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Endocytosis of growth factor receptors

A Sorkin1, C M Waters

  • 1Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-0146.

Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology
|June 1, 1993
PubMed

Insights

Growth factor (GF) binding to cell surface receptors triggers signaling cascades. Receptor-mediated endocytosis internalizes these complexes, leading to degradation and receptor down-regulation, impacting cell division.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Signal Transduction

Background:

  • Growth factors (GFs) bind to cell surface receptors, initiating signal transduction pathways crucial for cell division (mitosis).
  • GF:receptor complexes are internalized via receptor-mediated endocytosis, a process involving clathrin-coated pits.

Purpose of the Study:

  • To review biochemical, morphological, and kinetic studies on the mechanism of GF endocytosis.
  • To explore the role of GF endocytosis and receptor degradation in mitogenic signaling.

Main Methods:

  • Literature review of biochemical studies.
  • Morphological analysis of endocytosis.
  • Kinetic studies of receptor trafficking.

Main Results:

  • Internalized GF:receptor complexes are sorted into endosomal compartments.
  • A significant portion of internalized complexes bypass recycling and enter degradation pathways.
  • Ligand-induced internalization and lysosomal degradation lead to receptor down-regulation.

Conclusions:

  • Receptor-mediated endocytosis and subsequent degradation are key mechanisms for controlling cell surface receptor levels.
  • Receptor down-regulation via endocytosis plays a significant role in regulating mitogenic signaling pathways initiated by growth factors.

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