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The sarcolipin-bound calcium pump stabilizes calcium sites exposed to the cytoplasm

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  • Anne-Marie L. Winther

    (Pcovery, Thorvaldsensvej 57, DK-1871 Frederiksberg, Denmark
    Centre for Membrane Pumps in Cells and Disease—PUMPkin, Danish National Research Foundation
    Aarhus University, Gustav Wieds Vej 10C, DK-8000 Aarhus, Denmark)

  • Maike Bublitz

    (Centre for Membrane Pumps in Cells and Disease—PUMPkin, Danish National Research Foundation
    Aarhus University, Gustav Wieds Vej 10C, DK-8000 Aarhus, Denmark)

  • Jesper L. Karlsen

    (Centre for Membrane Pumps in Cells and Disease—PUMPkin, Danish National Research Foundation
    Aarhus University, Gustav Wieds Vej 10C, DK-8000 Aarhus, Denmark)

  • Jesper V. Møller

    (Centre for Membrane Pumps in Cells and Disease—PUMPkin, Danish National Research Foundation
    Aarhus University, Ole Worms Allé 6, DK-8000 Aarhus, Denmark)

  • John B. Hansen

    (Pcovery, Thorvaldsensvej 57, DK-1871 Frederiksberg, Denmark)

  • Poul Nissen

    (Centre for Membrane Pumps in Cells and Disease—PUMPkin, Danish National Research Foundation
    Aarhus University, Gustav Wieds Vej 10C, DK-8000 Aarhus, Denmark)

  • Morten J. Buch-Pedersen

    (Pcovery, Thorvaldsensvej 57, DK-1871 Frederiksberg, Denmark)

Abstract

An X-ray crystal structure of sarcoplasmic reticulum Ca2+-ATPase (SERCA) in the presence of sarcolipin, a SERCA regulator, is presented; the structure shows that sarcolipin traps SERCA in a previously unidentified ‘open’ state in which its high-affinity Ca2+-binding sites are unoccupied, but accessible from the cytoplasm.

Suggested Citation

  • Anne-Marie L. Winther & Maike Bublitz & Jesper L. Karlsen & Jesper V. Møller & John B. Hansen & Poul Nissen & Morten J. Buch-Pedersen, 2013. "The sarcolipin-bound calcium pump stabilizes calcium sites exposed to the cytoplasm," Nature, Nature, vol. 495(7440), pages 265-269, March.
    • Handle: RePEc:nat:nature:v:495:y:2013:i:7440:d:10.1038_nature11900
    DOI: 10.1038/nature11900
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    Cited by:

    1. Yingying Guo & Yuanyuan Zhang & Renhong Yan & Bangdong Huang & Fangfei Ye & Liushu Wu & Ximin Chi & Yi shi & Qiang Zhou, 2022. "Cryo-EM structures of recombinant human sodium-potassium pump determined in three different states," Nature Communications, Nature, vol. 13(1), pages 1-9, December.
    2. Zongxin Guo & Fredrik Orädd & Viktoria Bågenholm & Christina Grønberg & Jian Feng Ma & Peter Ott & Yong Wang & Magnus Andersson & Per Amstrup Pedersen & Kaituo Wang & Pontus Gourdon, 2024. "Diverse roles of the metal binding domains and transport mechanism of copper transporting P-type ATPases," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    3. Nina Salustros & Christina Grønberg & Nisansala S. Abeyrathna & Pin Lyu & Fredrik Orädd & Kaituo Wang & Magnus Andersson & Gabriele Meloni & Pontus Gourdon, 2022. "Structural basis of ion uptake in copper-transporting P1B-type ATPases," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    4. Ping Li & Viktoria Bågenholm & Per Hägglund & Karin Lindkvist-Petersson & Kaituo Wang & Pontus Gourdon, 2024. "The structure and function of P5A-ATPases," Nature Communications, Nature, vol. 15(1), pages 1-15, December.

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