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Functional and Structural Insights into Sarcolipin, a Regulator of the Sarco-Endoplasmic Reticulum Ca2+-ATPases

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Regulation of Ca2+-ATPases,V-ATPases and F-ATPases

Part of the book series: Advances in Biochemistry in Health and Disease ((ABHD,volume 14))

Abstract

Sarcolipin (SLN), a transmembrane peptide from sarcoplasmic reticulum, is one of the major proteins involved in the muscle contraction/relaxation process. A number of enzymological studies have underlined its regulatory role in connection with the SERCA1a activity. Indeed, SLN folds as a unique transmembrane helix and binds to SERCA1a in a groove close to transmembrane helices M2, M6, and M9, as proposed initially by cross-linking experiments and recently detailed in the 3D structures of the SLN–Ca2+-ATPase complex. In addition, association of SLN with SERCAs may depend on its phosphorylation. SLN possesses a peculiar C-terminus (RSYQY) critical for the regulation of the ATPases. This luminal tail appears to be essential for addressing SLN to the ER membrane. Moreover, we recently demonstrated that some SLN isoforms are acylated on cysteine 9, a feature which remained unnoticed so far even in the recent crystal structures of the SLN–SERCA1a complex. The removal of the fatty acid chain was shown to increase the activity of the membrane-embedded Ca2+-ATPase by about 20 %. The exact functional and structural role of this post-translational modification is presently unknown. Recent data are in favor of a key regulator role of SLN in muscle-based thermogenesis in mammals. The possible link of SLN to heat production could occur through an uncoupling of the SERCA1a-mediated ATP hydrolysis from calcium transport. Considering those particular features and the fact that SLN is not expressed at the same level in different tissues, the role of SLN and its exact mechanism of regulation remain sources of interrogation.

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Abbreviations

SRER:

Sarco-endoplasmic reticulumEndoplasmic reticulum

ER:

Endoplasmic reticulum

SERCA1a or 2a:

Sarco-Endoplasmic Reticulum Ca2+-ATPase isoform 1a or 2a

SLN:

Sarcolipin

hSLN:

Human isoform of SLN

rSLN:

Rabbit isoform of SLN

mSLN:

Mouse isoform of SLN

PLN:

Phospholamban

DDM:

n-Dodecyl-β-d-maltopyranoside

C12E8 :

Octaethylene glycol monododecyl ether

DOC:

Deoxycholate

SDS:

Sodium dodecyl sulfate

DPC:

n-Dodecylphosphocholine or Fos-choline-12

SEC:

Size exclusion chromatography

MS:

Mass spectrometry

MALDI-TOF:

Matrix-assisted laser desorption ionization—time of flight

NMR:

Nuclear magnetic resonance

ssNMR:

Solid state nuclear magnetic resonance

MD:

Molecular dynamics

POPC:

1-Palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine

DOPC:

1,2-Dioleoyl-sn-glycero-3-phosphocholine

DOPE:

1,2-Dioleoyl-sn-glycero-3-phosphoethanolamine

EYPC:

Egg yolk phosphatidylcholine

EYPA:

Egg yolk phosphatic acid

RyR:

Ryanodine Receptor

FCCP:

Carbonyl cyanide-p-trifluoromethoxyphenylhydrazone

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Acknowledgments

This work was supported by the French Infrastructure for Integrated Structural Biology (FRISBI) and by grants from the Agence Nationale pour la Recherche and the Ile de France region (Domaine d’Intérêt Majeur Maladies Infectieuses, DIM MALINF).

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Authors and Affiliations

  1. Institute for Integrative Biology of the Cell (I2BC), Commissariat à l’Energie Atomique et aux Energies Alternatives (CEA), Centre National de la Recherche Scientifique (CNRS), Université Paris-Sud, iBiTec-S/SB2SM/Laboratoire des Protéines et Systèmes Membranaires, CEA-Saclay, 91191, Gif-sur-Yvette CEDEX, France

    Thomas Barbot, Cédric Montigny, Marc le Maire, Christine Jaxel, Nadège Jamin & Veronica Beswick

  2. Pharmacologie et biochimie de la synapse, Neuro PSI, UMR9197, CNRS, Université Paris-Sud, 91405, Orsay CEDEX, France

    Paulette Decottignies

  3. Physics Department, Université d’Evry-Val-d’Essonne, 91025, Evry CEDEX, France

    Veronica Beswick

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  1. Thomas Barbot
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  2. Cédric Montigny
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Correspondence to Veronica Beswick .

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  1. Biochemistry and Biophysics, University of Kalyani, Kalyani, West Bengal, India

    Sajal Chakraborti

  2. University of Manitoba, Institute of Cardiovascular Science St. Boniface Hospital Research, Winnipeg, Manitoba, Canada

    Naranjan S Dhalla

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Barbot, T. et al. (2016). Functional and Structural Insights into Sarcolipin, a Regulator of the Sarco-Endoplasmic Reticulum Ca2+-ATPases. In: Chakraborti, S., Dhalla, N. (eds) Regulation of Ca2+-ATPases,V-ATPases and F-ATPases. Advances in Biochemistry in Health and Disease, vol 14. Springer, Cham. https://doi.org/10.1007/978-3-319-24780-9_10

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