Wip1 regulates Smad4 phosphorylation and inhibits TGF‐β signaling
| Autor: | Eun Young Kim, Gang-Ho Yoon, Dong-Seok Park, Kyuhee Kim, Peter Cw Lee, Sun-Cheol Choi, Taehyeong Lee, Eun-Ju Chang |
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| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
MAPK/ERK pathway
animal structures Phosphatase Xenopus Xenopus Proteins Biochemistry Dephosphorylation Xenopus laevis 03 medical and health sciences 0302 clinical medicine Transforming Growth Factor beta Genetics Animals Humans News & Views Phosphorylation Protein kinase A Molecular Biology Tissue homeostasis Smad4 Protein 030304 developmental biology 0303 health sciences biology Chemistry Post-translational Modifications Proteolysis & Proteomics Articles biology.organism_classification digestive system diseases Cell biology Protein Phosphatase 2C Mesoderm formation embryonic structures Mitogen-Activated Protein Kinases Development & Differentiation 030217 neurology & neurosurgery Signal Transduction |
| Zdroj: | EMBO Rep EMBO Reports |
| Popis: | Members of the transforming growth factor‐β (TGF‐β) family play key roles in embryogenesis and in maintaining tissue homeostasis, and their perturbation can result in a broad range of diseases. One way TGF‐β family signaling pathways are kept in check is by reversible (de)phosphorylation of intracellular Smad effectors. In this issue of EMBO Reports, Park et al [1] identify the phosphatase wild‐type p53‐induced phosphatase 1 (Wip1) as a negative regulator of TGF‐β family signaling. Mechanistically, Wip1 constrains TGF‐β family signaling through direct dephosphorylation of Thr277, an activating MAP kinase phosphorylation site located in the linker region of the common mediator Smad4. TGF‐β family signaling pathways are regulated by reversible phosphorylation of Smad effectors. A study in this issue identifies the phosphatase Wip1 as a novel negative regulator of TGF‐β signaling. |
| Databáze: | OpenAIRE |
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