Association of AXIN1 assemblies with microtubules inhibits Wnt/β-catenin signaling.

Microtubule binding of AXIN1 drives formation of stable, stationary AXIN1 assemblies that suppress Wnt/β-catenin signaling, with CK1-dependent phosphorylation inhibiting fibrillar tethering.

• Why it matters: Wnt/β-catenin activity depends on AXIN1 recruitment and destruction-complex assembly, but how cytoskeletal structures regulate AXIN1 function and pathway output is unclear.
• What they did: The study shows direct AXIN1–microtubule binding via a positively charged site, spanning peripheral condensates to fibrillar assemblies, and tests effects of CK1-dependent phosphorylation plus pharmacologic/genetic blockade of microtubule binding.
• The result: In multiple cellular systems, inhibiting AXIN1 microtubule binding activates Wnt/β-catenin signaling, and a cell-permeable competitive peptide increases signaling and stimulates Wnt-dependent osteoblast differentiation.

AI summary of the abstract · may contain errors · not medical advice · read the paper.