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Naše nové dva články v Communications Biology


Two accepted papers in Communications Biology: July and August 2021

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

14-3-3-protein regulates Nedd4-2 by modulating interactions between HECT and WW domains | Communications Biology (nature.com)

Commun. Biol. 2021 July 22; 4(1):899.

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

14-3-3 proteins inactivate DAPK2 by promoting its dimerization and protecting key regulatory phosphosites | Communications Biology (nature.com)

Commun. Biol. 2021 August 19; 4(1):986.

 

IF = 6.268
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.
 
Horvath et al. structurally and biochemically characterized the full-lenght human DAPK-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.
 
 
 
 
Characterization of the interaction between Nedd4-2 and 14-3-3 in solution. a) Sedimentation coefficient distributions (c(s)) , b) Isotherm of weight-averaged sedimentation coefficients (sw) derived from SV-AUC analysis, c) SAXS-based structural model of the complex with the crystal structures of the Nedd4-2 phosphopeptides.