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Hyperphosphorylation of Human Osteopontin and Its Impact on Structural Dynamics and Molecular Recognition

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cris.lastimport.scopus2024-02-12T19:53:58Z
dc.abstract.enProtein phosphorylation is an abundant post-translational modification (PTM) and an essential modulator of protein functionality in living cells. Intrinsically disordered proteins (IDPs) are particular targets of PTM protein kinases due to their involvement in fundamental protein interaction networks. Despite their dynamic nature, IDPs are far from having random-coil conformations but exhibit significant structural heterogeneity. Changes in the molecular environment, most prominently in the form of PTM via phosphorylation, can modulate these structural features. Therefore, how phosphorylation events can alter conformational ensembles of IDPs and their interactions with binding partners is of great interest. Here we study the effects of hyperphosphorylation on the IDP osteopontin (OPN), an extracellular target of the Fam20C kinase. We report a full characterization of the phosphorylation sites of OPN using a combined nuclear magnetic resonance/mass spectrometry approach and provide evidence for an increase in the local flexibility of highly phosphorylated regions and the ensuing overall structural elongation. Our study emphasizes the simultaneous importance of electrostatic and hydrophobic interactions in the formation of compact substates in IDPs and their relevance for molecular recognition events.
dc.affiliationUniwersytet Warszawski
dc.contributor.authorHolzinger, Julian
dc.contributor.authorMateos, Borja
dc.contributor.authorKonrat, Robert
dc.contributor.authorAnrather, Dorothea
dc.contributor.authorSealey-Cardona, Marco
dc.contributor.authorPlatzer, Gerald
dc.contributor.authorConrad-Billroth, Clara
dc.contributor.authorŻerko, Szymon
dc.contributor.authorKoźmiński, Wiktor
dc.date.accessioned2024-01-25T03:31:59Z
dc.date.available2024-01-25T03:31:59Z
dc.date.copyright2021-04-20
dc.date.issued2021
dc.description.accesstimeAT_PUBLICATION
dc.description.financePublikacja bezkosztowa
dc.description.number17
dc.description.versionFINAL_PUBLISHED
dc.description.volume60
dc.identifier.doi10.1021/ACS.BIOCHEM.1C00050
dc.identifier.issn0006-2960
dc.identifier.urihttps://repozytorium.uw.edu.pl//handle/item/108813
dc.identifier.weblinkhttps://pubs.acs.org/doi/pdf/10.1021/acs.biochem.1c00050
dc.languageeng
dc.pbn.affiliationchemical sciences
dc.relation.ispartofBiochemistry
dc.relation.pages1347-1355
dc.rightsCC-BY
dc.sciencecloudnosend
dc.titleHyperphosphorylation of Human Osteopontin and Its Impact on Structural Dynamics and Molecular Recognition
dc.typeJournalArticle
dspace.entity.typePublication