Molecular basis for Gβy-dependent interactions
Publication
, Conference
Ford, CE; Bae, H; Skiba, NP; Hamm, HE
Published in: FASEB Journal
December 1, 1997
Gβy-dependent interactions have profound effects on diverse signaling pathways. In many instances, Ga-GDP disrupts interactions between Gβy and its binding partners. The molecular basis of Gβy-dependent interactions with cellular proteins was studied by using alanine scanning mutagenesis of every amino acid of the Gβ subunit demonstrated to contact the Ga-GDP subunit. Each alanme-substituted mutant was analyzed for its ability to interact with the Ga-GDP, phosducin, and PLC-β2. As expected, some of the mutants were inhibitory but surprisingly, some of the alanine-substituted mutants exhibit enhanced activity in comparison with wildtype Gβy. Our results suggest a molecular logic for interaction between Gβy and its binding partners.
Duke Scholars
Published In
FASEB Journal
ISSN
0892-6638
Publication Date
December 1, 1997
Volume
11
Issue
9
Related Subject Headings
- Biochemistry & Molecular Biology
- 1116 Medical Physiology
- 0606 Physiology
- 0601 Biochemistry and Cell Biology
Citation
APA
Chicago
ICMJE
MLA
NLM
Ford, C. E., Bae, H., Skiba, N. P., & Hamm, H. E. (1997). Molecular basis for Gβy-dependent interactions. In FASEB Journal (Vol. 11).
Ford, C. E., H. Bae, N. P. Skiba, and H. E. Hamm. “Molecular basis for Gβy-dependent interactions.” In FASEB Journal, Vol. 11, 1997.
Ford CE, Bae H, Skiba NP, Hamm HE. Molecular basis for Gβy-dependent interactions. In: FASEB Journal. 1997.
Ford, C. E., et al. “Molecular basis for Gβy-dependent interactions.” FASEB Journal, vol. 11, no. 9, 1997.
Ford CE, Bae H, Skiba NP, Hamm HE. Molecular basis for Gβy-dependent interactions. FASEB Journal. 1997.
Published In
FASEB Journal
ISSN
0892-6638
Publication Date
December 1, 1997
Volume
11
Issue
9
Related Subject Headings
- Biochemistry & Molecular Biology
- 1116 Medical Physiology
- 0606 Physiology
- 0601 Biochemistry and Cell Biology