IndraLab

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CTNNB1 dephosphorylates CTNNB1. 31 / 31
| 31

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"We use nuclease-free base editing to install a S33F mutation in beta-catenin that blocks beta-catenin phosphorylation, impedes beta-catenin degradation, and upregulates Wnt signaling."

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"Beta-catenin functions as a significant component in the Wnt signaling pathway, and interactions with frizzled and LRP5/6 receptors result in the dephosphorylation of beta-catenin (non phosphorylated active beta-catenin)."

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"Since phosphorylated Axin binds beta-catenin better than unphosphorylated Axin [27], beta-catenin will no longer be recruited to the Axin and GSK-3beta complex, thus preventing beta-catenin phosphoryl[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Together, we could show that PGAM5 released from damaged mitochondria activates Wnt and beta-catenin signaling cell intrinsically via direct dephosphorylation of beta-catenin."

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"Wnt and beta-catenin signaling pathway leads to dephosphorylation, stabilization, and nuclear translocation of beta-catenin."

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"The Wnt and beta-catenin signaling pathway leads to de-phosphorylation, stabilization, and nuclear translocation of beta-catenin."

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"When the pathway is activated, Wnt inhibits β-catenin phosphorylation, which in turn will increase the levels of unphosphorylated β-catenin in the cytoplasm."
| PMC

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"It has been documented that in some CRCs, hyperactive Wnt signaling might result from mutations affecting additional pathway negative regulators AXIN1 [12] and AXIN2 [13], or upon missense mutations in the CTNNB1 gene that impair β-catenin protein N-terminal phosphorylation [14]."

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"SBSN-2 in ESCC cell lines increased the activity of WNT and beta-catenin signalling pathway, which resulted in TCF/LEF transcriptional activity, nuclear translocation and reduced phosphorylation of WNT and beta-catenin, and increased transcript levels of WNT / beta-catenin signalling regulated genes such as AXIN2, MYC, CCND1, FRA1, MMP7 and JUN.."

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"We also show that the core component of the beta-catenin destruction complex, axin, promotes beta-catenin dephosphorylation by Pgam5."

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"This β-catenin isoform increases the stability of full-length β-catenin by antagonizing GSK3β-induced β-catenin phosphorylation and degradation and eventually results in the activation of the Wnt pathway (113)."

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"Canonical Wnt signaling is transduced intracellularly by the interaction of the Dvl DIX protein domain with the β-catenin destruction complex, which prevents β-catenin phosphorylation and degradation (Fiedler et al., 2011; Kimelman and Xu, 2006; Kishida et al., 1999; Wallingford and Habas, 2005)."

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"The B55a subunit directly binds to the beta-catenin destruction complex, where PP2A dephosphorylates beta-catenin and induces its degradation [XREF_BIBR]."

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"In the absence of Wnt signals, this multi protein complex promotes degradation of free beta-catenin via GSK3beta mediated phosphorylation of specific beta-catenin residues; phosphorylated beta-catenin is subsequently ubiquitinated and degraded by the proteasome."

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"Canagliflozin promotes the degradation of beta-catenin via inhibiting PP2A-mediated dephosphorylation of beta-catenin."

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"The following primary antibodies were employed: VE-cadherin (1 : 1000, ab33168, Abcam, USA), β-catenin (1 : 1000, 610154, BD Transduction Laboratories, USA), dephosphorylated active β-catenin (05-665, Millipore, Germany), Sirt3 (1 : 500, ab189860, Abcam, USA), matrix metallopeptidase-7 (MMP-7, 1 : 400, ab5706; Abcam, USA), and cyclooxygenase-2 (COX-2, 1 : 1000, ab62331, Abcam, USA)."

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"MUC1 increases cytoplasmic and nuclear beta-catenin levels by inhibiting GSK3beta mediated phosphorylation and degradation of beta-catenin."

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"Pgam5 dependent stabilization of beta-catenin after hypoxia is in line with CCCP induced beta-catenin dephosphorylation by Pgam5."

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"In the absence of a mitotic signal from outside the cell, beta-catenin is sequestered in a complex with the adenomatous polyposis coli (APC) gene product, a serine threonine glycogen synthetase kinase (GSK-3beta) and an adapter protein axin (or a homologue conductin), enabling phosphorylation and degradation of free beta-catenin by the ubiquitin-proteasome system [XREF_BIBR]."

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"We observed that compared to control cultures, DKK3-overexpressing organoids showed higher level of phosphorylated (inactive) β-catenin and reduced levels of non-phosphorylated (active) β-catenin."

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"In the absence of Wnt, the association of beta-catenin with glycogen synthase kinase 3beta (GSK3beta), Axin, and the adenomatous polyposis coli (APC) protein leads to GSK3beta mediated phosphorylation[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"We examined changes in the expression of beta-catenin target genes and DP signature genes by real-time PCR using hDPCs treated with MPA and/or IFN-gamma for 24 h. Expression of Axin-2 was used as an indicator of beta-catenin signaling pathway activity, which promotes the phosphorylation and degradation of beta-catenin [XREF_BIBR]."

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"Mutations in the N-terminal region of beta-catenin abrogate the phosphorylation of beta-catenin and, subsequently, its degradation."

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"The activation of WNT and beta-catenin inhibits the phosphorylation of beta-catenin and releases it from the destruction complex, which prevents TAZ degradation, resulting in the concomitant beta-catenin and TAZ accumulation."

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"We found that, in addition to the previously implicated Galpha o [XREF_BIBR, XREF_BIBR] and Galpha q [XREF_BIBR, XREF_BIBR], Galpha i2 also inhibited exogenous beta-catenin degradation and phosphorylation of endogenous beta-catenin by GSK3."

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"Dephosphorylation and stabilization of β-catenin is promoted by signal transduction from the fizzled receptor and subsequent localization of β-catenin to the nucleus leading to increased expression of target genes."

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"Degradation of phosphorylated β-catenin limits β-catenin nuclear translocation to inactivate LEF1 translation, resulting in an inhibited Wnt/β-catenin signaling activation."

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"Most beta-catenin pathway activating mutations were missense mutations in exon 3 of CTNNB1 that disrupt phosphorylation of beta-catenin and its ubiquitin mediated degradation, leading to increased beta-catenin levels XREF_BIBR - XREF_BIBR."

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"In normal cells the degradation of beta-catenin is regulated by Wnt signaling : beta-catenin is constitutively phosphorylated by the beta-catenin destruction complex, which marks beta-catenin for ubiquitination followed by rapid proteasomal degradation; Wnt signaling inactivates the beta-catenin destruction complex, thereby inhibiting phosphorylation of beta-catenin and consequently ubiquitination and degradation of the protein."

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"Both phosphorylation of beta-catenin and betaTrCP binding are required for beta-catenin degradation.Abrogation of NH2-terminal phosphorylation of beta-catenin as a result either of oncogenic mutations[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"PTEN phosphorylation by 3MC mediated AhR and RhoA activation increased the proteasomal degradation of beta-catenin through PKCdelta and pGSK3beta mediated beta-catenin phosphorylation; the crucial roles of AhR and RhoA in this process were verified by using gain- or loss-of-function experiments."