philip yeagle

In 2007 he became Dean of the Faculty of Arts & Sciences at Rutgers University Newark. To better understand the activation of rhodopsin, the GPCR responsible for visual transduction, we report studies on the three-dimensional structure for the activated state of this receptor, metarhodopsin II. in peptide fragments. It may therefore be useful to confront the problem by a combination of alternate techniques. It is a critical component of protein... Because of their central role in regulation of cellular function, structure/function relationships for G-protein coupled receptors (GPCR) are of vital importance, yet only recently have sufficient data been obtained to begin mapping those relationships. Yet they play roles in gene exp... New membrane lipid is synthesized and inserted into existing membrane. Philip Yeagle graduated from St. Olaf College (magna cum laude, honors in chemistry) in 1971, including two terms at the University of Cambridge. For example, introduction of most phospholipids to water will lead to the formation of liposomes, multiple layers of concentric bilayers, often referred to as multilamellar vesicles. The fusion of enveloped viruses to target membranes is promoted by certain viral fusion proteins. No high resolution structure has been available for any G protein receptor, a many-membered family of cell surface receptors. The disposition of serines explains receptor kinase specificity. The mechanism by which the hydrophobic peptide Z-D-Phe-L-PheGly inhibits membrane fusion was investigated. The cytoplasmic face of the transmembrane protein, rhodopsin, is made up of one carboxyl terminal and three cytoplasmic loops connecting six of the seven transmembrane helices. Professor Emeritus. A useful unilamellar form of bilayer can be formed by sonicati... Three linked functions connect the two major components of biological membranes, lipids and proteins. He began his faculty career in the School of Medicine, University at Buffalo In 1985 he was a Visiting Scientist at the CSIRO, Australia. Yet most of the lipids of cell membranes are capable of forming lipid bilayers, the fundamental architecture of all biological membranes. The structure of rhodopsin is a subject of intense interest. Integral membrane proteins may be transmembrane (exposed on both sides of the membrane) o... Membranes fundamentally separate compartments. In 1993 and in 2003 he was a visiting professor in the Department of Biochemistry, University of Oxford. Contact Information; Email: philip.yeagle@uconn.edu: Phone: 860-486-6296: Fax: 860-486-4331: Mailing Address: 91 North Eagleville Road, Unit 3125, Storrs, CT 06269-3125 Philip Yeagle. Biological membranes provide the fundamental structure of cells and viruses. The Gram-negative bacterium, Aggregatibacter actinomycetemcomitans, is a common inhabitant of the human upper aerodigestive tract. Since α-helices and turns (helix-turn-helix motif) are stabilized by short-range interactions, and since many membrane proteins Critical Problems of Membrane Protein Structure He moved in 1997 to the Department of Molecular & Cell Biology, University of Connecticut as Head of department. Several studies carried out on this domai... G protein-coupled receptors (GPCRs) are a family of seven transmembrane helical proteins that initiate a cellular response to an environmental signal. A 19 amino acid peptide that corresponds to the carboxyl terminal end of rhodopsin (residues 330-348) and contains these phosphorylation sites was synthesized. These interactions are not independent. Older disks are found at the apical tip of the ROS and are low in membrane cholesterol. The complex behavior of lipids in biological membranes and in lipid bilayers is in part due to the largely two-dimensional world described by the membrane. It can be hypothesized that information about secondary structure—such as h... Activation of G-protein coupled receptors (GPCR) is not yet understood. The lipids of cell membranes are highly varied in structure and support many membrane functions. Disk membranes from the bovine retinal rod outer segments (ROS) were found to fuse with vesicles made of lipids extracted from unbleached ROS disk membranes, using a lipid mixing assay for membrane fusion (relief of self-quenching of R18, octadecylrhodamine B chloride). Fusion between N-methyldioleoylphosphatidylethanolamine (DOPE) large unilamellar vesicles (LUV) and fusion between Sendai virus and N-methyl-DOPE LUV were measured. From the subcellular level of organelles to the supercellular level of cell–cell interactions, membranes provide the structures necessary for biological function and organization. Upon activation by light, rhodopsin is subject to phosphorylation by rhodopsin kinase at serine and threonine residues in the carboxyl terminal region of the protein. Some turns in proteins are stabilized by short range interactions and can behave as small domains. © 2008-2020 ResearchGate GmbH. Court Records found View. The formation of new biological membranes actually begins with the biosynthesis and insertion into existing membranes of newly synthesized lipid and protein components. Passive transport does not require cellular energy to occur. The membranes of cells undergo a process called membrane fusion when intracellular transport vesicles form and when enveloped viruses infect cells. Newly synthesized lipid components must be inserted into membranes and placed on the proper side of the membrane (reflecting the known membrane asymmetry of membrane lipid across ma... Polar lipids and membrane proteins are major components of biological membranes, both cell membranes and membranes of enveloped viruses. The biologically active carboxy-terminal peptide of the G-protein receptor, rhodopsin, forms a compact structure, suggesting that it is a structural domain in this integral membrane protein. This domain is roughly perpendicular to the transmembrane bundle in the presence of an interface and may be a loop-like structure in the absence of an interface. The plasma membrane vesicles were labeled with the fluorescent probe octadecylrhodamine B chloride (R18) to a level at which the R18 fluorescence was self-quenched. However, many other proteins and peptides stabilize bilayer membranes and inhibit membrane fusion. The enzymes for the last steps of synthesis are located at the endoplasmic reticulum. Once activated by an extracellular signal, GPCRs trigger the intracellular signal transduction cascade by activating a heterotrimeric G protein. The membranes of living cells support much of the functionality of biology. No high-resolution structure exists for any member of this family due to the insolubility of membrane proteins and the difficulty in crystallizing membrane proteins. A 'read' is counted each time someone views a publication summary (such as the title, abstract, and list of authors), clicks on a figure, or views or downloads the full-text. Philip is related to David A Yeagle and James A Yeagle as well as 1 additional person. As part of an alternative approach to determine of membrane protein structure, we are pursuing the structure of cytoplasmic domains of this G-protein receptor. Here’s how. Rhodopsin is one of the most extensively investigated members of this family because for many years it was the only G-protein receptor that could be isolated... Low resolution electron density maps have revealed the general orientation of the transmembrane helices of rhodopsin. It was the first GPCR to be obtained in quantity and studied in detail. Also in 2014, he returned to the University of Connecticut as Professor Emeritus. In 1988 he developed the first in a series of FASEB Summer Research Conferences on membrane structure. Interim Chancellor and Dean of Arts & Sciences, Universidad del País Vasco / Euskal Herriko Unibertsitatea, University at Buffalo, The State University of New York, Department of Cell Stress Biology; Department of Physiology and Biophysics Jacobs School of Medicine and Biomedical Sciences, Watch dogs: Scientific integrity at Science Advances, Non-covalent binding of membrane lipids to membrane proteins, Aggregatibacter actinomycetemcomitans leukotoxin cytotoxicity occurs through bilayer destabilization, Introduction to lipid-protein interactions in biological membranes, The structure of biological membranes: Third edition, The determination of rhodopsin structure may require alternative approaches, Membrane Protein Fragments Reveal Both Secondary and Tertiary Structure of Membrane Proteins, A Small Subset of Signal Peptidase Residues are Perturbed by Signal Peptide Binding, Solution NMR of signal peptidase, a membrane protein, Calcium dependent association of calmodulin with the C‐terminal domain of the tetraspanin protein peripherin/rds, Peripherin-2: An Intracellular Analogy to Viral Fusion Proteins †, Calcium-Dependent Association of Calmodulin with the C-Terminal Domain of the Tetraspanin Protein Peripherin/rds †, Transmembrane helices of membrane proteins may flex to satisfy hydrophobic mismatch, The Tetraspanin Protein Peripherin-2 Forms a Complex with Melanoregulin, a Putative Membrane Fusion Regulator †, Asymmetric Stability among the Transmembrane Helices of Lactose Permease †, Insight into Membrane Protein Structure from High-Resolution NMR, Erratum: Molecular dynamics simulations of retinal in rhodopsin: From the dark-adapted state towards lumirhodopsin (Biochemistry (September 27, 2005) 44, 38 (12667-12680)), Molecular Dynamics Simulations of Retinal in Rhodopsin: From the Dark-Adapted State towards Lumirhodopsin, Stability of Loops in the Structure of Lactose Permease †, The Roles of Cholesterol in the Biology of Cells, The Structures of G-Protein Coupled Receptors, Structural studies of the putative helix 8 in the human β2 adrenergic receptor: An NMR study, A Conformational Trigger for Activation of a G Protein by a G Protein-Coupled Receptor †, Structural Studies of Metarhodopsin II, the Activated Form of the G-Protein Coupled Receptor, Rhodopsin †, Structures of the transmembrane helices of the G‐protein coupled receptor, rhodopsin, Structures of the intradiskal loops and amino terminus of the G‐protein receptor, rhodopsin, Use of nuclear magnetic resonance to study the three-dimensional structure of rhodopsin, Phosphorylation alters the three dimensional structure of the carboxyl terminal of bovine rhodopsin, Studies on the Structure of the G-Protein-Coupled Receptor Rhodopsin Including the Putative G-Protein Binding Site in Unactivated and Activated Forms †, Assembly of a Polytopic Membrane Protein Structure from the Solution Structures of Overlapping Peptide Fragments of Bacteriorhodopsin, Structures of the transmembrane helices of the G-protein coupled receptor, rhodopsin, Structure of bacteriorhodopsin by nuclear magnetic resonance spectroscopy, An alternative approach to membrane protein structure using NMR, Three dimensional structure of the seventh transmembrane helical domain of the G-protein receptor, rhodopsin, Structures of the intradiskal loops and amino terminus of the G-protein receptor, rhodopsin, Solution structure of the loops of bacteriorhodopsin closely resemble the crystal structure, [8] Domain approach to three-dimensional structure of rhodopsin using high-resolution nuclear magnetic resonance, Structural aspects of the G-protein receptor, rhodopsin, Solution structure of the sixth transmembrane helix of the G-protein-coupled receptor, rhodopsin, Solution structure of the sixth transmembrane helix of the G-protein-coupled receptor, rhodopsin 1 1 This work was supported by National Institutes of Health Grant EY03328 and in part by CA16056, Altering the state of phosphorylation of rat liver keratin intermediate filaments by ethanol treatment in vivo changes their structure, Effects of phosphorylation on the structure of the G-protein receptor rhodopsin, Structure of the G-protein-coupled receptor, rhodopsin: A domain approach, A distance measurement between specific sites on the cytoplasmic surface of bovine rhodopsin in rod outer segment disk membranes, Three-Dimensional Structure of the Cytoplasmic Face of the G Protein Receptor Rhodopsin †, The First and Second Cytoplasmic Loops of the G-Protein Receptor, Rhodopsin, Independently Form β-Turns †, Structure determination of the fourth cytoplasmic loop and carboxyl terminal domain in bovine rhodopsin, The three dimensional structure of the cytoplasmic face of the G protein receptor, rhodopsin, and its interaction with the G protein, transducin, Rhodopsin-cholesterol interactions in bovine rod outer segment disk membranes, Differential membrane protein phosphorylation in bovine retinal rod outer segment disk membranes as a function of disk age, Structure of the cytoplasmic surface of bovine rhodopsin, Site-specificity of ethanol-induced dephosphorylation of rat hepatocyte keratins 8 and 18: A31P NMR study, Structure of the third cytoplasmic loop of bovine rhodopsin, Structure of the carboxy-terminal domain of bovine rhodopsin, THE DETERMINATION OF RHODOPSIN STRUCTURE MAY REQUIRE ALTERNATIVE APPROACHES, A study of carbobenzoxy-D-phenylalanine-L-phenylalanine-glycine, an inhibitor of membrane fusion, in phospholipid bilayers with multinuclear magnetic resonance, Lipids and Lipid-Intermediate Structures in the Fusion of Biological Membranes, Diacylglycerol and hexadecane increase divalent cation-induced lipid mixing rates between phosphatidylserine large unilamellar vesicles, Inhibition of Membrane Fusion by Lysophosphatidylcholine, Effect of cholesterol on retinal rod outer segment disk membranes, The antiviral peptide carbobenzoxy-D-phenylalanyl-L-phenylalanylglycine changes the average conformation of phospholipids in membranes, Structural requirements for the inhibition of membrane-fusion by carbobenzoxy-D-Phe-Phe-Gly, Phosphorus-31 nuclear magnetic resonance in membrane fusion studies, USING LOW-PRESSURE EXTRUDED LIPOSOMES IN THE LABORATORY, The biophysics and cell biology of cholesterol: an hypothesis for the essential role of cholesterol in mammalian cells, Retinal and retinol promote membrane fusion, Book Review:Membrane Fusion.