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Home Technologies A tool to facilitate high affinity binding between beta-Arrestin and GPCR
A tool to facilitate high affinity binding between beta-Arrestin and GPCR

A tool to facilitate high affinity binding between beta-Arrestin and GPCR

Unmet Need

Beta-arrestins are a highly conserved family of cytosolic adaptor proteins that contribute to a multitude of physiological functions through a canonical interaction with various G protein-coupled receptors (GPCRs). Through agonist binding to GPCRs, beta-arrestins are able to invoke a host of cellular responses to hormones, agonist stimuli to promote specific responses. There is a need in research for a useful tool to promote beta-arrestin recruitment to GPCRs artificially in order to fully study the wide range of effects the molecule has on cellular functions in various settings.


Duke inventors have developed a small molecule that is a SUMOylated form of beta-arrestin2. This molecule promotes the formation of high affinity GPCR- beta-arrestin2 and Ran GAP1- beta-arrestin2 complexes. This is intended to be a research tool in the field of GPCR research. Specifically, downstream outcomes of SUMOylated beta-arrestin2 -dependent signaling pathways, including, beta-arrestin recruiting ligands and biased agonists of GPCRs, will lead to enhanced knowledge in the field. SUMOylation provides a new molecular mechanism to direct beta-arrestin to specific sub-cellular compartments and interact with cellular proteins. SUMOYlation has distinct biological consequences that make it the ideal choice for studying this protein-protein interaction in vitro. This has been demonstrated in vitro using various cell lines and fluorescent tags to confirm the localization of SUMOylated beta-arrestin2 and its increased efficacy over ubiquitinated beta-arrestin2.

Other Applications

This technology could also be altered to include both SUMOylation and ubiquitination of beta-arrestin2, allowing for researchers to identify new beta-arrestin signaling pathways.


  • SUMOylation of beta-arrestin2 allows for downstream assessment of beta-arrestin-GPCR interaction
  • High affinity binding to GPCRs allows for the screening of biased agonists
  • SUMOylation of beta-arrestin2 is more effective than regulation by ubiquitination
  • A unique research tool that can be used to identify novel downstream pathways in the field

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