R7-binding protein targets the G protein β5/R7-regulator of G protein signaling complex to lipid rafts in neuronal cells and brain |
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Authors: | Lylia Nini Abdul A Waheed Leelamma M Panicker Meggan Czapiga Jian-Hua Zhang William F Simonds |
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Institution: | (1) Metabolic Diseases Branch, 10/8C-101, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA;(2) Virus-Cell Interaction Section, HIV Drug Resistance Program, National Cancer Institute at Frederick, Frederick, MD 21702, USA;(3) Research Technologies Branch, Bldg. 4Room B2-30B, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA |
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Abstract: | Background Heterotrimeric guanine nucleotide-binding regulatory proteins (G proteins), composed of Gα, Gβ, and Gγ subunits, are positioned
at the inner face of the plasma membrane and relay signals from activated G protein-coupled cell surface receptors to various
signaling pathways. Gβ5 is the most structurally divergent Gβ isoform and forms tight heterodimers with regulator of G protein
signalling (RGS) proteins of the R7 subfamily (R7-RGS). The subcellular localization of Gβ 5/R7-RGS protein complexes is regulated
by the palmitoylation status of the associated R7-binding protein (R7BP), a recently discovered SNARE-like protein. We investigate
here whether R7BP controls the targeting of Gβ5/R7-RGS complexes to lipid rafts, cholesterol-rich membrane microdomains where
conventional heterotrimeric G proteins and some effector proteins are concentrated in neurons and brain. |
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