Disappearance of Cdc14 from the daughter spindle pole body requires Glc7-Bud14.
Bud14
Cdc14
mitotic exit network
protein phosphatase 1
spindle pole body
Journal
Turkish journal of biology = Turk biyoloji dergisi
ISSN: 1303-6092
Titre abrégé: Turk J Biol
Pays: Turkey
ID NLM: 9434434
Informations de publication
Date de publication:
2024
2024
Historique:
received:
17
02
2024
revised:
15
10
2024
accepted:
17
09
2024
medline:
30
10
2024
pubmed:
30
10
2024
entrez:
30
10
2024
Statut:
epublish
Résumé
The conserved phosphatase Cdc14 facilitates mitotic exit in budding yeast by counteracting mitotic cyclin-dependent kinase activity. Cdc14 is kept in the nucleolus until anaphase onset, when it is released transiently into the nucleoplasm. In late anaphase, Cdc14 is fully released into the cytoplasm upon activation of the mitotic exit network (MEN) to trigger mitotic exit. Cdc14 also localizes to yeast spindle pole bodies (SPBs) in anaphase and dephosphorylates key targets residing on SPBs to allow SPB duplication and prime the MEN. Protein phosphatase 1 (Glc7) with regulatory subunit Bud14 is another phosphatase that plays a key role in the spatiotemporal control of mitotic exit. In this study, we investigated the regulation of Cdc14 localization by Bud14-Glc7. We used fluorescence microscopy to analyze Cdc14 localization in We found that Cdc14 remains at the SPBs longer in Our results suggest that Glc7-Bud14 is part of a mechanism that promotes Cdc14 disappearance from the dSPB.
Sections du résumé
Background/aim
UNASSIGNED
The conserved phosphatase Cdc14 facilitates mitotic exit in budding yeast by counteracting mitotic cyclin-dependent kinase activity. Cdc14 is kept in the nucleolus until anaphase onset, when it is released transiently into the nucleoplasm. In late anaphase, Cdc14 is fully released into the cytoplasm upon activation of the mitotic exit network (MEN) to trigger mitotic exit. Cdc14 also localizes to yeast spindle pole bodies (SPBs) in anaphase and dephosphorylates key targets residing on SPBs to allow SPB duplication and prime the MEN. Protein phosphatase 1 (Glc7) with regulatory subunit Bud14 is another phosphatase that plays a key role in the spatiotemporal control of mitotic exit. In this study, we investigated the regulation of Cdc14 localization by Bud14-Glc7.
Materials and methods
UNASSIGNED
We used fluorescence microscopy to analyze Cdc14 localization in
Results
UNASSIGNED
We found that Cdc14 remains at the SPBs longer in
Conclusion
UNASSIGNED
Our results suggest that Glc7-Bud14 is part of a mechanism that promotes Cdc14 disappearance from the dSPB.
Identifiants
pubmed: 39474039
doi: 10.55730/1300-0152.2707
pii: tjb-48-05-308
pmc: PMC11518377
doi:
Types de publication
Journal Article
Langues
eng
Pagination
308-318Informations de copyright
© TÜBİTAK.
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