14-3-3 binding creates a memory of kinase action by stabilizing the modified state of phospholamban

Author:

Menzel Julia1ORCID,Kownatzki-Danger Daniel2ORCID,Tokar Sergiy3ORCID,Ballone Alice45,Unthan-Fechner Kirsten1,Kilisch Markus1,Lenz Christof67ORCID,Urlaub Henning67,Mori Mattia4,Ottmann Christian5ORCID,Shattock Michael J.3ORCID,Lehnart Stephan E.28ORCID,Schwappach Blanche178ORCID

Affiliation:

1. Department of Molecular Biology, Universitätsmedizin Göttingen, Humboldtallee 23, 37073 Göttingen, Germany.

2. Heart Research Center Göttingen, Department of Cardiology & Pneumology, Universitätsmedizin Göttingen, Robert-Koch-Straße 42a, 37075 Göttingen, Germany.

3. School of Cardiovascular Medicine and Sciences, King’s College London, Westminster Bridge Road, London SE17H, UK.

4. Department of Biotechnology, Chemistry and Pharmacy, Department of Excellence 2018-2022, University of Siena, Via Aldo Moro 2, 53100 Siena, Italy.

5. Laboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Eindhoven University of Technology, P. O. Box 513, 5600MB Eindhoven, Netherlands.

6. Bioanalytics Group, Institute of Clinical Chemistry, University Medical Center Göttingen, Robert-Koch-Straße 40, 37075 Göttingen, Germany

7. Max-Planck Institute for Biophysical Chemistry, Am Faßberg 11, 37077 Göttingen, Germany.

8. Cluster of Excellence “Multiscale Bioimaging: From Molecular Machines to Networks of Excitable Cells” (MBExC), University of Goettingen, Robert-Koch-Straße 40, 37075 Göttingen, Germany.

Abstract

Phosphorylation alters how phospholamban binds to 14-3-3 and affects cardiomyocyte Ca 2+ signaling.

Funder

H2020 Marie Skłodowska-Curie Actions

British Heart Foundation

Deutsche Forschungsgemeinschaft

Fondation Leducq

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Cell Biology,Molecular Biology,Biochemistry

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