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Articles by Daniel Isom
TM184C is a GPCR-like regulator of intercellular exchange and autophagy
Abstract Sequence similarity underlies most protein annotation, yet many functions remain hidden beyond detectable homology1,2,3. By mining millions of AlphaFold2 models4,5, we identify two human families of ‘superdark’ seven-transmembrane proteins—TM184 and PRRT—with structural homology to G-protein-coupled receptors (GPCRs). These proteins exhibit hallmark GPCR activities, including β-arrestin recruitment and GPCR kinase (GRK)-dependent phosphorylation.
Compartment-Specific Activation of the Proton-Sensor GPR65 is Uncoupled from Receptor Trafficking
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Predictable cholesterol binding sites in GPCRs lack consensus motifs
Highlights • A rapidly growing number of GPCR structures have been solved by cryo-EM • Cholesterol-binding patterns are similar in cryo-EM and X-ray GPCR structures • 92% of cholesterol in GPCR structures map to 12 Cholesterol Network Clusters (CNCs) • There are no broadly recurring cholesterol-binding motifs in GPCRs Summary A rich diversity of transmembrane G protein-coupled receptors (GPCRs) are used by eukaryotes to sense physical and chemical signals.
HCAR3: an underexplored metabolite sensor
BIOBUSINESS BRIEFS 02 October 2020 Nicholas J. Kapolka & Department of Molecular and Cellular Pharmacology, University of Miami Miller School of Medicine, Miami, FL, USA. Daniel G. Isom 1Department of Molecular and Cellular Pharmacology, University of Miami Miller School of Medicine, Miami, FL, USA.2University of Miami Sylvester Comprehensive Cancer Center, Miami, FL, USA.3Institute for Data Science and Computing, University of Miami, Coral Gables, FL, USA.
Coordinated regulation of intracellular pH by two glucose-sensing pathways in yeast
The yeast Saccharomyces cerevisiae employs multiple pathways to coordinate sugar availability and metabolism. Glucose and other sugars are detected by a G protein–coupled receptor, Gpr1, as well as a pair of transporter-like proteins, Rgt2 and Snf3. When glucose is limiting, however, an ATP-driven proton pump (Pma1) is inactivated, leading to a marked decrease in cytoplasmic pH. Here we determine the relative contribution of the two sugar-sensing pathways to pH regulation.
Coordinated Regulation of Intracellular pH by Two Glucose Sensing Pathways in Yeast
The yeast Saccharomyces cerevisiae employs multiple pathways to coordinate sugar availability and metabolism. Glucose and other sugars are detected by a G protein coupled receptor, Gpr1, as well as a pair of transporter-like proteins, Rgt2 and Snf3. When glucose is limiting however, an ATP-driven proton pump (Pma1) is inactivated leading to a marked decrease in cytoplasmic pH. Here we determine the relative contribution of the two sugar sensing pathways to pH regulation.
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