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Ap-2/eps15 interaction is required for receptor-mediated endocytosis

Academic Article
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Overview

authors

  • Benmerah, A.
  • Lamaze, C.
  • Begue, B.
  • Schmid, Sandra
  • Dautry-Varsat, A.
  • Cerf-Bensussan, N.

publication date

  • March 1998

journal

  • Journal of Cell Biology  Journal

abstract

  • We have previously shown that the protein Eps15 is constitutively associated with the plasma membrane adaptor complex, AP-2, suggesting its possible role in endocytosis. To explore the role of Eps15 and the function of AP-2/Eps15 association in endocytosis, the Eps15 binding domain for AP-2 was precisely delineated. The entire COOH-terminal domain of Eps15 or a mutant form lacking all the AP-2-binding sites was fused to the green fluorescent protein (GFP), and these constructs were transiently transfected in HeLa cells. Overexpression of the fusion protein containing the entire COOH-terminal domain of Eps15 strongly inhibited endocytosis of transferrin, whereas the fusion protein in which the AP-2-binding sites had been deleted had no effect. These results were confirmed in a cell-free assay that uses perforated A431 cells to follow the first steps of coated vesicle formation at the plasma membrane. Addition of Eps15-derived glutathione-S-transferase fusion proteins containing the AP-2-binding site in this assay inhibited not only constitutive endocytosis of transferrin but also ligand-induced endocytosis of epidermal growth factor. This inhibition could be ascribed to a competition between the fusion protein and endogenous Eps15 for AP-2 binding. Altogether, these results show that interaction of Eps15 with AP-2 is required for efficient receptor-mediated endocytosis and thus provide the first evidence that Eps15 is involved in the function of plasma membrane-coated pits.

subject areas

  • Adaptor Proteins, Signal Transducing
  • Adaptor Proteins, Vesicular Transport
  • Binding Sites
  • Calcium-Binding Proteins
  • Endocytosis
  • HeLa Cells
  • Humans
  • Intracellular Signaling Peptides and Proteins
  • Nerve Tissue Proteins
  • Phosphoproteins
  • Receptor, Epidermal Growth Factor
  • Receptors, Transferrin
  • Recombinant Fusion Proteins
  • Transferrin
  • Tumor Cells, Cultured
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Identity

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.140.5.1055

PubMed ID

  • 9490719
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Additional Document Info

start page

  • 1055

end page

  • 1062

volume

  • 140

issue

  • 5

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