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@article{2262440,
author = {Joshi, Rohit and Pohl, Pavel and Strachotova, Dita and Herman, Petr and Obsil, Tomas and Obsilova, Veronika},
article_location = {Bethesda, USA},
article_number = {7},
doi = {http://dx.doi.org/10.1016/j.bpj.2022.02.025},
keywords = {14-3-3 Proteins; Catalytic Domain; Endosomal Sorting Complexes Required for Transport;},
language = {eng},
issn = {0006-3495},
journal = {Biophysical Journal},
title = {Nedd4-2 binding to 14-3-3 modulates the accessibility of its catalytic site and WW domains},
url = {https://www.sciencedirect.com/science/article/abs/pii/S0006349522001497?via%3Dihub},
volume = {121},
year = {2022}
}
TY - JOUR
ID - 2262440
AU - Joshi, Rohit - Pohl, Pavel - Strachotova, Dita - Herman, Petr - Obsil, Tomas - Obsilova, Veronika
PY - 2022
TI - Nedd4-2 binding to 14-3-3 modulates the accessibility of its catalytic site and WW domains
JF - Biophysical Journal
VL - 121
IS - 7
SP - 1299-1311
EP - 1299-1311
PB - Biophysical Society
SN - 00063495
KW - 14-3-3 Proteins
KW - Catalytic Domain
KW - Endosomal Sorting Complexes Required for Transport;
UR - https://www.sciencedirect.com/science/article/abs/pii/S0006349522001497?via%3Dihub
N2 - Neural precursor cells expressed developmentally downregulated protein 4-2 (Nedd4-2), a homologous to the E6 AP carboxyl terminus (HECT) ubiquitin ligase, triggers the endocytosis and degradation of its downstream target molecules by regulating signal transduction through interactions with other targets, including 14-3-3 proteins. In our previous study, we found that 14-3-3 binding induces a structural rearrangement of Nedd4-2 by inhibiting interactions between its structured domains. Here, we used time-resolved fluorescence intensity and anisotropy decay measurements, together with fluorescence quenching and mass spectrometry, to further characterize interactions between Nedd4-2 and 14-3-3 proteins. The results showed that 143-3 binding affects the emission properties of AEDANS-labeled WW3, WW4, and, to a lesser extent, WW2 domains, and reduces their mobility, but not those of the WW1 domain, which remains mobile. In contrast, 14-3-3 binding has the opposite effect on the active site of the HECT domain, which is more solvent exposed and mobile in the complexed form than in the apo form of Nedd4-2. Overall, our results suggest that steric hindrance of the WW3 and WW4 domains combined with conformational changes in the catalytic domain may account for the 14-3-3 binding-mediated regulation of Nedd4-2.
ER -
JOSHI, Rohit, Pavel POHL, Dita STRACHOTOVA, Petr HERMAN, Tomas OBSIL a Veronika OBSILOVA. Nedd4-2 binding to 14-3-3 modulates the accessibility of its catalytic site and WW domains. \textit{Biophysical Journal}. Bethesda, USA: Biophysical Society, 2022, roč.~121, č.~7, s.~1299-1311. ISSN~0006-3495. Dostupné z: https://dx.doi.org/10.1016/j.bpj.2022.02.025.
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