Heterotrimeric G protein beta1gamma2 subunits change orientation upon complex formation with G protein-coupled receptor kinase 2 (GRK2) on a model membrane.
basic_science · Level V
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- Record sourced from PubMed, PMID 21876134.
- Also identified by DOI 10.1073/pnas.1108236108 and PMC identifier 3174637.
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Abstract
Few experimental techniques can assess the orientation of peripheral membrane proteins in their native environment. Sum Frequency Generation (SFG) vibrational spectroscopy was applied to study the formation of the complex between G protein-coupled receptor (GPCR) kinase 2 (GRK2) and heterotrimeric G protein β(1)γ(2) subunits (Gβγ) at a lipid bilayer, without any exogenous labels. The most likely membrane orientation of the GRK2-Gβγ complex differs from that predicted from the known protein crystal structure, and positions the predicted receptor docking site of GRK2 such that it would more optimally interact with GPCRs. Gβγ also appears to change its orientation after binding to GRK2. The developed methodology is widely applicable for the study of other membrane proteins in situ.
Medical subject headings
- G-Protein-Coupled Receptor Kinase 2
- GTP-Binding Protein beta Subunits
- GTP-Binding Protein gamma Subunits
- Membranes, Artificial