Prediction of protein interactions with function in protein (de-)phosphorylation
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F25%3A00143909" target="_blank" >RIV/00216224:14740/25:00143909 - isvavai.cz</a>
Result on the web
<a href="https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0319084" target="_blank" >https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0319084</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1371/journal.pone.0319084" target="_blank" >10.1371/journal.pone.0319084</a>
Alternative languages
Result language
angličtina
Original language name
Prediction of protein interactions with function in protein (de-)phosphorylation
Original language description
Protein-protein interactions (PPIs) form a complex network called "interactome" that regulates many functions in the cell. In recent years, there is an increasing accumulation of evidence supporting the existence of a hyperbolic geometry underlying the network representation of complex systems such as the interactome. In particular, it has been shown that the embedding of the human Protein-Interaction Network (hPIN) in hyperbolic space (H2) captures biologically relevant information. Here we explore whether this mapping contains information that would allow us to predict the function of PPIs, more specifically interactions related to post-translational modification (PTM). We used a random forest algorithm to predict PTM-related directed PPIs, concretely, protein phosphorylation and dephosphorylation, based on hyperbolic properties and centrality measures of the hPIN mapped in H2. To evaluate the efficacy of our algorithm, we predicted PTM-related PPIs of ataxin-1, a protein which is responsible for Spinocerebellar Ataxia type 1 (SCA1). Proteomics analysis in a cellular model revealed that several of the predicted PTM-PPIs were indeed dysregulated in a SCA1-related disease network. A compact cluster composed of ataxin-1, its dysregulated PTM-PPIs and their common upstream regulators may represent critical interactions for disease pathology. Thus, our algorithm may infer phosphorylation activity on proteins through directed PPIs.
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
10600 - Biological sciences
Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2025
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
PLoS Biology
ISSN
1932-6203
e-ISSN
1932-6203
Volume of the periodical
20
Issue of the periodical within the volume
3
Country of publishing house
US - UNITED STATES
Number of pages
21
Pages from-to
1-21
UT code for WoS article
001437514700024
EID of the result in the Scopus database
2-s2.0-86000330544