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

Juan Manuel Valverde; Geronimo Dubra; Michael Phillips; Austin Haider; Carlos Elena-Real; Aurélie Fournet; Emile Alghoul; Dhanvantri Chahar; Nuria Andrés-Sanchez; Matteo Paloni; Pau Bernadó; Guido van Mierlo; Michiel Vermeulen; Henk van den Toorn; Albert J.R. Heck; Angelos Constantinou; Alessandro Barducci; Kingshuk Ghosh; Nathalie Sibille; Puck Knipscheer; Liliana Krasinska; Daniel Fisher; Maarten Altelaar

doi:10.1038/s41467-023-42049-0

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

Juan Manuel Valverde, Geronimo Dubra, Michael Phillips, Austin Haider, Carlos Elena-Real, Aurélie Fournet, Emile Alghoul, Dhanvantri Chahar, Nuria Andrés-Sanchez, Matteo Paloni, Pau Bernadó, Guido van Mierlo, Michiel Vermeulen, Henk van den Toorn, Albert J.R. Heck, Angelos Constantinou, Alessandro Barducci, Kingshuk Ghosh, Nathalie Sibille, Puck KnipscheerLiliana Krasinska, Daniel Fisher^*, Maarten Altelaar^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

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.

Original language	English
Article number	6316
Pages (from-to)	1-23
Number of pages	23
Journal	Nature Communications
Volume	14
Issue number	1
DOIs	https://doi.org/10.1038/s41467-023-42049-0
Publication status	Published - 9 Oct 2023

Bibliographical note

Funding Information:
We thank Merlijn Witte for technical assistance with the Xenopus laevis egg fertilisation experiments, Ariane Abrieu for a gift of CSF egg extracts, Markus Raschle from the Technical University of Kaiserslautern for providing the Xenopus laevis protein database, Jonathan Huihui during early phases of theoretical analysis using SCDM, and Damien Coudreuse for critical reading of the manuscript. A.J.R.H. and M.A. acknowledge support from the Horizon 2020 program INFRAIA project Epic-XS (Project 823839) and the NWO funded Netherlands Proteomics Centre through the National Road Map for Large-scale Infrastructures program X-Omics (Project 184.034.019) of the Netherlands Proteomics Centre. J.M.V. is supported by scholarships from the Ministry of Science and Technology of Costa Rica (MICITT) and the University of Costa Rica (UCR). M.P. acknowledges support from NSF award number DMR-2213103. P.K. and M.V. are funded by the Oncode Institute which is financed by the Dutch Cancer Society and by the gravitation program CancerGenomiCs.nl from the Netherlands Organisation for Scientific Research (NWO). D.F. and L.K. are INSERM employees. GD is funded by the Institut National de Cancer, France (INCa) PRT-K programme (PRT-K17 n° 2018-023). The Fisher lab was funded by the Ligue Nationale Contre le Cancer, France (EL2018.LNCC/DF) and INCa (PLBIO18-094) and is currently supported by the Fondation ARC (N° ARCPGA12021010002850_3574). N.S. is supported by the ANR GPCteR (ANR-17- CE11-0022-01). D.F. and N.S. also acknowledge support from the I-SITE Excellence Program of the University of Montpellier, part of the Investissements France 2030. The CBS is a member of France-BioImaging (FBI) and the French Infrastructure for Integrated Structural Biology (FRISBI), supported by the French National Research Agency (ANR-10-INBS-04-01 and ANR-10-INBS-05). K.G. acknowledges support from NIH R01GM138901.

Funding Information:
We thank Merlijn Witte for technical assistance with the Xenopus laevis egg fertilisation experiments, Ariane Abrieu for a gift of CSF egg extracts, Markus Raschle from the Technical University of Kaiserslautern for providing the Xenopus laevis protein database, Jonathan Huihui during early phases of theoretical analysis using SCDM, and Damien Coudreuse for critical reading of the manuscript. A.J.R.H. and M.A. acknowledge support from the Horizon 2020 program INFRAIA project Epic-XS (Project 823839) and the NWO funded Netherlands Proteomics Centre through the National Road Map for Large-scale Infrastructures program X-Omics (Project 184.034.019) of the Netherlands Proteomics Centre. J.M.V. is supported by scholarships from the Ministry of Science and Technology of Costa Rica (MICITT) and the University of Costa Rica (UCR). M.P. acknowledges support from NSF award number DMR-2213103. P.K. and M.V. are funded by the Oncode Institute which is financed by the Dutch Cancer Society and by the gravitation program CancerGenomiCs.nl from the Netherlands Organisation for Scientific Research (NWO). D.F. and L.K. are INSERM employees. GD is funded by the Institut National de Cancer, France (INCa) PRT-K programme (PRT-K17 n° 2018-023). The Fisher lab was funded by the Ligue Nationale Contre le Cancer, France (EL2018.LNCC/DF) and INCa (PLBIO18-094) and is currently supported by the Fondation ARC (N° ARCPGA12021010002850_3574). N.S. is supported by the ANR GPCteR (ANR-17- CE11-0022-01). D.F. and N.S. also acknowledge support from the I-SITE Excellence Program of the University of Montpellier, part of the Investissements France 2030. The CBS is a member of France-BioImaging (FBI) and the French Infrastructure for Integrated Structural Biology (FRISBI), supported by the French National Research Agency (ANR-10-INBS-04-01 and ANR-10-INBS-05). K.G. acknowledges support from NIH R01GM138901.

Publisher Copyright:
© 2023, Springer Nature Limited.

Funding

We thank Merlijn Witte for technical assistance with the Xenopus laevis egg fertilisation experiments, Ariane Abrieu for a gift of CSF egg extracts, Markus Raschle from the Technical University of Kaiserslautern for providing the Xenopus laevis protein database, Jonathan Huihui during early phases of theoretical analysis using SCDM, and Damien Coudreuse for critical reading of the manuscript. A.J.R.H. and M.A. acknowledge support from the Horizon 2020 program INFRAIA project Epic-XS (Project 823839) and the NWO funded Netherlands Proteomics Centre through the National Road Map for Large-scale Infrastructures program X-Omics (Project 184.034.019) of the Netherlands Proteomics Centre. J.M.V. is supported by scholarships from the Ministry of Science and Technology of Costa Rica (MICITT) and the University of Costa Rica (UCR). M.P. acknowledges support from NSF award number DMR-2213103. P.K. and M.V. are funded by the Oncode Institute which is financed by the Dutch Cancer Society and by the gravitation program CancerGenomiCs.nl from the Netherlands Organisation for Scientific Research (NWO). D.F. and L.K. are INSERM employees. GD is funded by the Institut National de Cancer, France (INCa) PRT-K programme (PRT-K17 n° 2018-023). The Fisher lab was funded by the Ligue Nationale Contre le Cancer, France (EL2018.LNCC/DF) and INCa (PLBIO18-094) and is currently supported by the Fondation ARC (N° ARCPGA12021010002850_3574). N.S. is supported by the ANR GPCteR (ANR-17- CE11-0022-01). D.F. and N.S. also acknowledge support from the I-SITE Excellence Program of the University of Montpellier, part of the Investissements France 2030. The CBS is a member of France-BioImaging (FBI) and the French Infrastructure for Integrated Structural Biology (FRISBI), supported by the French National Research Agency (ANR-10-INBS-04-01 and ANR-10-INBS-05). K.G. acknowledges support from NIH R01GM138901. We thank Merlijn Witte for technical assistance with the Xenopus laevis egg fertilisation experiments, Ariane Abrieu for a gift of CSF egg extracts, Markus Raschle from the Technical University of Kaiserslautern for providing the Xenopus laevis protein database, Jonathan Huihui during early phases of theoretical analysis using SCDM, and Damien Coudreuse for critical reading of the manuscript. A.J.R.H. and M.A. acknowledge support from the Horizon 2020 program INFRAIA project Epic-XS (Project 823839) and the NWO funded Netherlands Proteomics Centre through the National Road Map for Large-scale Infrastructures program X-Omics (Project 184.034.019) of the Netherlands Proteomics Centre. J.M.V. is supported by scholarships from the Ministry of Science and Technology of Costa Rica (MICITT) and the University of Costa Rica (UCR). M.P. acknowledges support from NSF award number DMR-2213103. P.K. and M.V. are funded by the Oncode Institute which is financed by the Dutch Cancer Society and by the gravitation program CancerGenomiCs.nl from the Netherlands Organisation for Scientific Research (NWO). D.F. and L.K. are INSERM employees. GD is funded by the Institut National de Cancer, France (INCa) PRT-K programme (PRT-K17 n° 2018-023). The Fisher lab was funded by the Ligue Nationale Contre le Cancer, France (EL2018.LNCC/DF) and INCa (PLBIO18-094) and is currently supported by the Fondation ARC (N° ARCPGA12021010002850_3574). N.S. is supported by the ANR GPCteR (ANR-17- CE11-0022-01). D.F. and N.S. also acknowledge support from the I-SITE Excellence Program of the University of Montpellier, part of the Investissements France 2030. The CBS is a member of France-BioImaging (FBI) and the French Infrastructure for Integrated Structural Biology (FRISBI), supported by the French National Research Agency (ANR-10-INBS-04-01 and ANR-10-INBS-05). K.G. acknowledges support from NIH R01GM138901.

Funders	Funder number
We thank Merlijn Witte for technical assistance with the <italic>Xenopus laevis</italic> egg fertilisation experiments, Ariane Abrieu for a gift of CSF egg extracts, Markus Raschle from the Technical University of Kaiserslautern for providing the <italic>X	823839
NWO funded Netherlands Proteomics Centre through the National Road Map for Large-scale Infrastructures program X-Omics	184.034.019
Ministry of Science and Technology of Costa Rica (MICITT)
University of Costa Rica (UCR)	DMR-2213103
NSF
Oncode Institute
Dutch Cancer Society
Netherlands Organisation for Scientific Research (NWO)	PRT-K17 ndegrees 2018-023
INSERM - Institut National de Cancer, France (INCa)
Ligue Nationale Contre le Cancer, France (EL2018.LNCC/DF)	PLBIO18-094
INCa
Fondation ARC	Ndegrees ARCPGA12021010002850_3574, ANR-17- CE11-0022-01
I-SITE Excellence Program of the University of Montpellier
Investissements France
CBS is a member of France-BioImaging (FBI)
French Infrastructure for Integrated Structural Biology (FRISBI)	ANR-10-INBS-04-01, ANR-10-INBS-05
French National Research Agency
NIH	R01GM138901

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s41467-023-42049-0Final published version, 25.3 MBLicence: CC BY

Cite this

Valverde, J. M., Dubra, G., Phillips, M., Haider, A., Elena-Real, C., Fournet, A., Alghoul, E., Chahar, D., Andrés-Sanchez, N., Paloni, M., Bernadó, P., van Mierlo, G., Vermeulen, M., van den Toorn, H., Heck, A. J. R., Constantinou, A., Barducci, A., Ghosh, K., Sibille, N., ... Altelaar, M. (2023). A cyclin-dependent kinase-mediated phosphorylation switch of disordered protein condensation. Nature Communications, 14(1), 1-23. Article 6316. https://doi.org/10.1038/s41467-023-42049-0

@article{e003b8a3f53c4c53be562704a274774a,

title = "A cyclin-dependent kinase-mediated phosphorylation switch of disordered protein condensation",

abstract = "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.",

author = "Valverde, {Juan Manuel} and Geronimo Dubra and Michael Phillips and Austin Haider and Carlos Elena-Real and Aur{\'e}lie Fournet and Emile Alghoul and Dhanvantri Chahar and Nuria Andr{\'e}s-Sanchez and Matteo Paloni and Pau Bernad{\'o} and {van Mierlo}, Guido and Michiel Vermeulen and {van den Toorn}, Henk and Heck, {Albert J.R.} and Angelos Constantinou and Alessandro Barducci and Kingshuk Ghosh and Nathalie Sibille and Puck Knipscheer and Liliana Krasinska and Daniel Fisher and Maarten Altelaar",

note = "Funding Information: We thank Merlijn Witte for technical assistance with the Xenopus laevis egg fertilisation experiments, Ariane Abrieu for a gift of CSF egg extracts, Markus Raschle from the Technical University of Kaiserslautern for providing the Xenopus laevis protein database, Jonathan Huihui during early phases of theoretical analysis using SCDM, and Damien Coudreuse for critical reading of the manuscript. A.J.R.H. and M.A. acknowledge support from the Horizon 2020 program INFRAIA project Epic-XS (Project 823839) and the NWO funded Netherlands Proteomics Centre through the National Road Map for Large-scale Infrastructures program X-Omics (Project 184.034.019) of the Netherlands Proteomics Centre. J.M.V. is supported by scholarships from the Ministry of Science and Technology of Costa Rica (MICITT) and the University of Costa Rica (UCR). M.P. acknowledges support from NSF award number DMR-2213103. P.K. and M.V. are funded by the Oncode Institute which is financed by the Dutch Cancer Society and by the gravitation program CancerGenomiCs.nl from the Netherlands Organisation for Scientific Research (NWO). D.F. and L.K. are INSERM employees. GD is funded by the Institut National de Cancer, France (INCa) PRT-K programme (PRT-K17 n° 2018-023). The Fisher lab was funded by the Ligue Nationale Contre le Cancer, France (EL2018.LNCC/DF) and INCa (PLBIO18-094) and is currently supported by the Fondation ARC (N° ARCPGA12021010002850_3574). N.S. is supported by the ANR GPCteR (ANR-17- CE11-0022-01). D.F. and N.S. also acknowledge support from the I-SITE Excellence Program of the University of Montpellier, part of the Investissements France 2030. The CBS is a member of France-BioImaging (FBI) and the French Infrastructure for Integrated Structural Biology (FRISBI), supported by the French National Research Agency (ANR-10-INBS-04-01 and ANR-10-INBS-05). K.G. acknowledges support from NIH R01GM138901. Funding Information: We thank Merlijn Witte for technical assistance with the Xenopus laevis egg fertilisation experiments, Ariane Abrieu for a gift of CSF egg extracts, Markus Raschle from the Technical University of Kaiserslautern for providing the Xenopus laevis protein database, Jonathan Huihui during early phases of theoretical analysis using SCDM, and Damien Coudreuse for critical reading of the manuscript. A.J.R.H. and M.A. acknowledge support from the Horizon 2020 program INFRAIA project Epic-XS (Project 823839) and the NWO funded Netherlands Proteomics Centre through the National Road Map for Large-scale Infrastructures program X-Omics (Project 184.034.019) of the Netherlands Proteomics Centre. J.M.V. is supported by scholarships from the Ministry of Science and Technology of Costa Rica (MICITT) and the University of Costa Rica (UCR). M.P. acknowledges support from NSF award number DMR-2213103. P.K. and M.V. are funded by the Oncode Institute which is financed by the Dutch Cancer Society and by the gravitation program CancerGenomiCs.nl from the Netherlands Organisation for Scientific Research (NWO). D.F. and L.K. are INSERM employees. GD is funded by the Institut National de Cancer, France (INCa) PRT-K programme (PRT-K17 n° 2018-023). The Fisher lab was funded by the Ligue Nationale Contre le Cancer, France (EL2018.LNCC/DF) and INCa (PLBIO18-094) and is currently supported by the Fondation ARC (N° ARCPGA12021010002850_3574). N.S. is supported by the ANR GPCteR (ANR-17- CE11-0022-01). D.F. and N.S. also acknowledge support from the I-SITE Excellence Program of the University of Montpellier, part of the Investissements France 2030. The CBS is a member of France-BioImaging (FBI) and the French Infrastructure for Integrated Structural Biology (FRISBI), supported by the French National Research Agency (ANR-10-INBS-04-01 and ANR-10-INBS-05). K.G. acknowledges support from NIH R01GM138901. Publisher Copyright: {\textcopyright} 2023, Springer Nature Limited.",

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month = oct,

day = "9",

doi = "10.1038/s41467-023-42049-0",

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Valverde, JM, Dubra, G, Phillips, M, Haider, A, Elena-Real, C, Fournet, A, Alghoul, E, Chahar, D, Andrés-Sanchez, N, Paloni, M, Bernadó, P, van Mierlo, G, Vermeulen, M, van den Toorn, H , Heck, AJR, Constantinou, A, Barducci, A, Ghosh, K, Sibille, N, Knipscheer, P, Krasinska, L, Fisher, D & Altelaar, M 2023, 'A cyclin-dependent kinase-mediated phosphorylation switch of disordered protein condensation', Nature Communications, vol. 14, no. 1, 6316, pp. 1-23. https://doi.org/10.1038/s41467-023-42049-0

TY - JOUR

T1 - A cyclin-dependent kinase-mediated phosphorylation switch of disordered protein condensation

AU - Valverde, Juan Manuel

AU - Dubra, Geronimo

AU - Phillips, Michael

AU - Haider, Austin

AU - Elena-Real, Carlos

AU - Fournet, Aurélie

AU - Alghoul, Emile

AU - Chahar, Dhanvantri

AU - Andrés-Sanchez, Nuria

AU - Paloni, Matteo

AU - Bernadó, Pau

AU - van Mierlo, Guido

AU - Vermeulen, Michiel

AU - van den Toorn, Henk

AU - Heck, Albert J.R.

AU - Constantinou, Angelos

AU - Barducci, Alessandro

AU - Ghosh, Kingshuk

AU - Sibille, Nathalie

AU - Knipscheer, Puck

AU - Krasinska, Liliana

AU - Fisher, Daniel

AU - Altelaar, Maarten

N1 - Funding Information: We thank Merlijn Witte for technical assistance with the Xenopus laevis egg fertilisation experiments, Ariane Abrieu for a gift of CSF egg extracts, Markus Raschle from the Technical University of Kaiserslautern for providing the Xenopus laevis protein database, Jonathan Huihui during early phases of theoretical analysis using SCDM, and Damien Coudreuse for critical reading of the manuscript. A.J.R.H. and M.A. acknowledge support from the Horizon 2020 program INFRAIA project Epic-XS (Project 823839) and the NWO funded Netherlands Proteomics Centre through the National Road Map for Large-scale Infrastructures program X-Omics (Project 184.034.019) of the Netherlands Proteomics Centre. J.M.V. is supported by scholarships from the Ministry of Science and Technology of Costa Rica (MICITT) and the University of Costa Rica (UCR). M.P. acknowledges support from NSF award number DMR-2213103. P.K. and M.V. are funded by the Oncode Institute which is financed by the Dutch Cancer Society and by the gravitation program CancerGenomiCs.nl from the Netherlands Organisation for Scientific Research (NWO). D.F. and L.K. are INSERM employees. GD is funded by the Institut National de Cancer, France (INCa) PRT-K programme (PRT-K17 n° 2018-023). The Fisher lab was funded by the Ligue Nationale Contre le Cancer, France (EL2018.LNCC/DF) and INCa (PLBIO18-094) and is currently supported by the Fondation ARC (N° ARCPGA12021010002850_3574). N.S. is supported by the ANR GPCteR (ANR-17- CE11-0022-01). D.F. and N.S. also acknowledge support from the I-SITE Excellence Program of the University of Montpellier, part of the Investissements France 2030. The CBS is a member of France-BioImaging (FBI) and the French Infrastructure for Integrated Structural Biology (FRISBI), supported by the French National Research Agency (ANR-10-INBS-04-01 and ANR-10-INBS-05). K.G. acknowledges support from NIH R01GM138901. Funding Information: We thank Merlijn Witte for technical assistance with the Xenopus laevis egg fertilisation experiments, Ariane Abrieu for a gift of CSF egg extracts, Markus Raschle from the Technical University of Kaiserslautern for providing the Xenopus laevis protein database, Jonathan Huihui during early phases of theoretical analysis using SCDM, and Damien Coudreuse for critical reading of the manuscript. A.J.R.H. and M.A. acknowledge support from the Horizon 2020 program INFRAIA project Epic-XS (Project 823839) and the NWO funded Netherlands Proteomics Centre through the National Road Map for Large-scale Infrastructures program X-Omics (Project 184.034.019) of the Netherlands Proteomics Centre. J.M.V. is supported by scholarships from the Ministry of Science and Technology of Costa Rica (MICITT) and the University of Costa Rica (UCR). M.P. acknowledges support from NSF award number DMR-2213103. P.K. and M.V. are funded by the Oncode Institute which is financed by the Dutch Cancer Society and by the gravitation program CancerGenomiCs.nl from the Netherlands Organisation for Scientific Research (NWO). D.F. and L.K. are INSERM employees. GD is funded by the Institut National de Cancer, France (INCa) PRT-K programme (PRT-K17 n° 2018-023). The Fisher lab was funded by the Ligue Nationale Contre le Cancer, France (EL2018.LNCC/DF) and INCa (PLBIO18-094) and is currently supported by the Fondation ARC (N° ARCPGA12021010002850_3574). N.S. is supported by the ANR GPCteR (ANR-17- CE11-0022-01). D.F. and N.S. also acknowledge support from the I-SITE Excellence Program of the University of Montpellier, part of the Investissements France 2030. The CBS is a member of France-BioImaging (FBI) and the French Infrastructure for Integrated Structural Biology (FRISBI), supported by the French National Research Agency (ANR-10-INBS-04-01 and ANR-10-INBS-05). K.G. acknowledges support from NIH R01GM138901. Publisher Copyright: © 2023, Springer Nature Limited.

PY - 2023/10/9

Y1 - 2023/10/9

N2 - 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.

AB - 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.

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U2 - 10.1038/s41467-023-42049-0

DO - 10.1038/s41467-023-42049-0

M3 - Article

C2 - 37813838

AN - SCOPUS:85173646007

SN - 2041-1723

VL - 14

SP - 1

EP - 23

JO - Nature Communications

JF - Nature Communications

IS - 1

M1 - 6316

ER -

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

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