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- _7 value "Inhibition of either KPC1 or KPC2 by RNA interference or with dominant-negative mutants delays p27 degradation at the G0 G1 transition . These results indicate that the degradation of p27 is regulated by two distinct mechanisms: translocation-coupled cytoplasmic ubiquitylation by KPC at the G0 G1 transition and nuclear ubiquitylation by SKP2 during S and G2 phases (see Supplementary information S2 (figure)). Given that, in a subset of breast cancers (32 out of 84 samples)45, p27 levels were low despite SKP2 not being expressed, it remains possible that the expression of KPC might be elevated in such cases. Surprisingly, SKP2 also binds to MYC through its MB2 and helix loop helix leucine zipper (HLHZip) domains, and thereby mediates its ubiquitylation and degradation. However, SKP2 unexpectedly increases the transactivation activity of MYC, indicating that SKP2 is a transcriptional cofactor. Consistent with this notion, MYC accumulates, but its transcriptional activity is reduced, in mouse Skp2 ko cells." provenance.
- _7 wasQuotedFrom 16633365 provenance.