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

FEBS Letters

Krishnasastry, M.V¹  Navneet, Sangha¹  Surinder, Kaur¹  Vandana, Sharma¹ 

[1] National Center for Cell Science, Ganeshkind Road, Pune 411 007, India

关键词: α-Hemolysin;    Epidermal growth factor receptor;    Pore formation;    Tyrosine phosphorylation;    Dephosphorylation;   

DOI  :  10.1016/S0014-5793(02)03862-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown