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- W4311632368 abstract "Abstract N-terminal phosphorylation at residues T3 and S13 is believed to have important beneficial implications for the biological and pathological properties of mutant huntingtin, where IKBKB was identified as a candidate regulator of huntingtin N-terminal phosphorylation. The paucity of mechanistic information on IKK pathways, together with the lack of sensitive methods to quantify endogenous huntingtin phosphorylation, prevented detailed study of the role of IKBKB in Huntington’s disease. Using novel ultrasensitive assays, we demonstrate that IKBKB can regulate endogenous S13 huntingtin phosphorylation in a manner dependent on its kinase activity and known regulators. We found that the ability of IKBKB to phosphorylate endogenous huntingtin S13 is mediated through a non-canonical IRF3-mediated IKK-pathway, distinct from the established involvement of IKBKB in mutant huntingtin’s pathological mechanisms mediated via the canonical pathway. Furthermore, increased huntingtin S13 phosphorylation by IKBKB resulted in decreased aggregation of mutant huntingtin in cells, again dependent on its kinase activity. These findings point to a non-canonical IKK-pathway linking S13 huntingtin phosphorylation to the pathological properties of mutant huntingtin aggregation, thought to be significant to Huntington’s disease." @default.
- W4311632368 created "2022-12-27" @default.
- W4311632368 creator A5013451369 @default.
- W4311632368 creator A5039055702 @default.
- W4311632368 creator A5044285886 @default.
- W4311632368 creator A5053444203 @default.
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- W4311632368 creator A5074445567 @default.
- W4311632368 creator A5076050728 @default.
- W4311632368 creator A5079753774 @default.
- W4311632368 date "2022-12-05" @default.
- W4311632368 modified "2023-10-16" @default.
- W4311632368 title "IKBKB reduces huntingtin aggregation by phosphorylating Serine 13 via a non-canonical IKK pathway" @default.
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