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Homo- and Hetero-oligomerization of β-Arrestins in Living Cells

Arrestins are important proteins, which regulate the function of serpentine heptahelical receptors and contribute to multiple signaling pathways downstream of receptors. The ubiquitous β-arrestins are believed to function exclusively as monomers, although self-association is assumed to control the a...

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Published in:The Journal of biological chemistry 2005-12, Vol.280 (48), p.40210-40215
Main Authors: Storez, Hélène, Scott, Mark G.H., Issafras, Hassan, Burtey, Anne, Benmerah, Alexandre, Muntaner, Olivier, Piolot, Tristan, Tramier, Marc, Coppey-Moisan, Maité, Bouvier, Michel, Labbé-Jullié, Catherine, Marullo, Stefano
Format: Article
Language:English
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Summary:Arrestins are important proteins, which regulate the function of serpentine heptahelical receptors and contribute to multiple signaling pathways downstream of receptors. The ubiquitous β-arrestins are believed to function exclusively as monomers, although self-association is assumed to control the activity of visual arrestin in the retina, where this isoform is particularly abundant. Here the oligomerization status of β-arrestins was investigated using different approaches, including co-immunoprecipitation of epitope-tagged β-arrestins and resonance energy transfer (BRET and FRET) in living cells. At steady state and at physiological concentrations, β-arrestins constitutively form both homo- and hetero-oligomers. Co-expression of β-arrestin2 and β-arrestin1 prevented β-arrestin1 accumulation into the nucleus, suggesting that hetero-oligomerization may have functional consequences. Our data clearly indicate that β-arrestins can exist as homo- and hetero-oligomers in living cells and raise the hypothesis that the oligomeric state may regulate their subcellular distribution and functions.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M508001200