Homo- and hetero-oligomerization of β-arrestins in living cells

被引:74
作者
Storez, H
Scott, MGH
Issafras, H
Burtey, A
Benmerah, A
Muntaner, O
Piolot, T
Coppey-Moisan, M
Bouvier, M
Labbé-Jullie, C
Marullo, S
机构
[1] Inst Cochin, Dept Cell Biol, F-75014 Paris, France
[2] Inst Cochin, Dept Infect Dis, F-75014 Paris, France
[3] INSERM, U567, F-75014 Paris, France
[4] CNRS, UMR 8104, F-75014 Paris, France
[5] Univ Paris 05, Fac Med Rene Descartes, UMR S 8104, F-75014 Paris, France
[6] Univ Paris 06, Inst Jacques Monod, UMR 7592, CNRS, Paris, France
[7] Univ Paris 07, Inst Jacques Monod, UMR 7592, CNRS, Paris, France
[8] Univ Montreal, Dept Biochem, Montreal, PQ H3C 3J7, Canada
关键词
D O I
10.1074/jbc.M508001200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Arrestins are important proteins, which regulate the function of serpentine heptahelical receptors and contribute to multiple signaling pathways downstream of receptors. The ubiquitous beta-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 beta-arrestins was investigated using different approaches, including co-immunoprecipitation of epitope-tagged beta-arrestins and resonance energy transfer (BRET and FRET) in living cells. At steady state and at physiological concentrations, beta-arrestins constitutively form both homo- and hetero-oligomers. Co-expression of beta-arrestin2 and beta-arrestin1 prevented beta-arrestin1 accumulation into the nucleus, suggesting that hetero- oligomerization may have functional consequences. Our data clearly indicate that beta-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.
引用
收藏
页码:40210 / 40215
页数:6
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