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PMID:10074450
| Citation |
Jaspersen, SL, Charles, JF and Morgan, DO (1999) Inhibitory phosphorylation of the APC regulator Hct1 is controlled by the kinase Cdc28 and the phosphatase Cdc14. Curr. Biol. 9:227-36 |
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| Abstract |
Exit from mitosis requires inactivation of mitotic cyclin-dependent kinases (CDKs). A key mechanism of CDK inactivation is ubiquitin-mediated cyclin proteolysis, which is triggered by the late mitotic activation of a ubiquitin ligase known as the anaphase-promoting complex (APC). Activation of the APC requires its association with substoichiometric activating subunits termed Cdc20 and Hct1 (also known as Cdh1). Here, we explore the molecular function and regulation of the APC regulatory subunit Hct1 in Saccharomyces cerevisiae. |
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| Keywords |
CDC28 Protein Kinase, S cerevisiae/metabolism; Cell Cycle Proteins/metabolism; Enzyme Activation; Fungal Proteins/metabolism; Ligases/metabolism; Mitosis; Phosphoprotein Phosphatases/metabolism; Phosphorylation; Protein Tyrosine Phosphatases; Saccharomyces cerevisiae Proteins; Ubiquitin-Protein Ligase Complexes; Ubiquitin-Protein Ligases |
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Significance
Annotations
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
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References
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