Probing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy
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Probing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy. / Gustavsson, Martin; Traaseth, Nathaniel J; Veglia, Gianluigi.
I: Biochimica et biophysica acta, Bind 1818, Nr. 2, 02.2012, s. 146-53.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Probing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy
AU - Gustavsson, Martin
AU - Traaseth, Nathaniel J
AU - Veglia, Gianluigi
N1 - Copyright © 2011 Elsevier B.V. All rights reserved.
PY - 2012/2
Y1 - 2012/2
N2 - In this paper, we analyzed the ground and excited states of phospholamban (PLN), a membrane protein that regulates sarcoplasmic reticulum calcium ATPase (SERCA), in different membrane mimetic environments. Previously, we proposed that the conformational equilibria of PLN are central to SERCA regulation. Here, we show that these equilibria detected in micelles and bicelles are also present in native sarcoplasmic reticulum lipid membranes as probed by MAS solid-state NMR. Importantly, we found that the kinetics of conformational exchange and the extent of ground and excited states in detergent micelles and lipid bilayers are different, revealing a possible role of the membrane composition on the allosteric regulation of SERCA. Since the extent of excited states is directly correlated to SERCA inhibition, these findings open up the exciting possibility that calcium transport in the heart can be controlled by the lipid bilayer composition. This article is part of a Special Issue entitled: Membrane protein structure and function.
AB - In this paper, we analyzed the ground and excited states of phospholamban (PLN), a membrane protein that regulates sarcoplasmic reticulum calcium ATPase (SERCA), in different membrane mimetic environments. Previously, we proposed that the conformational equilibria of PLN are central to SERCA regulation. Here, we show that these equilibria detected in micelles and bicelles are also present in native sarcoplasmic reticulum lipid membranes as probed by MAS solid-state NMR. Importantly, we found that the kinetics of conformational exchange and the extent of ground and excited states in detergent micelles and lipid bilayers are different, revealing a possible role of the membrane composition on the allosteric regulation of SERCA. Since the extent of excited states is directly correlated to SERCA inhibition, these findings open up the exciting possibility that calcium transport in the heart can be controlled by the lipid bilayer composition. This article is part of a Special Issue entitled: Membrane protein structure and function.
KW - Animals
KW - Calcium-Binding Proteins/chemistry
KW - Cell Membrane/chemistry
KW - Kinetics
KW - Magnetic Resonance Spectroscopy/methods
KW - Membrane Lipids/chemistry
KW - Protein Conformation
KW - Protein Structure, Tertiary
KW - Rabbits
KW - Sarcoplasmic Reticulum Calcium-Transporting ATPases/chemistry
U2 - 10.1016/j.bbamem.2011.07.040
DO - 10.1016/j.bbamem.2011.07.040
M3 - Journal article
C2 - 21839724
VL - 1818
SP - 146
EP - 153
JO - Biochimica et biophysica acta
JF - Biochimica et biophysica acta
SN - 0006-3002
IS - 2
ER -
ID: 329436360