Phosphorylation-induced changes in the PDZ domain of Dishevelled 3
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F21%3A00118888" target="_blank" >RIV/00216224:14740/21:00118888 - isvavai.cz</a>
Alternative codes found
RIV/68081707:_____/21:00541958
Result on the web
<a href="https://www.nature.com/articles/s41598-020-79398-5" target="_blank" >https://www.nature.com/articles/s41598-020-79398-5</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/s41598-020-79398-5" target="_blank" >10.1038/s41598-020-79398-5</a>
Alternative languages
Result language
angličtina
Original language name
Phosphorylation-induced changes in the PDZ domain of Dishevelled 3
Original language description
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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2021
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Scientific Reports
ISSN
2045-2322
e-ISSN
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Volume of the periodical
11
Issue of the periodical within the volume
1
Country of publishing house
DE - GERMANY
Number of pages
14
Pages from-to
„1484“
UT code for WoS article
000609782400005
EID of the result in the Scopus database
2-s2.0-85100070769