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Pin1 Catalyzes Conformational Changes of Thr-187 in p27(Kip1) and Mediates Its Stability through a Polyubiquitination Process
The cis-trans peptidylprolyl isomerase Pin1 plays a critical role in regulating a subset of phosphoproteins by catalyzing conformational changes on the phosphorylated Ser/Thr-Pro motifs. The phosphorylation-directed ubiquitination is one of the major mechanisms to regulate the abundance of p27(Kip1)...
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Main Authors: | , , , , , , , , |
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Format: | Artigo |
Language: | Inglês |
Published: |
American Society for Biochemistry and Molecular Biology
2009
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Subjects: | |
Online Access: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2781992/ https://ncbi.nlm.nih.gov/pubmed/19584057 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M109.022814 |
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