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Ion Pathways in the Sarcoplasmic Reticulum Ca2+-ATPase

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Ion Pathways in the Sarcoplasmic Reticulum Ca2+-ATPase. / Bublitz, Maike; Musgaard, Maria; Poulsen, Hanne; Thøgersen, Lea; Olesen, Claus; Schiøtt, Birgit; Morth, Preben; Møller, Jesper V; Nissen, Poul.

In: Journal of Biological Chemistry, Vol. 288, 12.04.2013, p. 10759-10765.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Bublitz, M, Musgaard, M, Poulsen, H, Thøgersen, L, Olesen, C, Schiøtt, B, Morth, P, Møller, JV & Nissen, P 2013, 'Ion Pathways in the Sarcoplasmic Reticulum Ca2+-ATPase', Journal of Biological Chemistry, vol. 288, pp. 10759-10765. https://doi.org/10.1074/jbc.R112.436550

APA

Bublitz, M., Musgaard, M., Poulsen, H., Thøgersen, L., Olesen, C., Schiøtt, B., Morth, P., Møller, J. V., & Nissen, P. (2013). Ion Pathways in the Sarcoplasmic Reticulum Ca2+-ATPase. Journal of Biological Chemistry, 288, 10759-10765. https://doi.org/10.1074/jbc.R112.436550

CBE

Bublitz M, Musgaard M, Poulsen H, Thøgersen L, Olesen C, Schiøtt B, Morth P, Møller JV, Nissen P. 2013. Ion Pathways in the Sarcoplasmic Reticulum Ca2+-ATPase. Journal of Biological Chemistry. 288:10759-10765. https://doi.org/10.1074/jbc.R112.436550

MLA

Bublitz, Maike et al. "Ion Pathways in the Sarcoplasmic Reticulum Ca2+-ATPase". Journal of Biological Chemistry. 2013, 288. 10759-10765. https://doi.org/10.1074/jbc.R112.436550

Vancouver

Bublitz M, Musgaard M, Poulsen H, Thøgersen L, Olesen C, Schiøtt B et al. Ion Pathways in the Sarcoplasmic Reticulum Ca2+-ATPase. Journal of Biological Chemistry. 2013 Apr 12;288:10759-10765. https://doi.org/10.1074/jbc.R112.436550

Author

Bublitz, Maike ; Musgaard, Maria ; Poulsen, Hanne ; Thøgersen, Lea ; Olesen, Claus ; Schiøtt, Birgit ; Morth, Preben ; Møller, Jesper V ; Nissen, Poul. / Ion Pathways in the Sarcoplasmic Reticulum Ca2+-ATPase. In: Journal of Biological Chemistry. 2013 ; Vol. 288. pp. 10759-10765.

Bibtex

@article{d35a4cbdc8af4eb99a3ee555b6b211da,
title = "Ion Pathways in the Sarcoplasmic Reticulum Ca2+-ATPase",
abstract = "The sarco(endo)plasmic reticulum Ca2+- ATPase (SERCA) is a transmembrane ion transporter belonging to the PII-type ATPases. It performs the vital task of re-sequestering cytoplasmic Ca2+ to the sarco-endoplasmic reticulum store, thereby also terminating Ca2+-induced signaling such as in muscle contraction. This article focuses on the transport pathways of Ca2+ and H+ ions across the lipid bilayer through SERCA. The ion binding sites of SERCA are accessible from either the cytoplasm or the SR/ER lumen at a time, and the Ca2+ entry and exit channels are both formed mainly by rearrangements of four N-terminal transmembrane (TM) alpha-helices. Recent improvements in the resolution of the crystal structures of rabbit SERCA1a have revealed a hydrated pathway in the Cterminal TM region leading from the ion binding sites to the cytosol. A comparison of different SERCA conformations reveals that this C-terminal pathway is exclusive to Ca2+- free E2-states, suggesting that it may play a functional role in proton release from the ion binding sites. This is in agreement with molecular dynamics (MD) simulations, mutational studies, and in striking analogy to a similar pathway recently described for the related sodium pump. We therefore suggest a model for the ion exchange mechanism in PII-ATPases including not only one, but two cytoplasmic pathways working in concert.",
author = "Maike Bublitz and Maria Musgaard and Hanne Poulsen and Lea Th{\o}gersen and Claus Olesen and Birgit Schi{\o}tt and Preben Morth and M{\o}ller, {Jesper V} and Poul Nissen",
year = "2013",
month = apr,
day = "12",
doi = "10.1074/jbc.R112.436550",
language = "English",
volume = "288",
pages = "10759--10765",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",

}

RIS

TY - JOUR

T1 - Ion Pathways in the Sarcoplasmic Reticulum Ca2+-ATPase

AU - Bublitz, Maike

AU - Musgaard, Maria

AU - Poulsen, Hanne

AU - Thøgersen, Lea

AU - Olesen, Claus

AU - Schiøtt, Birgit

AU - Morth, Preben

AU - Møller, Jesper V

AU - Nissen, Poul

PY - 2013/4/12

Y1 - 2013/4/12

N2 - The sarco(endo)plasmic reticulum Ca2+- ATPase (SERCA) is a transmembrane ion transporter belonging to the PII-type ATPases. It performs the vital task of re-sequestering cytoplasmic Ca2+ to the sarco-endoplasmic reticulum store, thereby also terminating Ca2+-induced signaling such as in muscle contraction. This article focuses on the transport pathways of Ca2+ and H+ ions across the lipid bilayer through SERCA. The ion binding sites of SERCA are accessible from either the cytoplasm or the SR/ER lumen at a time, and the Ca2+ entry and exit channels are both formed mainly by rearrangements of four N-terminal transmembrane (TM) alpha-helices. Recent improvements in the resolution of the crystal structures of rabbit SERCA1a have revealed a hydrated pathway in the Cterminal TM region leading from the ion binding sites to the cytosol. A comparison of different SERCA conformations reveals that this C-terminal pathway is exclusive to Ca2+- free E2-states, suggesting that it may play a functional role in proton release from the ion binding sites. This is in agreement with molecular dynamics (MD) simulations, mutational studies, and in striking analogy to a similar pathway recently described for the related sodium pump. We therefore suggest a model for the ion exchange mechanism in PII-ATPases including not only one, but two cytoplasmic pathways working in concert.

AB - The sarco(endo)plasmic reticulum Ca2+- ATPase (SERCA) is a transmembrane ion transporter belonging to the PII-type ATPases. It performs the vital task of re-sequestering cytoplasmic Ca2+ to the sarco-endoplasmic reticulum store, thereby also terminating Ca2+-induced signaling such as in muscle contraction. This article focuses on the transport pathways of Ca2+ and H+ ions across the lipid bilayer through SERCA. The ion binding sites of SERCA are accessible from either the cytoplasm or the SR/ER lumen at a time, and the Ca2+ entry and exit channels are both formed mainly by rearrangements of four N-terminal transmembrane (TM) alpha-helices. Recent improvements in the resolution of the crystal structures of rabbit SERCA1a have revealed a hydrated pathway in the Cterminal TM region leading from the ion binding sites to the cytosol. A comparison of different SERCA conformations reveals that this C-terminal pathway is exclusive to Ca2+- free E2-states, suggesting that it may play a functional role in proton release from the ion binding sites. This is in agreement with molecular dynamics (MD) simulations, mutational studies, and in striking analogy to a similar pathway recently described for the related sodium pump. We therefore suggest a model for the ion exchange mechanism in PII-ATPases including not only one, but two cytoplasmic pathways working in concert.

U2 - 10.1074/jbc.R112.436550

DO - 10.1074/jbc.R112.436550

M3 - Journal article

C2 - 23400778

VL - 288

SP - 10759

EP - 10765

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

ER -