Interaction between the tRNA-Binding and C-Terminal Domains of Yeast Gcn2 Regulates Kinase Activity In Vivo

Eitemau Tebyg

• Enhanced Interaction between Pseudokinase and Kinase Domains in Gcn2 stimulates eIF2α Phosphorylation in Starved Cells
  gan: Lageix, Sebastien, et al.
  Cyhoeddwyd: (2014)
• The tRNA-binding moiety in GCN2 contains a dimerization domain that interacts with the kinase domain and is required for tRNA binding and kinase activation
  gan: Qiu, Hongfang, et al.
  Cyhoeddwyd: (2001)
• Mutations that bypass tRNA binding activate the intrinsically defective kinase domain in GCN2
  gan: Qiu, Hongfang, et al.
  Cyhoeddwyd: (2002)
• Dimerization by Translation Initiation Factor 2 Kinase GCN2 Is Mediated by Interactions in the C-Terminal Ribosome-Binding Region and the Protein Kinase Domain
  gan: Qiu, Hongfang, et al.
  Cyhoeddwyd: (1998)
• Separate domains in GCN1 for binding protein kinase GCN2 and ribosomes are required for GCN2 activation in amino acid-starved cells
  gan: Sattlegger, Evelyn, et al.
  Cyhoeddwyd: (2000)