Publication date: April 2018 Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volume 105
Author(s): Binyong Liang, Lukas K. Tamm
SNARE-mediated membrane fusion is a ubiquitous process responsible for intracellular vesicle trafficking, including membrane fusion in exocytosis that leads to hormone and neurotransmitter release. The proteins that facilitate this process are highly dynamic and adopt multiple conformations when they interact with other proteins and lipids as they form highly regulated molecular machines that operate on membranes. Solution NMR is an ideal method to capture high-resolution glimpses of the molecular transformations that take place when these proteins come together and work on membranes. Since solution NMR has limitations on the size of proteins and complexes that can be studied, lipid bilayer model membranes cannot be used in these approaches, so the relevant interactions are typically studied in various types of membrane-mimetics that are tractable by solution NMR methods. In this review we therefore first summarize different membrane-mimetic systems that are commonly used or that show promise for solution NMR studies of membrane-interacting proteins. We then summarize recent NMR studies on two SNARE proteins, syntaxin and synaptobrevin, and two related regulatory proteins, complexin and ?-synuclein, and their interactions with membrane lipids. These studies provide a structural and dynamical framework for how these proteins might carry out their functions in the vicinity of lipid membranes. The common theme throughout these studies is that membrane interactions have major influences on the structural dynamics of these proteins that cannot be ignored when attempting to explain their functions in contemporary models of SNARE-mediated membrane fusion. Graphical abstract
[NMR paper] Solution NMR of SNAREs, complexin and ?-synuclein in association with membrane-mimetics.
Solution NMR of SNAREs, complexin and ?-synuclein in association with membrane-mimetics.
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Prog Nucl Magn Reson Spectrosc. 2018 Apr;105:41-53
Authors: Liang B, Tamm LK
Abstract
SNARE-mediated membrane fusion is a ubiquitous process responsible for intracellular vesicle trafficking, including membrane fusion in exocytosis that leads to hormone and neurotransmitter release. The proteins that facilitate this process are highly...
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03-20-2018 10:11 PM
[NMR paper] Micelles, Bicelles, and Nanodiscs: Comparing the Impact of Membrane Mimetics on Membrane Protein Backbone Dynamics
Micelles, Bicelles, and Nanodiscs: Comparing the Impact of Membrane Mimetics on Membrane Protein Backbone Dynamics
Detergents are often used to investigate the structure and dynamics of membrane proteins. Whereas the structural integrity seems to be preserved in detergents for many membrane proteins, their functional activity is frequently compromised, but can be restored in a lipid environment. Herein we show with per-residue resolution that while OmpX forms a stable ?-barrel in DPC detergent micelles, DHPC/DMPC bicelles, and DMPC nanodiscs, the pico- to nanosecond and micro- to...
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[NMR paper] Effects of Membrane Mimetics on Cytochrome P450-Cytochrome b5 Interactions Characterized by NMR Spectroscopy.
Effects of Membrane Mimetics on Cytochrome P450-Cytochrome b5 Interactions Characterized by NMR Spectroscopy.
Effects of Membrane Mimetics on Cytochrome P450-Cytochrome b5 Interactions Characterized by NMR Spectroscopy.
J Biol Chem. 2015 Mar 20;
Authors: Zhang M, Huang R, Im SC, Waskell L, Ramamoorthy A
Abstract
Mammalian cytochrome P450 (P450) is a membrane-bound monooxygenase whose catalytic activities require two electrons to be sequentially delivered from its redox partners: cytochrome b5 (cytb5) and cytochrome P450...
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03-22-2015 06:36 PM
[NMR paper] Characterization of the insertase BamA in three different membrane mimetics by solution NMR spectroscopy.
Characterization of the insertase BamA in three different membrane mimetics by solution NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Characterization of the insertase BamA in three different membrane mimetics by solution NMR spectroscopy.
J Biomol NMR. 2015 Feb 1;
Authors: Morgado L, Zeth K, Burmann BM, Maier T, Hiller S
Abstract
The insertase BamA is the central protein of the Bam complex responsible for...
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Characterization of the insertase BamA in three different membrane mimetics by solution NMR spectroscopy
Characterization of the insertase BamA in three different membrane mimetics by solution NMR spectroscopy
Abstract
The insertase BamA is the central protein of the Bam complex responsible for outer membrane protein biogenesis in Gram-negative bacteria. BamA features a 16-stranded transmembrane β-barrel and five periplasmic POTRA domains, with a total molecular weight of 88Â*kDa. Whereas the structure of BamA has recently been determined by X-ray crystallography, its functional mechanism is not well understood. This mechanism comprises the insertion of...
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[NMR paper] Ca(2+) modulating ?-synuclein membrane transient interactions revealed by solution NMR spectroscopy.
Ca(2+) modulating ?-synuclein membrane transient interactions revealed by solution NMR spectroscopy.
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Authors: Zhang Z, Dai C, Bai J, Xu G, Liu M, Li C
Abstract
?-synuclein is involved in Parkinson's disease and its interaction with cell membrane is crucial to its pathological and physiological functions. Membrane properties, such as curvature, lipid composition have been shown to affect the...
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[NMR paper] Cell-free Expressed Bacteriorhodopsin in Different Soluble Membrane Mimetics: Biophysical Properties and NMR Accessibility.
Cell-free Expressed Bacteriorhodopsin in Different Soluble Membrane Mimetics: Biophysical Properties and NMR Accessibility.
Cell-free Expressed Bacteriorhodopsin in Different Soluble Membrane Mimetics: Biophysical Properties and NMR Accessibility.
Structure. 2013 Feb 12;
Authors: Etzkorn M, Raschle T, Hagn F, Gelev V, Rice AJ, Walz T, Wagner G
Abstract
Selecting a suitable membrane-mimicking environment is of fundamental importance for the investigation of membrane proteins. Nonconventional surfactants, such as amphipathic polymers...
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Choosing membrane mimetics for NMR structural studies of transmembrane proteins.
Choosing membrane mimetics for NMR structural studies of transmembrane proteins.
Choosing membrane mimetics for NMR structural studies of transmembrane proteins.
Biochim Biophys Acta. 2011 Apr 5;
Authors: Warschawski DE, Arnold AA, Beaugrand M, Gravel A, Chartrand E, Marcotte I
The native environment of membrane proteins is complex and scientists have felt the need to simplify it to reduce the number of varying parameters. However, experimental problems can also arise from oversimplification which contributes to why membrane proteins are...
Solution NMR of SNAREs, complexin and ?-synuclein in association with membrane-mimetics
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