Epidermal growth factor (EGF) promotes phosphorylation at threonine-654 of the EGF receptor: possible role of protein kinase C in homologous regulation of the EGF receptor

Eitemau Tebyg

• Phosphorylation at threonine-654 is not required for negative regulation of the epidermal growth factor receptor by non-phorbol tumor promoters.
  gan: Friedman, B A, et al.
  Cyhoeddwyd: (1989)
• Tumor-promoting phorbol diesters cause the phosphorylation of epidermal growth factor receptors in normal human fibroblasts at threonine-654.
  gan: Davis, R J, et al.
  Cyhoeddwyd: (1985)
• Inhibition of the apparent affinity of the epidermal growth factor receptor caused by phorbol diesters correlates with phosphorylation of threonine-654 but not other sites on the receptor.
  gan: Davis, R J, et al.
  Cyhoeddwyd: (1986)
• Stimulation of phosphorylation of lipocortin at threonine residues by epidermal growth factor (EGF) and the EGF receptor: addition of protein kinase P with polylysine inhibits this effect.
  gan: Abdel-Ghany, M, et al.
  Cyhoeddwyd: (1989)
• Platelet-derived growth factor mimics phorbol diester action on epidermal growth factor receptor phosphorylation at threonine-654.
  gan: Davis, R J, et al.
  Cyhoeddwyd: (1985)