ArticleThe Journal of biological chemistry2011
Structural basis for the 14-3-3 protein-dependent inhibition of the regulator of G protein signaling 3 (RGS3) function.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 27 citations in OpenAlex.
- The interaction of the mitochondrial protein importer TOMM34 with HSP70 is regulated by TOMM34 phosphorylation and binding to 14-3-3 adaptors.The Journal of biological chemistry · 2020Article
- 14-3-3γ binds regulator of G protein signaling 14 (RGS14) at distinct sites to inhibit the RGS14:GαThe Journal of biological chemistry · 2018Article
- Coordination and redox state-dependent structural changes of the heme-based oxygen sensorThe Journal of biological chemistry · 2017Article
- Molecular basis of the 14-3-3 protein-dependent activation of yeast neutral trehalase Nth1.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Regulation of tyrosine hydroxylase is preserved across different homo- and heterodimeric 14-3-3 proteins.Amino acids · 2016Article
- Novel Entropically Driven Conformation-specific Interactions with Tomm34 Protein Modulate Hsp70 Protein Folding and ATPase Activities.Molecular & cellular proteomics : MCP · 2016Article
- Structural Characterization of Phosducin and Its Complex with the 14-3-3 Protein.The Journal of biological chemistry · 2015Article
- Phosphorylation dependence and stoichiometry of the complex formed by tyrosine hydroxylase and 14-3-3γ.Molecular & cellular proteomics : MCP · 2014Article
- Role of the EF-hand-like motif in the 14-3-3 protein-mediated activation of yeast neutral trehalase Nth1.The Journal of biological chemistry · 2014Article
- The assembly and intermolecular properties of the Hsp70-Tomm34-Hsp90 molecular chaperone complex.The Journal of biological chemistry · 2014Article
- Structural modulation of phosducin by phosphorylation and 14-3-3 protein binding.Biophysical journal · 2012Article
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Regulator of G protein signaling (RGS) proteins function as GTPase-activating proteins for the α-subunit of heterotrimeric G proteins. The function of certain RGS proteins is negatively regulated by 14-3-3 proteins, a family of highly conserved regulatory molecules expressed in all eukaryotes. In this study, we provide a structural mechanism for 14-3-3-dependent inhibition of RGS3-Gα interaction. We have used small angle x-ray scattering, hydrogen/deuterium exchange kinetics, and Förster resonance energy transfer measurements to determine the low-resolution solution structure of the 14-3-3ζ·RGS3 complex. The structure shows the RGS domain of RGS3 bound to the 14-3-3ζ dimer in an as-yet-unrecognized manner interacting with less conserved regions on the outer surface of the 14-3-3 dimer outside its central channel. Our results suggest that the 14-3-3 protein binding affects the structure of the Gα interaction portion of RGS3 as well as sterically blocks the interaction between the RGS domain and the Gα subunit of heterotrimeric G proteins.
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