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- W2897795455 abstract "β-Catenin functions as an adherens junction protein for cell–cell adhesion and as a signaling protein. β-catenin function is dependent on its stability, which is regulated by protein–protein interactions that stabilize β-catenin or target it for proteasome-mediated degradation. In this study, we show that β-catenin stability is regulated by intracellular pH (pHi) dynamics, with decreased stability at higher pHi in both mammalian cells and Drosophila melanogaster. β-Catenin degradation requires phosphorylation of N-terminal residues for recognition by the E3 ligase β-TrCP. While β-catenin phosphorylation was pH independent, higher pHi induced increased β-TrCP binding and decreased β-catenin stability. An evolutionarily conserved histidine in β-catenin (found in the β-TrCP DSGIHS destruction motif) is required for pH-dependent binding to β-TrCP. Expressing a cancer-associated H36R–β-catenin mutant in the Drosophila eye was sufficient to induce Wnt signaling and produced pronounced tumors not seen with other oncogenic β-catenin alleles. We identify pHi dynamics as a previously unrecognized regulator of β-catenin stability, functioning in coincidence with phosphorylation." @default.
- W2897795455 created "2018-10-26" @default.
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- W2897795455 date "2018-10-12" @default.
- W2897795455 modified "2023-09-25" @default.
- W2897795455 title "β-Catenin is a pH sensor with decreased stability at higher intracellular pH" @default.
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- W2897795455 doi "https://doi.org/10.1083/jcb.201712041" @default.
- W2897795455 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6219716" @default.
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