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Signal‐induced ubiquitination of p57Kip2 is independent of the C‐terminal consensus Cdk phosphorylation site
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The cyclin‐dependent kinase inhibitor p57Kip2 is required for normal mouse embryonic development. p57Kip2 consists of four structurally distinct domains in which the conserved C‐terminal nuclear targeting domain contains a putative Cdk phosphorylation site (Thr342) that shares a great similitude in the adjacent sequences with p27Kip1 but not with p21Cip1. Phosphorylation on Thr187 has been shown to promote degradation of p27Kip1. Although there is sequence homology between the C‐terminal part of p27Kip1 and p57Kip2, we show that the ubiquitination and degradation of p57Kip2 are independent of Thr342. In contrast a destabilizing element located in the N‐terminal is implicated in p57Kip2 destabilization.
Title: Signal‐induced ubiquitination of p57Kip2 is independent of the C‐terminal consensus Cdk phosphorylation site
Description:
The cyclin‐dependent kinase inhibitor p57Kip2 is required for normal mouse embryonic development.
p57Kip2 consists of four structurally distinct domains in which the conserved C‐terminal nuclear targeting domain contains a putative Cdk phosphorylation site (Thr342) that shares a great similitude in the adjacent sequences with p27Kip1 but not with p21Cip1.
Phosphorylation on Thr187 has been shown to promote degradation of p27Kip1.
Although there is sequence homology between the C‐terminal part of p27Kip1 and p57Kip2, we show that the ubiquitination and degradation of p57Kip2 are independent of Thr342.
In contrast a destabilizing element located in the N‐terminal is implicated in p57Kip2 destabilization.
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