Oliver P. Ernst

Oliver P. Ernst

Professor

Address MSB, Room 5316A
1 King's College Circle
Toronto, ON M5S 1A8
Lab Ernst Lab
Lab Phone 416-978-3852
Office Phone 416-978-3849
Email oliver.ernst@utoronto.ca

Research Description

Transmembrane Signaling by GPCRs

Cell membranes are natural borders for signal transduction between cells and their environment. Different strategies to enable signals to cross the membrane barrier employ protein classes such as G protein-coupled receptors (GPCRs), ion channels, and transporters. Our research is directed at understanding transmembrane signaling by GPCRs. We investigate the inner workings of these proteins and their interaction with signaling proteins like G proteins and arrestins. Using different spectroscopic techniques and X-ray crystallography, we aim to get insight into the mechanism, specificity and structural basis of these interactions. A focus of our work is on rhodopsin, the photoreceptor protein in the vertebrate retina. The knowledge how GPCRs work on a molecular level will help to understand their role in health and disease.

Publications

View all publications on PubMed

Genetically Encoded Quinone Methides Enabling Rapid, Site-Specific, and Photocontrolled Protein Modification with Amine Reagents
Liu et al.
JACS (2020) 142:17057-17068.  Read

The crystal structures of a chloride-pumping microbial rhodopsin and its proton-pumping mutant illuminate proton transfer determinants
Besaw et al.
JBC (2020) 295:14793-14804  Read

Cryo-EM structure of the native rhodopsin dimer in nanodiscs
Zhao et al.
JBC (2019) 294:14215-14230  Read

Stationary Phase EPR Spectroscopy for Monitoring Membrane Protein Refolding by Conformational Response
Balo et al.
Analytical Chemistry (2019) 91:1071-1079  Read

Cryo-EM structure of human rhodopsin bound to an inhibitory G protein
Kang et al.
Nature (2018) 558:553-558  Read

Mechanistic insights into allosteric regulation of the A2A adenosine G protein-coupled receptor by physiological cations
Ye et al.
Nature Communications (2018) 9:1372.  Read

Gi- and Gs-coupled GPCRs show different modes of G-protein binding
Van Eps et al.
PNAS (2018) 115:2383-2388.  Read

High-throughput in situ X-ray screening of and data collection from protein crystals at room temperature and under cryogenic conditions
Broecker et al.
Nature Protocols (2018) 13:260-92.  Read

Structure of the glucagon receptor in complex with a glucagon analogue
Zhang et al.
Nature (2018) 553:106-10.  Read

Accessible virtual reality of biomolecular structural models using the Autodesk Molecule Viewer
Balo et al.
Nature Methods (2017) 14:1122-3.  Read

Identification of Phosphorylation Codes for Arrestin Recruitment by G Protein-Coupled Receptors
Zhou et al.
Cell (2017) 170:457-69.  Read

Molecular assembly of rhodopsin with G protein-coupled receptor kinases
He et al.
Cell Research (2017) 27:728-47.  Read

Conformational equilibria of light-activated rhodopsin in nanodiscs
Van Eps et al.
PNAS (2017) 114:E3268-75.  Read

Crystallogenesis of Membrane Proteins Mediated by Polymer-Bounded Lipid Nanodiscs
Broecker et al.
Structure (2017) 25:384-92.  Read

Dimerization deficiency of enigmatic retinitis pigmentosa-linked rhodopsin mutants
Ploier et al.
Nature Communications (2016) 7:12832.  Read

Activation of the A2A adenosine G-protein-coupled receptor by conformational selection
Ye et al.
Nature (2016) 533:265-8.  Read

Local vibrational coherences drive the primary photochemistry of vision
Johnson et al.
Nature Chemistry (2015) 7:980-6.  Read

Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser
Kang et al.
Nature (2015) 523:561-7.  Read

Constitutive phospholipid scramblase activity of a G protein-coupled receptor
Goren et al.
Nature Communication (2014) 5:5115.  Read

Microbial and animal rhodopsins: structures, functions, and molecular mechanisms
Ernst et al.
Chemical Reviews (2014) 114:126-63.  Read

Opsin, a structural model for olfactory receptors?
Park et al.
Angew Chem Int Ed Engl (2013) 52:11021-4.  Read

Crystal structure of pre-activated arrestin p44
Kim et al.
Nature (2013) 497:142-6.  Read