ArticleJournal of the American Chemical Society2013
Membrane orientation of Gα(i)β(1)γ(2) and Gβ(1)γ(2) determined via combined vibrational spectroscopic studies.
Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 43 citations in OpenAlex.
- Engineering Proteins at Interfaces: From Complementary Characterization to Material Surfaces with Designed Functions.Angewandte Chemie (International ed. in English) · 2018Review
- Effect of Lipid Composition on the Membrane Orientation of the G Protein-Coupled Receptor Kinase 2-Gβ1γ2 Complex.Biochemistry · 2016Article
- Theoretical Sum Frequency Generation Spectroscopy of Peptides.The journal of physical chemistry. B · 2015Article
- A new criterion to evaluate water vapor interference in protein secondary structural analysis by FTIR spectroscopy.International journal of molecular sciences · 2014Article
- Unveiling the membrane-binding properties of N-terminal and C-terminal regions of G protein-coupled receptor kinase 5 by combined optical spectroscopies.Langmuir : the ACS journal of surfaces and colloids · 2014Article
- Lipid Fluid-Gel Phase Transition Induced Alamethicin Orientational Change Probed by Sum Frequency Generation Vibrational Spectroscopy.The journal of physical chemistry. C, Nanomaterials and interfaces · 2013Article
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5 authors at 1 institution in 1 country.
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Abstract
The manner in which the heterotrimeric G protein complexes Gβ1γ2 and Gαiβ1γ2 interact with membranes is likely related to their biological function. We combined complementary measurements from sum frequency generation (SFG) vibrational and attenuated total reflectance Fourier transform infrared (ATR-FTIR) spectroscopy to determine the possible membrane orientations of Gβ1γ2 and the Gαiβ1γ2 heterotrimer more precisely than could be achieved using SFG alone. The most likely orientations of Gβ1γ2 and the Gαiβ1γ2 heterotrimer were both determined to fall within a similar narrow range of twist and tilt angles, suggesting that Gβ1γ2 may bind to Gαi without a significant change in orientation. This "basal" orientation seems to depend primarily on the geranylgeranylated C-terminus of Gγ2 along with basic residues at the N-terminus of Gαi, and suggests that activated G protein-coupled receptors (GPCRs) must reorient G protein heterotrimers at lipid bilayers to catalyze nucleotide exchange. The innovative methodologies developed in this paper can be widely applied to study the membrane orientation of other proteins in situ.
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