The hippo tumor pathway promotes TAZ degradation by phosphorylating a phosphodegron and recruiting the SCF{beta}-TrCP E3 ligase.

The TAZ transcription co-activator promotes cell proliferation and epithelial-mesenchymal transition. TAZ is inhibited by the Hippo tumor suppressor pathway, which promotes TAZ cytoplasmic localization by phosphorylation. We report here that TAZ protein stability is controlled by a phosphodegron recognized by the F-box protein β-TrCP and ubiquitylated by the SCF/CRL1(β-TrCP) E3 ...
ligase. The interaction between TAZ and β-TrCP is regulated by the Hippo pathway. Phosphorylation of a phosphodegron in TAZ by LATS primes it for further phosphorylation by CK1ε and subsequent binding by β-TrCP. Therefore, the Hippo pathway negatively regulates TAZ function by both limiting its nuclear accumulation and promoting its degradation. The phosphodegron-mediated TAZ degradation plays an important role in negatively regulating TAZ biological functions.
Mesh Terms:
Animals, Casein Kinase I, Drosophila Proteins, HEK293 Cells, Humans, Intracellular Signaling Peptides and Proteins, Mice, NIH 3T3 Cells, Phosphorylation, Protein Binding, Protein Stability, Protein-Serine-Threonine Kinases, SKP Cullin F-Box Protein Ligases, Signal Transduction
J. Biol. Chem.
Date: Nov. 26, 2010
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