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SUMO1-dependent modulation of SERCA2a in heart failure

Author

Listed:
  • Changwon Kho

    (Cardiovascular Research Center, Mount Sinai School of Medicine, 1 Gustave L. Levy Place, Box 1030)

  • Ahyoung Lee

    (Cardiovascular Research Center, Mount Sinai School of Medicine, 1 Gustave L. Levy Place, Box 1030)

  • Dongtak Jeong

    (Cardiovascular Research Center, Mount Sinai School of Medicine, 1 Gustave L. Levy Place, Box 1030)

  • Jae Gyun Oh

    (College of Life Sciences, Gwangju Institute of Science and Technology, 261 Cheomdan-gwagiro, Buk-gu)

  • Antoine H. Chaanine

    (Cardiovascular Research Center, Mount Sinai School of Medicine, 1 Gustave L. Levy Place, Box 1030)

  • Eddy Kizana

    (Westmead Millennium Institute, Westmead Hospital)

  • Woo Jin Park

    (College of Life Sciences, Gwangju Institute of Science and Technology, 261 Cheomdan-gwagiro, Buk-gu)

  • Roger J. Hajjar

    (Cardiovascular Research Center, Mount Sinai School of Medicine, 1 Gustave L. Levy Place, Box 1030)

Abstract

SUMO1 level linked to heart failure SERCA2a is an ATPase responsible for calcium reuptake during excitation contraction coupling. Levels and activity of SERCA2a are decreased in heart failure, and a gene-therapy approach to deliver SERCA2a to failing hearts is being tested in clinical trials. Roger Hajjar and colleagues now show that SUMOylation, the attachment of SUMO (small ubiquitin-like modifier) proteins, is essential for preserving the stability and activity of SERCA2a and that levels of SUMO1 are decreased in failing hearts. They also show in a mouse model of heart failure that gene delivery of SUMO1 can restore heart function to the same degree as delivery of SERCA2a, pointing to SUMO1 as a potential therapeutic candidate for treating heart failure.

Suggested Citation

  • Changwon Kho & Ahyoung Lee & Dongtak Jeong & Jae Gyun Oh & Antoine H. Chaanine & Eddy Kizana & Woo Jin Park & Roger J. Hajjar, 2011. "SUMO1-dependent modulation of SERCA2a in heart failure," Nature, Nature, vol. 477(7366), pages 601-605, September.
    • Handle: RePEc:nat:nature:v:477:y:2011:i:7366:d:10.1038_nature10407
    DOI: 10.1038/nature10407
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    Cited by:

    1. Sangsang Zhu & Chao Quan & Ruizhen Wang & Derong Liang & Shu Su & Ping Rong & Kun Zhou & Xinyu Yang & Qiaoli Chen & Min Li & Qian Du & Jingzi Zhang & Lei Fang & Hong-Yu Wang & Shuai Chen, 2022. "The RalGAPα1–RalA signal module protects cardiac function through regulating calcium homeostasis," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    2. Fabrice Gonnot & Laura Boulogne & Camille Brun & Maya Dia & Yves Gouriou & Gabriel Bidaux & Christophe Chouabe & Claire Crola Da Silva & Sylvie Ducreux & Bruno Pillot & Andrea Kaczmarczyk & Christelle, 2023. "SERCA2 phosphorylation at serine 663 is a key regulator of Ca2+ homeostasis in heart diseases," Nature Communications, Nature, vol. 14(1), pages 1-18, December.

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