Arrestin mobilizes signaling proteins to the cytoskeleton and redirects their activity.

Hanson SM, Cleghorn WM, Francis DJ, Vishnivetskiy SA, Raman D, Song X, Nair KS, Slepak VZ, Klug CS, Gurevich VV
J Mol Biol. 2007 368 (2): 375-87

PMID: 17359998 · PMCID: PMC1904837 · DOI:10.1016/j.jmb.2007.02.053

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.

MeSH Terms (17)

Animals Arrestin Binding Sites Cell Line Cell Survival Cercopithecus aethiops COS Cells Dimerization Extracellular Signal-Regulated MAP Kinases Humans Microtubules Protein Binding Protein Conformation Protein Transport Proto-Oncogene Proteins c-mdm2 Signal Transduction Tubulin

Connections (2)

This publication is referenced by other Labnodes entities: