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Emerging From the Unknown: Structural and Functional Features of Agnoprotein of Polyomaviruses.

Authors
  • Saribas, A Sami1
  • Coric, Pascale2
  • Hamazaspyan, Anahit1
  • Davis, William1
  • Axman, Rachael1
  • White, Martyn K1
  • Abou-Gharbia, Magid3
  • Childers, Wayne3
  • Condra, Jon H3
  • Serge Bouaziz2
  • Safak, Mahmut1
Type
Published Article
Journal
Journal of Cellular Physiology
Publisher
Wiley (John Wiley & Sons)
Publication Date
Feb 16, 2016
Volume
231
Issue
10
Pages
2115–2127
Identifiers
DOI: 10.1002/jcp.25329
PMID: 26831433
Source
USPC - SET - SVS
License
White

Abstract

Agnoprotein 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, HP1α, PP2A, AP-3, PCNA, and α-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. © 2016 Wiley Periodicals, Inc.

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