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beta-Arrestin 1 and Galphaq/11 coordinately activate RhoA and stress fiber formation following receptor stimulation.

Publication ,  Journal Article
Barnes, WG; Reiter, E; Violin, JD; Ren, X-R; Milligan, G; Lefkowitz, RJ
Published in: J Biol Chem
March 4, 2005

beta-Arrestins were initially shown, in conjunction with G protein-coupled receptor kinases, to be involved in the desensitization and internalization of activated seven-transmembrane receptors. Recently, beta-arrestin 2 has been shown to act as a signal mediator in mitogen-activated protein kinase cascades and to play a positive regulatory role in chemotaxis. We now show that beta-arrestin 1 is required to activate the small GTPase RhoA leading to the re-organization of stress fibers following the activation of the angiotensin II type 1A receptor. This angiotensin II type 1A receptor-directed RhoA activation and stress fiber formation also require the activation of the heterotrimeric G protein G(alphaq/11). Whereas neither beta-arrestin 1 nor G(alphaq/11) activation alone is sufficient to robustly activate RhoA, the concurrent recruitment of beta-arrestin 1 and activation of G(alphaq/11) leads to full activation of RhoA and to the subsequent formation of stress fibers.

Duke Scholars

Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

March 4, 2005

Volume

280

Issue

9

Start / End Page

8041 / 8050

Location

United States

Related Subject Headings

  • rhoA GTP-Binding Protein
  • beta-Arrestins
  • beta-Arrestin 2
  • beta-Arrestin 1
  • Transfection
  • Time Factors
  • Signal Transduction
  • Recombinant Fusion Proteins
  • Receptor, Angiotensin, Type 1
  • RNA, Small Interfering
 

Citation

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Barnes, W. G., Reiter, E., Violin, J. D., Ren, X.-R., Milligan, G., & Lefkowitz, R. J. (2005). beta-Arrestin 1 and Galphaq/11 coordinately activate RhoA and stress fiber formation following receptor stimulation. J Biol Chem, 280(9), 8041–8050. https://doi.org/10.1074/jbc.M412924200
Barnes, William G., Eric Reiter, Jonathan D. Violin, Xiu-Rong Ren, Graeme Milligan, and Robert J. Lefkowitz. “beta-Arrestin 1 and Galphaq/11 coordinately activate RhoA and stress fiber formation following receptor stimulation.J Biol Chem 280, no. 9 (March 4, 2005): 8041–50. https://doi.org/10.1074/jbc.M412924200.
Barnes WG, Reiter E, Violin JD, Ren X-R, Milligan G, Lefkowitz RJ. beta-Arrestin 1 and Galphaq/11 coordinately activate RhoA and stress fiber formation following receptor stimulation. J Biol Chem. 2005 Mar 4;280(9):8041–50.
Barnes, William G., et al. “beta-Arrestin 1 and Galphaq/11 coordinately activate RhoA and stress fiber formation following receptor stimulation.J Biol Chem, vol. 280, no. 9, Mar. 2005, pp. 8041–50. Pubmed, doi:10.1074/jbc.M412924200.
Barnes WG, Reiter E, Violin JD, Ren X-R, Milligan G, Lefkowitz RJ. beta-Arrestin 1 and Galphaq/11 coordinately activate RhoA and stress fiber formation following receptor stimulation. J Biol Chem. 2005 Mar 4;280(9):8041–8050.

Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

March 4, 2005

Volume

280

Issue

9

Start / End Page

8041 / 8050

Location

United States

Related Subject Headings

  • rhoA GTP-Binding Protein
  • beta-Arrestins
  • beta-Arrestin 2
  • beta-Arrestin 1
  • Transfection
  • Time Factors
  • Signal Transduction
  • Recombinant Fusion Proteins
  • Receptor, Angiotensin, Type 1
  • RNA, Small Interfering