Viral modulators of cullin RING ubiquitin ligases: culling the host defense

Sci STKE. 2006 May 16;2006(335):pe21. doi: 10.1126/stke.3352006pe21.

Abstract

Cullin RING ubiquitin ligases (CRULs) are found in all eukaryotes and play an essential role in targeting proteins for ubiquitin-mediated destruction, thus regulating a plethora of cellular processes. Viruses manipulate CRULs by redirecting this destruction machinery to eliminate unwanted host cell proteins, thus allowing viruses to slip past host immune barriers. Depending on the host organism, virus-modified CRULs can perform an amazing range of tasks, including the elimination of crucial signal transduction molecules in the human interferon pathway and suppression of virus-induced gene silencing in plants. This Perspective summarizes recent advances in our understanding of how viral proteins manipulate the function of CRULs.

Publication types

  • Review

MeSH terms

  • Animals
  • Arabidopsis Proteins / physiology
  • Carrier Proteins / physiology
  • Cullin Proteins / antagonists & inhibitors
  • Cullin Proteins / physiology*
  • DNA-Binding Proteins / physiology
  • Eukaryotic Cells / enzymology
  • Eukaryotic Cells / virology
  • Humans
  • Models, Biological
  • Multiprotein Complexes
  • Parainfluenza Virus 5 / physiology
  • Peptide Hydrolases / metabolism
  • Plant Viruses / physiology
  • Protein Interaction Mapping
  • Protein Processing, Post-Translational / physiology*
  • RNA Interference
  • STAT1 Transcription Factor / metabolism
  • Structure-Activity Relationship
  • Ubiquitin / physiology
  • Ubiquitin-Protein Ligases / antagonists & inhibitors
  • Ubiquitin-Protein Ligases / physiology*
  • Viral Proteins / pharmacology
  • Viral Proteins / physiology*

Substances

  • Arabidopsis Proteins
  • Carrier Proteins
  • Cullin Proteins
  • DDB1 protein, human
  • DNA-Binding Proteins
  • Multiprotein Complexes
  • RBX1 protein, human
  • STAT1 Transcription Factor
  • Ubiquitin
  • V protein, Paramyxovirus
  • Viral Proteins
  • Ubiquitin-Protein Ligases
  • Peptide Hydrolases