In this issue of the Biochemical Journal, Xu et al. describe how they use a spot peptide array to identify a unique sequence within β-arrestin-2 that is required for both multimerization and ERK1/2 (extracellular-signal-related kinase 1/2) scaffolding. They provide evidence that dimers may serve as more than just ‘storage forms’ of β-arrestins, incapable of interacting with receptors but, rather, perhaps, adding to the specificity of G-protein-coupled-receptor signalling. They show that key charged residues within this dimerization interface of β-arrestin-2 block association with ERK1/2 and subsequent activation of ERK1/2 by β2-adrenergic receptors, while internalization is unaffected. They suggest that self-association may serve as a means of sheltering scaffolding sites on β-arrestins from specific binding partners to prevent constitutive activation of key signalling pathways. These studies enhance our understanding of how β-arrestins can juggle their roles as scaffolds of multiple pathways in response to diverse signals.
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Commentary|
June 12 2008
β-Arrestin multimers: does a crowd help or hinder function?
Kathryn Anne Defea
Kathryn Anne Defea
1
1Division of Biomedical Sciences and Cell, Molecular, and Developmental Biology, University of California Riverside, 1620 Computer Statistics Building, Riverside, CA 92521, U.S.A.
1email: katie.defea@ucr.edu
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Publisher: Portland Press Ltd
Received:
May 20 2008
Accepted:
May 23 2008
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2008 Biochemical Society
2008
Biochem J (2008) 413 (1): e1–e3.
Article history
Received:
May 20 2008
Accepted:
May 23 2008
Citation
Kathryn Anne Defea; β-Arrestin multimers: does a crowd help or hinder function?. Biochem J 1 July 2008; 413 (1): e1–e3. doi: https://doi.org/10.1042/BJ20081009
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