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Related Experiment Videos

Insect cell-expressed p180erbB3 possesses an impaired tyrosine kinase activity

P M Guy1, J V Platko, L C Cantley

  • 1Department of Pharmacology, Cornell University, Ithaca, NY 14853.

Proceedings of the National Academy of Sciences of the United States of America
|August 16, 1994
PubMed
Summary

p180erbB3, a receptor tyrosine kinase, shows significantly impaired protein tyrosine kinase activity compared to the EGF receptor. This suggests a defect in its intrinsic kinase function, despite proper receptor expression.

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[56] Carbodiimide modification of proteins.

Methods in enzymology·2012

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Signaling

Background:

  • Protein kinases possess conserved residues crucial for catalytic activity.
  • The p180erbB3 receptor tyrosine kinase has altered residues in its catalytic domain, suggesting impaired function.
  • Epidermal Growth Factor (EGF) receptor subfamily members typically exhibit robust kinase activity.

Purpose of the Study:

  • To investigate the protein tyrosine kinase activity of p180erbB3.
  • To compare the kinase activity of p180erbB3 with the human EGF receptor.
  • To determine if altered residues in p180erbB3 impair its catalytic function.

Main Methods:

  • Expression of human EGF receptor and bovine p180erbB3 in insect cells using baculovirus infection.
  • Comparison of autophosphorylation and substrate phosphorylation activities between EGF receptor and p180erbB3.

Related Experiment Videos

  • Assessment of ATP analog binding to p180erbB3 to confirm receptor integrity.

    • Main Results:

    • p180erbB3 exhibited autophosphorylation and substrate phosphorylation at least 2 orders of magnitude less efficiently than the EGF receptor.
    • EGF receptor showed robust EGF-stimulated autophosphorylation and substrate phosphorylation.
    • p180erbB3 successfully bound the ATP analog 5'-p-fluorosulfonylbenzoyladenosine, indicating functional receptor expression.

    Conclusions:

    • p180erbB3 possesses significantly impaired intrinsic tyrosine kinase activity.
    • The observed lack of kinase activity is likely due to alterations in catalytic residues, not receptor denaturation or non-functionality.
    • These findings suggest a specific functional deficiency in p180erbB3's kinase domain.