Probing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy

Martin Gustavsson, Nathaniel Traaseth, Gianluigi Veglia

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish (US)
Pages (from-to)146-153
Number of pages8
JournalBBA - Biomembranes
Volume1818
Issue number2
DOIs
StatePublished - Feb 2012

Fingerprint

Magic angle spinning
Lipid Bilayers
Micelles
Membrane Lipids
Excited states
Ground state
Nuclear magnetic resonance spectroscopy
Membrane Proteins
Lipid bilayers
Magnetic Resonance Spectroscopy
Sarcoplasmic Reticulum Calcium-Transporting ATPases
Allosteric Regulation
Membranes
Sarcoplasmic Reticulum
Detergents
Calcium
Chemical analysis
Nuclear magnetic resonance
Kinetics
phospholamban

Keywords

  • Excited states
  • Lipid bilayers
  • Magic angle spinning
  • Membrane protein
  • NMR
  • Phospholamban

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Biophysics

Cite this

Probing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy. / Gustavsson, Martin; Traaseth, Nathaniel; Veglia, Gianluigi.

In: BBA - Biomembranes, Vol. 1818, No. 2, 02.2012, p. 146-153.

Research output: Contribution to journalArticle

@article{7ed6dcb413334f34940a014ea14f2594,
title = "Probing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy",
abstract = "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.",
keywords = "Excited states, Lipid bilayers, Magic angle spinning, Membrane protein, NMR, Phospholamban",
author = "Martin Gustavsson and Nathaniel Traaseth and Gianluigi Veglia",
year = "2012",
month = "2",
doi = "10.1016/j.bbamem.2011.07.040",
language = "English (US)",
volume = "1818",
pages = "146--153",
journal = "Biochimica et Biophysica Acta - Biomembranes",
issn = "0005-2736",
publisher = "Elsevier",
number = "2",

}

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

AU - Veglia, Gianluigi

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 - Excited states

KW - Lipid bilayers

KW - Magic angle spinning

KW - Membrane protein

KW - NMR

KW - Phospholamban

UR - http://www.scopus.com/inward/record.url?scp=81855192140&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=81855192140&partnerID=8YFLogxK

U2 - 10.1016/j.bbamem.2011.07.040

DO - 10.1016/j.bbamem.2011.07.040

M3 - Article

C2 - 21839724

AN - SCOPUS:81855192140

VL - 1818

SP - 146

EP - 153

JO - Biochimica et Biophysica Acta - Biomembranes

JF - Biochimica et Biophysica Acta - Biomembranes

SN - 0005-2736

IS - 2

ER -