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Appears in Networks 2

In-Edges 3

a(HBP:"amyloid-beta aggregates") association p(HGNC:CSNK1A1) View Subject | View Object

Isoforms of CK1 are responsible for tau phosphorylation. 129 The enzyme can modulate the activity of γ-secretase and consequently the production of Aβ. PubMed:30444369

a(PUBCHEM:208907) causesNoChange act(p(HGNC:CSNK1A1)) View Subject | View Object

The frentizole scaffold has been combined with the known monoamine oxidase inhibitor (MAOI) ladostigil to identify a molecule that has a dual effect; inhibiting both ABAD and MAO. A library of synthesized derivatives demonstrated that the most potent inhibitor for MAO (IC 50 = 6.34 µM) lacked ABAD inhibition activity. PubMed:30444369

a(PUBCHEM:33334) decreases act(p(HGNC:CSNK1A1)) View Subject | View Object

Screening previously synthesized frentizole derivatives for their efficiency to inhibit CK1 activity as well as ABAD, identified compound 13 which possessed an ABAD IC 50 = 1.67 µM, the most potent inhibitor of this chemotype identified to date. PubMed:30444369

Out-Edges 6

act(p(HGNC:CSNK1A1), ma(kin)) directlyIncreases p(HGNC:MAPT, pmod(Ph, Thr, 17)) View Subject | View Object

Hyperphosphorylation with Prostate-derived sterile 20-like kinase 1 alpha/beta (PSK1/TAOK2), Prostate-derived sterile 20-like kinase 2 (PSK2/TAOK1), CK1. PubMed:25974414

Appears in Networks:

p(HGNC:CSNK1A1) increases p(HGNC:CTNNB1, pmod(Ph, Ser, 35)) View Subject | View Object

The N-terminus of β-catenin has phosphorylation, ubiquitination, and acetylation sites that regulate its stability and signaling. In the absence of a Wnt signal, Ser33, Ser37, and Thr41 are constitutively phosphorylated by glycogen synthase kinase 3β (GSK3β). β-Catenin phosphorylated at these sites is recognized by β-transducin repeat-containing protein (βTrCP), which results in ubiquitination and degradation by the ubiquitin-proteasome pathway. The N-terminal regulatory domain of β-catenin also includes Ser45, a phosphorylation site for Casein Kinase 1α (CK1α) and Lys49, which is acetylated by the acetyltransferase p300/CBP-associated factor (PCAF). The relevance of Lys49 acetylation and Ser45 phosphorylation to the function of β-catenin is an active area of investigation. We find that HDAC6 inhibitors increase Lys49 acetylation and Ser45 phosphorylation but do not affect Ser33, Ser37, and Thr41 phosphorylation. Lys49 acetylation results in decreased ubiquitination of β-catenin in the presence of proteasome inhibition. While increased Lys49 acetylation does not affect total levels of β-catenin, it results in increased membrane localization of β-catenin. PubMed:25546293

Appears in Networks:

p(HGNC:CSNK1A1) increases p(HGNC:MAPT, pmod(Ph)) View Subject | View Object

Isoforms of CK1 are responsible for tau phosphorylation. 129 The enzyme can modulate the activity of γ-secretase and consequently the production of Aβ. PubMed:30444369

p(HGNC:CSNK1A1) regulates act(p(FPLX:"Gamma_secretase")) View Subject | View Object

Isoforms of CK1 are responsible for tau phosphorylation. 129 The enzyme can modulate the activity of γ-secretase and consequently the production of Aβ. PubMed:30444369

p(HGNC:CSNK1A1) association a(HBP:"amyloid-beta aggregates") View Subject | View Object

Isoforms of CK1 are responsible for tau phosphorylation. 129 The enzyme can modulate the activity of γ-secretase and consequently the production of Aβ. PubMed:30444369

About

BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.

If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.