Modulation of EGF receptor autophosphorylation by alpha-hemolysin of Staphylococcus aureus via protein tyrosine phosphatase

FEBS Lett. 2003 Jan 30;535(1-3):71-6. doi: 10.1016/s0014-5793(02)03862-0.

Abstract

In the presence of assembled alpha-hemolysin (alpha-HL) of Staphylococcus aureus, the epidermal growth factor receptor (EGFr) is rapidly dephosphorylated. Several obvious possibilities that otherwise would have contributed to the dephosphorylation were ruled out. Instead, an elevation in the activity of a protein tyrosine phosphatase appears to be responsible for the observed loss of phosphorylation signal of EGFr. For this dephosphorylation, the assembly of alpha-HL is necessary while lytic pore formation is not required. In summary, the EGFr is unable to retain its phosphorylation signal in the presence of alpha-HL and the process is irreversible.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Substitution
  • Bacterial Toxins / genetics
  • Bacterial Toxins / metabolism*
  • Bacterial Toxins / pharmacology*
  • Carcinoma, Squamous Cell / metabolism*
  • ErbB Receptors / drug effects
  • ErbB Receptors / metabolism*
  • Hemolysin Proteins / genetics
  • Hemolysin Proteins / metabolism*
  • Hemolysin Proteins / pharmacology*
  • Humans
  • Peptide Fragments / metabolism
  • Peptide Fragments / pharmacology
  • Phosphorylation / drug effects
  • Protein Binding / physiology
  • Protein Tyrosine Phosphatases / metabolism*
  • Staphylococcus aureus / enzymology
  • Tumor Cells, Cultured / drug effects

Substances

  • Bacterial Toxins
  • Hemolysin Proteins
  • Peptide Fragments
  • staphylococcal alpha-toxin
  • ErbB Receptors
  • Protein Tyrosine Phosphatases