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- W438311957 abstract "β-arrestins 1 and 2 (BARRIand I3ARR2) are two highly homologous proteins with multiple biological functions. First known as key regulators of G protein-coupled receptor (GPCR) desensitization and endocytosis, βARRs were shown more recently to act as scaffolding proteins for ERK1/2 and JNK3 cascades, to activate Src and to bind to ubiquitin ligases. In addition to their propensity to interact with multiple partners, βARRs might also auto-assemble to form oligomers, as suggested by the observation that both IJARR1 and visual arrestin, the isoform which is specifically expressed in the retina, form dimers in crystals. In a two-hybrid screen, based on the Sos Recruitment System and using a C-terminal truncated mutant of βARR2 as the bait, one of the preys corresponded to the C-terminal portion of βARR2 itself, suggesting that βARR2 might also form dimers in solution. To investigate whether βARR2 might function as a dimer in a more physiological context, we took advantage of the bioluminescence energy transfer (BRET) approach, which was developed recently to study protein-protein interaction in living cells. The cDNAs encoding Renilla luciferase (lue) and the yellow variant of the Green Fluorescent Protein (YFP), the BRET donor and accepter moieties, respectively, were fused 5' or 3' to the cDNAs of βARR1 or βARR2. Various appropriate combinations of the resulting constructs were transfected in COS-7 cells. A constitutive BRET was measured with βARR2 constructs. As expected for a specific non-random interaction between the BRET donor and accepter, BRET signals increased as a function of the BRET accepter concentration up to a maximal value (BRETmax), and constant BRET signals were measured when cells were transfected with increasing amounts of a fixed ratio of acceptordonor. Interestingly, significantly different BRETmax values were measured when the BRET donor construct (βARR2-luc) was co-expressed with fusion proteins in which the BRET accepter was located either at the N-terminal (YFP-βARR2) or the C-terminal (βARR2-YFP) extremity of βARR2, indicating that the βARR-2 dimer is oriented. A similar constitutive BRET was also measured for βARR1 and when the BRET donor and the accepter were fused to different UARRisoforms. These data are consistent with a model in which both βARR2 and βARR1 form constitutive homo-dimers in living cells and might also be engaged in constitutive hetero-dimers. Several important questions are still under investigation, such as the proportion of dimers versus monomers, the effect of GPCR activation on βARR dimerization, the potentially different biological function of monomers, homo-dimers and hetero-dimers" @default.
- W438311957 created "2016-06-24" @default.
- W438311957 creator A5054954261 @default.
- W438311957 date "2007-01-01" @default.
- W438311957 modified "2023-09-27" @default.
- W438311957 title "Identification de nouveaux partenaires d'interaction des β-arrestines : 1-oligomérisation des β-arrestines : 2-Caractérisation de l'intéraction β-arrestine- Filamine A" @default.
- W438311957 hasPublicationYear "2007" @default.
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