Arrestin Mobilizes Signaling Proteins to the Cytoskeleton and Redirects their Activity

Susan M. Hanson, Whitney M. Cleghorn, Derek J. Francis, Sergey A. Vishnivetskiy, Dayanidhi Raman, Xiufeng Song, K. Saidas Nair, Vladlen Z. Slepak, Candice S. Klug, Vsevolod V. Gurevich

Research output: Contribution to journalArticlepeer-review

92 Scopus citations


Arrestins regulate the activity and subcellular localization of G protein-coupled receptors and other signaling molecules. Here, we demonstrate that arrestins bind microtubules (MTs) in vitro and in vivo. The MT-binding site on arrestins overlaps significantly with the receptor-binding site, but the conformations of MT-bound and receptor-bound arrestin are different. Arrestins recruit ERK1/2 and the E3 ubiquitin ligase Mdm2 to MTs in cells, similar to the arrestin-dependent mobilization of these proteins to the receptor. Arrestin-mediated sequestration of ERK to MTs reduces the level of ERK activation. In contrast, recruitment of Mdm2 to MTs by arrestin channels Mdm2 activity toward cytoskeleton-associated proteins, increasing their ubiquitination dramatically. The mobilization of signaling molecules to MTs is a novel biological function of arrestin proteins.

Original languageEnglish (US)
Pages (from-to)375-387
Number of pages13
JournalJournal of molecular biology
Issue number2
StatePublished - Apr 27 2007


  • arrestin
  • ERK
  • G-protein coupled receptor
  • Mdm2
  • microtubules

ASJC Scopus subject areas

  • Virology


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