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June 1, 1997Journal of Biological Chemistry220 citationsOpen Access

Interaction of Arrestin with Clathrin in Receptor Internalization

Arrestin/Clathrin Interaction

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Authors

OGOscar B. GoodmanJKJason G. KrupnickVGVsevolod V. Gurevich

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Overview

This report demonstrates the binding interaction of arrestin with clathrin, highlighting its role in receptor internalization, particularly in G protein-coupled receptors.

Key Points

  • To identify the specific residues in clathrin responsible for the binding of nonvisual arrestins and understand their role in receptor internalization.
  • Limited proteolysis was performed on clathrin cages to assess binding changes.
  • Deletion analysis and alanine scanning mutagenesis localized the arrestin binding site to clathrin residues 89-100.
  • Site-directed mutagenesis identified critical residues in clathrin necessary for arrestin binding.
  • Arrestins beta-arrestin and arrestin3 specifically bind to the clathrin terminal domain fusion protein.
  • Key residues identified include Glu-89, Lys-96, and Lys-98 as critical for arrestin binding (p<0.001).
  • High-affinity clathrin binding by arrestins does not induce coat assembly.
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Cite This Study

Goodman et al. (1997) studied this question.

synapsesocial.com/papers/69d8ee6e1ab91f1400bed910https://doi.org/10.1074/jbc.272.23.15017
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