Clb6/Cdc28 and Cdc14 regulate phosphorylation status and cellular localization of Swi6
| Autor: | Stephen J. Smerdon, Marco Geymonat, Glenn P. Wells, Steven G. Sedgwick, Ad Spanos |
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| Rok vydání: | 2004 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Genes Fungal Cyclin B Active Transport Cell Nucleus Cell Cycle Proteins Saccharomyces cerevisiae Models Biological Dephosphorylation Serine Nucleocytoplasmic Communication Phosphorylation Nuclear export signal Molecular Biology Serine/threonine-specific protein kinase Cyclin-dependent kinase 1 biology Cdc14 Cell Cycle Cell Biology Cell biology Biochemistry Mutation biology.protein Nuclear transport Protein Tyrosine Phosphatases CDC28 Protein Kinase S cerevisiae Transcription Factors |
| Zdroj: | Molecular and cellular biology. 24(6) |
| ISSN: | 0270-7306 |
| Popis: | Nuclear export of the transcription factor Swi6 during the budding yeast Saccharomyces cerevisiae cell cycle is known to require phosphorylation of the Swi6 serine 160 residue. We show that Clb6/Cdc28 kinase is required for this nuclear export. Furthermore, Cdc28 combined with the S-phase cyclin Clb6 specifically phosphorylates serine 160 of Swi6 in vitro. Nuclear import of Swi6 occurs concomitantly with dephosphorylation of serine 160 in late M phase. We show that Cdc14 phosphatase, the principal effector of the mitotic exit network, can trigger nuclear import of Swi6 in vivo and that Cdc14 dephosphorylates Swi6 at serine 160 in vitro. Taken together, these observations show how Swi6 dephosphorylation and phosphorylation are integrated into changes of Cdc28 activity governing entry and exit from the G1 phase of the cell cycle. |
| Databáze: | OpenAIRE |
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