| JURÁSEK, Miroslav, Jitender KUMAR, Petra PACLÍKOVÁ, Alka Kumari JADAUN, Konstantinos TRIPSIANES, Vítězslav BRYJA and Robert VÁCHA. Phosphorylation-induced changes in the PDZ domain of Dishevelled 3. Scientific Reports. NATURE PUBLISHING GROUP, 2021, vol. 11, No 1, p. "1484", 14 pp. ISSN 2045-2322. Available from: https://dx.doi.org/10.1038/s41598-020-79398-5. |
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@article{1752563,
author = {Jurásek, Miroslav and Kumar, Jitender and Paclíková, Petra and Jadaun, Alka Kumari and Tripsianes, Konstantinos and Bryja, Vítězslav and Vácha, Robert},
article_number = {1},
doi = {http://dx.doi.org/10.1038/s41598-020-79398-5},
keywords = {HUMAN PHOSPHATASE HPTP1E; PARTICLE MESH EWALD; PROTEIN INTERACTIONS; LIGAND RECOGNITION; PAR-6 PDZ; BINDING; DYNAMICS; REVEALS; COMPLEX; MODES},
language = {eng},
issn = {2045-2322},
journal = {Scientific Reports},
title = {Phosphorylation-induced changes in the PDZ domain of Dishevelled 3},
url = {https://www.nature.com/articles/s41598-020-79398-5},
volume = {11},
year = {2021}
}
TY - JOUR
ID - 1752563
AU - Jurásek, Miroslav - Kumar, Jitender - Paclíková, Petra - Jadaun, Alka Kumari - Tripsianes, Konstantinos - Bryja, Vítězslav - Vácha, Robert
PY - 2021
TI - Phosphorylation-induced changes in the PDZ domain of Dishevelled 3
JF - Scientific Reports
VL - 11
IS - 1
SP - "1484"
EP - "1484"
PB - NATURE PUBLISHING GROUP
SN - 20452322
KW - HUMAN PHOSPHATASE HPTP1E
KW - PARTICLE MESH EWALD
KW - PROTEIN INTERACTIONS
KW - LIGAND RECOGNITION
KW - PAR-6 PDZ
KW - BINDING
KW - DYNAMICS
KW - REVEALS
KW - COMPLEX
KW - MODES
UR - https://www.nature.com/articles/s41598-020-79398-5
N2 - The PDZ domain of Dishevelled 3 protein belongs to a highly abundant protein recognition motif which typically binds short C-terminal peptides. The affinity of the PDZ towards the peptides could be fine-tuned by a variety of post-translation modifications including phosphorylation. However, how phosphorylations affect the PDZ structure and its interactions with ligands remains elusive. Combining molecular dynamics simulations, NMR titration, and biological experiments, we explored the role of previously reported phosphorylation sites and their mimetics in the Dishevelled PDZ domain. Our observations suggest three major roles for phosphorylations: (1) acting as an on/off PDZ binding switch, (2) allosterically affecting the binding groove, and (3) influencing the secondary binding site. Our simulations indicated that mimetics had similar but weaker effects, and the effects of distinct sites were non-additive. This study provides insight into the Dishevelled regulation by PDZ phosphorylation. Furthermore, the observed effects could be used to elucidate the regulation mechanisms in other PDZ domains.
ER -
JURÁSEK, Miroslav, Jitender KUMAR, Petra PACLÍKOVÁ, Alka Kumari JADAUN, Konstantinos TRIPSIANES, Vítězslav BRYJA and Robert VÁCHA. Phosphorylation-induced changes in the PDZ domain of Dishevelled 3. \textit{Scientific Reports}. NATURE PUBLISHING GROUP, 2021, vol.~11, No~1, p.~''1484'', 14 pp. ISSN~2045-2322. Available from: https://dx.doi.org/10.1038/s41598-020-79398-5.
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