Using In Vitro Pull-Down and In-Cell Overexpression Assays to Study Protein Interactions with Arrestin

Methods Mol Biol. 2019:1957:107-120. doi: 10.1007/978-1-4939-9158-7_7.

Abstract

Nonvisual arrestins (arrestin-2/arrestin-3) interact with hundreds of G protein-coupled receptor (GPCR) subtypes and dozens of non-receptor signaling proteins. Here we describe the methods used to identify the interaction sites of arrestin-binding partners on arrestin-3 and the use of monofunctional individual arrestin-3 elements in cells. Our in vitro pull-down assay with purified proteins demonstrates that relatively few elements in arrestin engage each partner, whereas cell-based functional assays indicate that certain arrestin elements devoid of other functionalities can perform individual functions in living cells.

Keywords: Arrestin; JNK3 activation; MAPK; Protein-protein interactions.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Arrestin / metabolism*
  • Biological Assay / methods*
  • COS Cells
  • Chlorocebus aethiops
  • HEK293 Cells
  • Humans
  • Immobilized Proteins / metabolism
  • Mice
  • Protein Binding
  • Protein Interaction Mapping / methods*
  • Recombinant Fusion Proteins / metabolism

Substances

  • Arrestin
  • Immobilized Proteins
  • Recombinant Fusion Proteins