دورية أكاديمية

A cyclin-dependent kinase-mediated phosphorylation switch of disordered protein condensation

التفاصيل البيبلوغرافية
العنوان: A cyclin-dependent kinase-mediated phosphorylation switch of disordered protein condensation
المؤلفون: Valverde, Juan Manuel, Dubra, Geronimo, Phillips, Michael, Haider, Austin, Elena-Real, Carlos, Fournet, Aurélie, Alghoul, Emile, Chahar, Dhanvantri, Andrés-Sanchez, Nuria, Paloni, Matteo, Bernadó, Pau, van Mierlo, Guido, Vermeulen, Michiel, van den Toorn, Henk, Heck, Albert J.R., Constantinou, Angelos, Barducci, Alessandro, Ghosh, Kingshuk, Sibille, Nathalie, Knipscheer, Puck, Krasinska, Liliana, Fisher, Daniel, Altelaar, Maarten
المساهمون: Hubrecht Institute with UMC
سنة النشر: 2023
مصطلحات موضوعية: General Chemistry, General Biochemistry,Genetics and Molecular Biology, General Physics and Astronomy
الوصف: Cell cycle transitions result from global changes in protein phosphorylation states triggered by cyclin-dependent kinases (CDKs). To understand how this complexity produces an ordered and rapid cellular reorganisation, we generated a high-resolution map of changing phosphosites throughout unperturbed early cell cycles in single Xenopus embryos, derived the emergent principles through systems biology analysis, and tested them by biophysical modelling and biochemical experiments. We found that most dynamic phosphosites share two key characteristics: they occur on highly disordered proteins that localise to membraneless organelles, and are CDK targets. Furthermore, CDK-mediated multisite phosphorylation can switch homotypic interactions of such proteins between favourable and inhibitory modes for biomolecular condensate formation. These results provide insight into the molecular mechanisms and kinetics of mitotic cellular reorganisation.
نوع الوثيقة: article in journal/newspaper
وصف الملف: application/pdf
اللغة: English
تدمد: 2041-1723
العلاقة: https://dspace.library.uu.nl/handle/1874/451131Test
الإتاحة: https://dspace.library.uu.nl/handle/1874/451131Test
حقوق: info:eu-repo/semantics/OpenAccess
رقم الانضمام: edsbas.14FD8D15
قاعدة البيانات: BASE