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

• Published in: FEBS letters 2003-01, Vol.535 (1-3), p.71-76
• Main Authors: Vandana, Sharma, Navneet, Sangha, Surinder, Kaur, Krishnasastry, M.V
• Format: Article
• Language: English
• Subjects: alpha -Hemolysin; Amino Acid Substitution; autophosphorylation; Bacterial Toxins - genetics; Bacterial Toxins - metabolism; Bacterial Toxins - pharmacology; Carcinoma, Squamous Cell - metabolism; Dephosphorylation; Epidermal growth factor receptor; 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; Pore formation; Protein Binding - physiology; Protein Tyrosine Phosphatases - metabolism; Staphylococcus aureus; Staphylococcus aureus - enzymology; Tumor Cells, Cultured - drug effects; Tyrosine phosphorylation; α-Hemolysin
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(02)03862-0

In the presence of assembled α-hemolysin (α-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 α-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 α-HL and the process is irreversible.