14-3-3 protein interacts with and affects the structure of RGS domain of regulator of G protein signaling 3 (RGS3)
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
20347994
DOI
10.1016/j.jsb.2010.03.009
PII: S1047-8477(10)00086-9
Knihovny.cz E-resources
- MeSH
- Spectrometry, Fluorescence MeSH
- Phosphorylation MeSH
- Protein Interaction Domains and Motifs MeSH
- Crystallography, X-Ray MeSH
- Humans MeSH
- Models, Molecular MeSH
- Multiprotein Complexes MeSH
- Mutagenesis, Site-Directed MeSH
- Protein Subunits MeSH
- 14-3-3 Proteins chemistry metabolism MeSH
- GTPase-Activating Proteins chemistry genetics metabolism MeSH
- RGS Proteins MeSH
- GTP-Binding Proteins chemistry genetics metabolism MeSH
- Recombinant Proteins chemistry genetics metabolism MeSH
- Fluorescence Resonance Energy Transfer MeSH
- Amino Acid Sequence MeSH
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization MeSH
- Protein Stability MeSH
- Amino Acid Substitution MeSH
- In Vitro Techniques MeSH
- Protein Structure, Tertiary MeSH
- Tryptophan chemistry MeSH
- Binding Sites MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Multiprotein Complexes MeSH
- Protein Subunits MeSH
- 14-3-3 Proteins MeSH
- GTPase-Activating Proteins MeSH
- RGS Proteins MeSH
- GTP-Binding Proteins MeSH
- Recombinant Proteins MeSH
- RGS3 protein, human MeSH Browser
- Tryptophan MeSH
Regulator of G protein signaling (RGS) proteins function as GTPase-activating proteins (GAPs) for the alpha-subunit of heterotrimeric G proteins. Several RGS proteins have been found to interact with 14-3-3 proteins. The 14-3-3 protein binding inhibits the GAP function of RGS proteins presumably by blocking their interaction with G(alpha) subunit. Since RGS proteins interact with G(alpha) subunits through their RGS domains, it is reasonable to assume that the 14-3-3 protein can either sterically occlude the G(alpha) interaction surface of RGS domain and/or change its structure. In this work, we investigated whether the 14-3-3 protein binding affects the structure of RGS3 using the time-resolved tryptophan fluorescence spectroscopy. Two single-tryptophan mutants of RGS3 were used to study conformational changes of RGS3 molecule. Our measurements revealed that the 14-3-3 protein binding induces structural changes in both the N-terminal part and the C-terminal RGS domain of phosphorylated RGS3 molecule. Experiments with the isolated RGS domain of RGS3 suggest that this domain alone can, to some extent, interact with the 14-3-3 protein in a phosphorylation-independent manner. In addition, a crystal structure of the RGS domain of RGS3 was solved at 2.3A resolution. The data obtained from the resolution of the structure of the RGS domain suggest that the 14-3-3 protein-induced conformational change affects the region within the G(alpha)-interacting portion of the RGS domain. This can explain the inhibitory effect of the 14-3-3 protein on GAP activity of RGS3.
References provided by Crossref.org
Structural basis for SARS-CoV-2 nucleocapsid (N) protein recognition by 14-3-3 proteins
The crystal structure of the phosphatidylinositol 4-kinase IIα
Structural modulation of phosducin by phosphorylation and 14-3-3 protein binding
