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

Huynh, J., Thomas, W. G., Aguilar, M. I. and Pattenden, L. K. (2009) Role of helix 8 in G protein-coupled receptors based on structure-function studies on the type 1 angiotensin receptor. Molecular and Cellular Endocrinology, 302 2: 118-127. doi:10.1016/j.mce.2009.01.002


Author Huynh, J.
Thomas, W. G.
Aguilar, M. I.
Pattenden, L. K.
Title Role of helix 8 in G protein-coupled receptors based on structure-function studies on the type 1 angiotensin receptor
Journal name Molecular and Cellular Endocrinology   Check publisher's open access policy
ISSN 0303-7207
Publication date 2009-04
Year available 2009
Sub-type Article (original research)
DOI 10.1016/j.mce.2009.01.002
Volume 302
Issue 2
Start page 118
End page 127
Total pages 10
Editor Dr. I T Huhtaniemi
Dr. W E Rainey
Place of publication Ireland
Publisher Elsevier Ireland Ltd
Collection year 2010
Language eng
Subject C1
970106 Expanding Knowledge in the Biological Sciences
060110 Receptors and Membrane Biology
060111 Signal Transduction
060199 Biochemistry and Cell Biology not elsewhere classified
060108 Protein Trafficking
060602 Animal Physiology - Cell
110201 Cardiology (incl. Cardiovascular Diseases)
110903 Central Nervous System
Abstract G protein-coupled receptors (GPCRs) are transmembrane receptors that convert extracellular stimuli to intracellular signals. The type I 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 alpha-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. (C) 2009 Elsevier Ireland Ltd. All rights reserved.
Q-Index Code C1
Q-Index Status Confirmed Code

Document type: Journal Article
Sub-type: Article (original research)
Collections: 2010 Higher Education Research Data Collection
School of Biomedical Sciences Publications
 
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Created: Thu, 10 Sep 2009, 10:21:48 EST by Cameron Harris on behalf of School of Biomedical Sciences