14-3-3 proteins inactivate DAPK2 by promoting its dimerization and protecting key regulatory phosphosites

Matej Horvath; Olivia Petrvalska; Petr Herman; Veronika Obsilova; Tomas Obsil

doi:10.1038/s42003-021-02518-y

Communications Biology (Aug 2021)

14-3-3 proteins inactivate DAPK2 by promoting its dimerization and protecting key regulatory phosphosites

Matej Horvath,
Olivia Petrvalska,
Petr Herman,
Veronika Obsilova,
Tomas Obsil

Affiliations

Matej Horvath: Department of Physical and Macromolecular Chemistry, Faculty of Science, Charles University
Olivia Petrvalska: Department of Physical and Macromolecular Chemistry, Faculty of Science, Charles University
Petr Herman: Institute of Physics, Faculty of Mathematics and Physics, Charles University
Veronika Obsilova: Department of Structural Biology of Signaling Proteins, Division BIOCEV, Institute of Physiology of the Czech Academy of Sciences
Tomas Obsil: Department of Physical and Macromolecular Chemistry, Faculty of Science, Charles University

DOI: https://doi.org/10.1038/s42003-021-02518-y
Journal volume & issue: Vol. 4, no. 1
pp. 1 – 14

Abstract

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Horvath et al. structurally and biochemically characterize the full-length human DAPK2-14-3-3 complex to investigate the effects of binding to DAPK2 on its dimerization, activation by dephosphorylation of Ser318, and Ca2+/calmodulin binding. Their results provide mechanistic insights into 14- 3-3-mediated DAPK2 inhibition and highlight the potential of the DAPK2:14-3-3 complex as a target for anti-inflammatory therapies.

Published in Communications Biology

ISSN: 2399-3642 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science: Biology (General)
Website: https://www.nature.com/commsbio/

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