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- W1978793039 abstract "Cyclin E, an activator of cyclin-dependent kinase 2 (Cdk2), is targeted for proteasomal degradation by phosphorylation-dependent multiubiquitylation via the ubiquitin ligase SCFhCdc4. SCF ubiquitin ligases are composed of a core of conserved subunits and one variable subunit (an F box protein) involved in substrate recognition. We show here that multiubiquitylation of cyclin E requires the sequential function of two distinct splice variant isoforms of the F box protein hCdc4 known as α and γ. SCFhCdc4α binds a complex containing cyclin E, Cdk2, and the prolyl cis/trans isomerase Pin1 and promotes the activity of Pin1 without directly ubiquitylating cyclin E. However, due to the action of this SCFhCdc4α-Pin1 complex, cyclin E becomes an efficient ubiquitylation substrate of SCFhCdc4γ. Furthermore, in the context of Cdc4α and cyclin E, mutational data suggest that Pin1 isomerizes a noncanonical proline-proline bond, with the possibility that Cdc4α may serve as a cofactor for altering the specificity of Pin1." @default.
- W1978793039 created "2016-06-24" @default.
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- W1978793039 date "2006-07-01" @default.
- W1978793039 modified "2023-10-17" @default.
- W1978793039 title "Ubiquitylation of Cyclin E Requires the Sequential Function of SCF Complexes Containing Distinct hCdc4 Isoforms" @default.
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- W1978793039 doi "https://doi.org/10.1016/j.molcel.2006.05.020" @default.
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