AI Article Synopsis
- The β-catenin destruction complex, which regulates β-catenin levels, is formed from various proteins including Axin, APC, GSK3β, and CK1α.
- The assembly of this complex is influenced by a process called liquid-liquid phase separation (LLPS), primarily driven by an intrinsically disordered region in Axin.
- This phase separation allows Axin to act as a scaffold, effectively recruiting other proteins like GSK3β and β-catenin, which is essential for proper phosphorylation and stability of β-catenin, thereby affecting Wnt/β-catenin signaling.
Article Abstract
In Wnt/β-catenin signaling, the β-catenin protein level is deliberately controlled by the assembly of the multiprotein β-catenin destruction complex composed of Axin, adenomatous polyposis coli (APC), glycogen synthase kinase 3β (GSK3β), casein kinase 1α (CK1α), and others. Here we provide compelling evidence that formation of the destruction complex is driven by protein liquid-liquid phase separation (LLPS) of Axin. An intrinsically disordered region in Axin plays an important role in driving its LLPS. Phase-separated Axin provides a scaffold for recruiting GSK3β, CK1α, and β-catenin. APC also undergoes LLPS in vitro and enhances the size and dynamics of Axin phase droplets. The LLPS-driven assembly of the destruction complex facilitates β-catenin phosphorylation by GSK3β and is critical for the regulation of β-catenin protein stability and thus Wnt/β-catenin signaling.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7931644 | PMC |
| http://dx.doi.org/10.1083/jcb.202012112 | DOI Listing |
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