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Recruitment of epidermal growth-factor receptors into coated pits requires their activated tyrosine kinase

Academic Article
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Overview

authors

  • Lamaze, C.
  • Schmid, Sandra

publication date

  • April 1995

journal

  • Journal of Cell Biology  Journal

abstract

  • EGF-receptor (EGF-R) tyrosine kinase is required for the down-regulation of activated EGF-R. However, controversy exists as to whether ligand-induced activation of the EGF-R tyrosine kinase is required for internalization or for lysosomal targeting. We have addressed this issue using a cell-free assay that selectively measures the recruitment of EGF-R into coated pits. Here we show that EGF bound to wild-type receptors is efficiently sequestered in coated pits. In contrast, sequestration of kinase-deficient receptors occurs inefficiently and at the same basal rate of endocytosis of unoccupied receptors or receptors lacking any cytoplasmic domain. Sequestration of deletion mutants of the EGF-R that lack autophosphorylation sites also requires an active tyrosine kinase. This suggests that a tyrosine kinase substrate(s) other than the EGF-R itself, is required for its efficient ligand-induced recruitment into coated pits. Addition of a soluble EGF-R tyrosine kinase fully and specifically restores the recruitment of kinase-deficient EGF-R into coated pits providing a powerful functional assay for identification of these substrate(s).

subject areas

  • Animals
  • Cell Line, Transformed
  • Coated Pits, Cell-Membrane
  • Down-Regulation
  • Endocytosis
  • Epidermal Growth Factor
  • Humans
  • Kinetics
  • L Cells (Cell Line)
  • Lysine
  • Methionine
  • Mice
  • Mutagenesis, Site-Directed
  • Receptor, Epidermal Growth Factor
  • Recombinant Proteins
  • Transfection
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Identity

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.129.1.47

PubMed ID

  • 7698994
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Additional Document Info

start page

  • 47

end page

  • 54

volume

  • 129

issue

  • 1

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