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- W3138934297 abstract "Abstract The seven 14-3-3 isoforms are highly abundant human proteins encoded by similar yet distinct genes. 14-3-3 proteins recognize phosphorylated motifs within numerous human and viral proteins. Here, we analyze by X-ray crystallography, fluorescence polarization, mutagenesis and fusicoccin-mediated modulation the structural basis and druggability of 14-3-3 binding to four E6 oncoproteins of tumorigenic human papillomaviruses. 14-3-3 isoforms bind variant and mutated phospho-motifs of E6 and unrelated protein RSK1 with different affinities, albeit following an ordered affinity ranking with conserved relative K D ratios. Remarkably, 14-3-3 isoforms obey the same hierarchy when binding to most of their established targets, as supported by literature and a recent human complexome map. This knowledge allows predicting proportions of 14-3-3 isoforms engaged with phosphoproteins in various tissues. Notwithstanding their individual functions, cellular concentrations of 14-3-3 may be collectively adjusted to buffer the strongest phosphorylation outbursts, explaining their expression variations in different tissues and tumors." @default.
- W3138934297 created "2021-03-29" @default.
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- W3138934297 date "2021-03-15" @default.
- W3138934297 modified "2023-10-17" @default.
- W3138934297 title "Hierarchized phosphotarget binding by the seven human 14-3-3 isoforms" @default.
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- W3138934297 doi "https://doi.org/10.1038/s41467-021-21908-8" @default.
- W3138934297 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7961048" @default.
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