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Successive Phosphorylation of p27(KIP1) Protein at Serine-10 and C Terminus Crucially Controls Its Potency to Inactivate Cdk2
During the G(1)-S transition, the activity of Cdk2 is regulated by its association with p27(KIP1), which in rodent fibroblasts undergoes phosphorylation mainly at serine 10, threonine 187, and C-terminal threonine 197 by KIS, Cdk2, and Pim or ROCK, respectively. Recently Cdc6 the AAA+ ATPase, identi...
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| Main Authors: | , , , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado: |
American Society for Biochemistry and Molecular Biology
2012
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| Assuntos: | |
| Acceso en liña: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3381138/ https://ncbi.nlm.nih.gov/pubmed/22584582 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M112.346254 |
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