Role of helix 8 in G protein-coupled receptors based on structure–function studies on the type 1 angiotensin receptor

G protein-coupled receptors (GPCRs) are transmembrane receptors that convert extracellular stimuli to intracellular signals. The type 1 angiotensin II receptor is a widely studied GPCR with roles in blood pressure regulation, water and salt balance and cell growth. The complex molecular and structur...

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Bibliographic Details
Published in:Molecular and cellular endocrinology 2009-04, Vol.302 (2), p.118-127
Main Authors: Huynh, John, Thomas, Walter Glen, Aguilar, Marie-Isabel, Pattenden, Leonard Keith
Format: Article
Language:English
Subjects:
Activation
Binding Sites
G protein-coupled receptor
Helix 8
Humans
Lipids - chemistry
Membranes
Phosphatidylinositol phosphates
Protein Binding
Protein Structure, Secondary
Receptor, Angiotensin, Type 1 - chemistry
Receptor, Angiotensin, Type 1 - metabolism
Receptor, Angiotensin, Type 1 - physiology
Receptors, G-Protein-Coupled - chemistry
Receptors, G-Protein-Coupled - metabolism
Receptors, G-Protein-Coupled - physiology
Signal Transduction
Type 1 angiotensin receptor
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Summary:G protein-coupled receptors (GPCRs) are transmembrane receptors that convert extracellular stimuli to intracellular signals. The type 1 angiotensin II receptor is a widely studied GPCR with roles in blood pressure regulation, water and salt balance and cell growth. The complex molecular and structural changes that underpin receptor activation and signaling are the focus of intense research. Increasingly, there is an appreciation that the plasma membrane participates in receptor function via direct, physical interactions that reciprocally modulate both lipid and receptor and provide microdomains for specialized activities. Reversible protein:lipid interactions are commonly mediated by amphipathic α-helices in proteins and one such motif – a short helix, referred to as helix VIII/8 (H8), located at the start of the carboxyl (C)-terminus of GPCRs – is gaining recognition for its importance to GPCR function. Here, we review the identification of H8 in GPCRs and examine its capacity to sense and interact with diverse proteins and lipid environment, most notably with acidic lipids that include phosphatidylinositol phosphates.
ISSN:0303-7207
1872-8057
DOI:10.1016/j.mce.2009.01.002