14-3-3-protein regulates Nedd4-2 by modulating interactions between HECT and WW domains

Pavel Pohl; Rohit Joshi; Olivia Petrvalska; Tomas Obsil; Veronika Obsilova

doi:10.1038/s42003-021-02419-0

Communications Biology (Jul 2021)

14-3-3-protein regulates Nedd4-2 by modulating interactions between HECT and WW domains

Pavel Pohl,
Rohit Joshi,
Olivia Petrvalska,
Tomas Obsil,
Veronika Obsilova

Affiliations

Pavel Pohl: Department of Structural Biology of Signaling Proteins, Division BIOCEV, Institute of Physiology of the Czech Academy of Sciences
Rohit Joshi: Department of Structural Biology of Signaling Proteins, Division BIOCEV, Institute of Physiology of the Czech Academy of Sciences
Olivia Petrvalska: Department of Structural Biology of Signaling Proteins, Division BIOCEV, Institute of Physiology of the Czech Academy of Sciences
Tomas Obsil: Department of Structural Biology of Signaling Proteins, Division BIOCEV, Institute of Physiology of the Czech Academy of Sciences
Veronika Obsilova: Department of Structural Biology of Signaling Proteins, Division BIOCEV, Institute of Physiology of the Czech Academy of Sciences

DOI: https://doi.org/10.1038/s42003-021-02419-0
Journal volume & issue: Vol. 4, no. 1
pp. 1 – 15

Abstract

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Pohl et al. investigated the structural basis of Nedd4-2 regulation by 14-3-3 and found that phosphorylated Ser342 and Ser448 are the main residues that facilitate 14-3-3 binding to Nedd4-2. The authors propose that the Nedd4-2:14-3-3 complex then stimulates a structural rearrangement of Nedd4-2 through inhibiting interaction of its structured domains.

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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