Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 286, Issue 50, Pages 43527-43536Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M111.273573
Keywords
-
Categories
Funding
- Grant Agency of the Academy of Sciences of the Czech Republic [IAA501110801]
- Grant Agency of Charles University [28510]
- Czech Science Foundation [P305/11/0708, P207/10/1040]
- Ministry of Education, Youth, and Sports of the Czech Republic [MSM0021620857, MSM0021620835]
- Ministry of Education, Youth, and Sports of the Czech Republic Center of Neurosciences [LC554]
- Academy of Sciences of the Czech Republic [AV0Z50110509, AV0Z50200510]
Ask authors/readers for more resources
Regulator of G protein signaling (RGS) proteins function as GTPase-activating proteins for the alpha-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-G alpha interaction. We have used small angle x-ray scattering, hydrogen/deuterium exchange kinetics, and Forster resonance energy transfer measurements to determine the low-resolution solution structure of the 14-3-3 zeta.RGS3 complex. The structure shows the RGS domain of RGS3 bound to the 14-3-3 zeta 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 G alpha interaction portion of RGS3 as well as sterically blocks the interaction between the RGS domain and the G alpha subunit of heterotrimeric G proteins.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available