Binding of CEP152 to PLK4 stimulates kinase activity to promote centriole assembly
Formation of a new procentriole starts with the assembly of a cartwheel structure that is catalyzed by the conserved PLK4 kinase. How PLK4 itself gets activated is not precisely known. - - The authors studied the activation of PLK4 by the centrosomal protein CEP152 in human cells using U-ExM. They...
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| Hauptverfasser: | , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
July 01, 2025
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| In: |
Molecular biology of the cell
Year: 2025, Jahrgang: 36, Heft: 7, Pages: 1-13 |
| ISSN: | 1939-4586 |
| DOI: | 10.1091/mbc.E24-12-0581 |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1091/mbc.E24-12-0581 Verlag, lizenzpflichtig, Volltext: https://www.molbiolcell.org/doi/10.1091/mbc.E24-12-0581 
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| Verfasserangaben: | Hazal Kübra Gürkaşlar, and Ingrid Hoffmann |
| Zusammenfassung: | Formation of a new procentriole starts with the assembly of a cartwheel structure that is catalyzed by the conserved PLK4 kinase. How PLK4 itself gets activated is not precisely known. - - The authors studied the activation of PLK4 by the centrosomal protein CEP152 in human cells using U-ExM. They found that CEP152 can phosphorylate and activate PLK4 both in vitro and in vivo. - - Their findings suggest that CEP152 is involved in PLK4 activation in S-phase by binding to the PB1-PB2 domains of PLK4. This in turn allows PLK4 dimerization and activation through phosphorylation to ensure proper centriole duplication. |
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| Beschreibung: | Online veröffentlicht: 01. Juli 2025 Gesehen am 18.11.2025 |
| Beschreibung: | Online Resource |
| ISSN: | 1939-4586 |
| DOI: | 10.1091/mbc.E24-12-0581 |