Molecular basis for gβγ-effector interaction: Structural correlation with ga binding site

N. Skiba*, H. Bae, C. Ford, Y. Daaka, E. Reuvenv, L. Shekter, T. Van Biesen, C. S. Yang, D. Lambright, J. Sondek, P. Sigler, Richard J Miller, L. Jan, R. Lefkowitz, H. Hamm

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


This work is a collaborative study by several laboratories directed at localizing sites of interaction between Gβγ, an important mediator of transmembrane signaling, and numerous downstream partners. To this end we have targeted residues on Gβγ that contact the Get subunit in the heterotrimeric complex, since Ga often acts as a negative regulator of Gβy. A traditional alanine scanning mutagenesis approach was used to evaluate the role of each amino acid residue within Ga binding surface of Gβ in the ability of dimer to interact with G-protein receptor kinase 2 (βARK). inward rectifying potassium channel (GIRK), and the a subunits of Ca-channels The data presented supports the idea that Gβγ interacts uniquely with different effectors, although sites of interaction can overlap.

Original languageEnglish (US)
JournalFASEB Journal
Issue number9
StatePublished - Dec 1 1997

ASJC Scopus subject areas

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Genetics


Dive into the research topics of 'Molecular basis for gβγ-effector interaction: Structural correlation with ga binding site'. Together they form a unique fingerprint.

Cite this