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Beta-arrestin 2: a receptor-regulated MAPK scaffold for the activation of JNK3

Academic Article
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Overview

authors

  • McDonald, Patricia
  • Chow, C. W.
  • Miller, W. E.
  • Laporte, S. A.
  • Field, M. E.
  • Lin, F. T.
  • Davis, R. J.
  • Lefkowitz, R. J.

publication date

  • November 2000

journal

  • Science  Journal

abstract

  • beta-Arrestins, originally discovered in the context of heterotrimeric guanine nucleotide binding protein-coupled receptor (GPCR) desensitization, also function in internalization and signaling of these receptors. We identified c-Jun amino-terminal kinase 3 (JNK3) as a binding partner of beta-arrestin 2 using a yeast two-hybrid screen and by coimmunoprecipitation from mouse brain extracts or cotransfected COS-7 cells. The upstream JNK activators apoptosis signal-regulating kinase 1 (ASK1) and mitogen-activated protein kinase (MAPK) kinase 4 were also found in complex with beta-arrestin 2. Cellular transfection of beta-arrestin 2 caused cytosolic retention of JNK3 and enhanced JNK3 phosphorylation stimulated by ASK1. Moreover, stimulation of the angiotensin II type 1A receptor activated JNK3 and triggered the colocalization of beta-arrestin 2 and active JNK3 to intracellular vesicles. Thus, beta-arrestin 2 acts as a scaffold protein, which brings the spatial distribution and activity of this MAPK module under the control of a GPCR.

subject areas

  • Angiotensin II
  • Animals
  • Arrestins
  • COS Cells
  • Cell Line
  • Cell Nucleus
  • Cytosol
  • Endosomes
  • Enzyme Activation
  • Humans
  • MAP Kinase Kinase 4
  • MAP Kinase Kinase Kinase 5
  • MAP Kinase Kinase Kinases
  • MAP Kinase Signaling System
  • Mice
  • Mitogen-Activated Protein Kinase 10
  • Mitogen-Activated Protein Kinase Kinases
  • Mitogen-Activated Protein Kinases
  • Mutation
  • Phosphorylation
  • Protein-Tyrosine Kinases
  • Proto-Oncogene Proteins c-jun
  • Rats
  • Receptor, Angiotensin, Type 1
  • Receptors, Angiotensin
  • Recombinant Fusion Proteins
  • Transfection
  • Two-Hybrid System Techniques
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Identity

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.290.5496.1574

PubMed ID

  • 11090355
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Additional Document Info

start page

  • 1574

end page

  • 1577

volume

  • 290

issue

  • 5496

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