMID: 26831433 PMCID: PMC5217748
AbstractAgnoprotein is an important regulatory protein of polyomaviruses, including JCV, BKV, and SV40. In the absence of its expression, these viruses are unable to sustain their productive life cycle. It is a highly basic phosphoprotein that localizes mostly to the perinuclear area of infected cells, although a small amount of the protein is also found in nucleus. Much has been learned about the structure and function of this important regulatory protein in recent years. It forms highly stable dimers/oligomers in vitro and in vivo through its Leu/Ile/Phe-rich domain. Structural NMR studies revealed that this domain adopts an alpha-helix conformation and plays a critical role in the stability of the protein. It associates with cellular proteins, including YB-1, p53, Ku70, FEZ1, HP1alpha, PP2A, AP-3, PCNA, and alpha-SNAP; and viral proteins, including small t antigen, large T antigen, HIV-1 Tat, and JCV VP1; and significantly contributes the viral transcription and replication. This review summarizes the recent advances in the structural and functional properties of this important regulatory protein. J. Cell. Physiol. 231: 2115-2127, 2016. (c) 2016 Wiley Periodicals, Inc.
Notes1097-4652 Saribas, A Sami Coric, Pascale Hamazaspyan, Anahit Davis, William Axman, Rachael White, Martyn K Abou-Gharbia, Magid Childers, Wayne Condra, Jon H Bouaziz, Serge Safak, Mahmut R01 NS090949/NS/NINDS NIH HHS/United States Journal Article Review United States J Cell Physiol. 2016 Oct;231(10):2115-27. doi: 10.1002/jcp.25329. Epub 2016 Feb 24.