IndraLab

Statements

KCNG1 binds PI3K. 7 / 7
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"In a K13 mutant background, the K13–PI3K interaction may be altered, leading to decreased ubiquitination and increased levels of PI3K, along with its products, for example, the lipid phosphatidylinosi[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
31699532
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"K13 and PI3K associate with the parasite ER and are potentially involved in quality control of exported and cytoplasmic proteins [ xref , xref ]."
32569299
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"A prior report associated ART resistance with elevated PI3P levels, mediated by an interaction between K13 and PI3K. The rise in PI3P levels in mutant parasites was attributed to reduced binding of K13 to PI3K, resulting in attenuated ubiquitin-mediated degradation of the kinase [ xref ]."
32310999
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"K13 could similarly associate with PI3K and promote its degradation."
28688800
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"As a predicted substrate adaptor for the E3 ligase, Pf K13 binds to and ubiquitinates phosphatidylinositol-3-kinase ( Pf PI3K), facilitating its proteasomal degradation."
35420484
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"In ART-resistant parasites harboring mutations in the K13 propeller domains, K13 cannot bind and target PI3K for proteasome-mediated degradation."
28688800
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"Their model of artemisinin mode of action ( xref ) proposes that the interaction between wild-type K13 and PI3K targets the latter for proteosomal degradation."
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