CDK1-cyclin-B1-induced kindlin degradation drives focal adhesion disassembly at mitotic entry.
Journal
Nature cell biology
ISSN: 1476-4679
Titre abrégé: Nat Cell Biol
Pays: England
ID NLM: 100890575
Informations de publication
Date de publication:
05 2022
05 2022
Historique:
received:
10
08
2021
accepted:
03
03
2022
pubmed:
27
4
2022
medline:
18
5
2022
entrez:
26
4
2022
Statut:
ppublish
Résumé
The disassembly of integrin-containing focal adhesions (FAs) at mitotic entry is essential for cell rounding, mitotic retraction fibre formation, bipolar spindle positioning and chromosome segregation. The mechanism that drives FA disassembly at mitotic entry is unknown. Here, we show that the CDK1-cyclin B1 complex phosphorylates the integrin activator kindlin, which results in the recruitment of the cullin 9-FBXL10 ubiquitin ligase complex that mediates kindlin ubiquitination and degradation. This molecular pathway is essential for FA disassembly and cell rounding, as phospho-inhibitory mutations of the CDK1 motif prevent kindlin degradation, FA disassembly and mitotic cell rounding. Conversely, phospho-mimetic mutations promote kindlin degradation in interphase, accelerate mitotic cell rounding and impair mitotic retraction fibre formation. Despite the opposing effects on kindlin stability, both types of mutations cause severe mitotic spindle defects, apoptosis and aneuploidy. Thus, the exquisite regulation of kindlin levels at mitotic entry is essential for cells to progress accurately through mitosis.
Identifiants
pubmed: 35469017
doi: 10.1038/s41556-022-00886-z
pii: 10.1038/s41556-022-00886-z
pmc: PMC9106588
doi:
Substances chimiques
Cell Cycle Proteins
0
Cyclin B1
0
Integrins
0
CDC2 Protein Kinase
EC 2.7.11.22
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
723-736Informations de copyright
© 2022. The Author(s).
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