Axin-mediated CKI phosphorylation of β-catenin at Ser 45: a molecular switch for the Wnt pathway

Genes and Development - Tập 16 Số 9 - Trang 1066-1076 - 2002
Sharon Amit1, Ada Hatzubai1, Yaara Birman1, Jens Andersen2, Etti Ben-Shushan1, Matthias Mann2, Yinon Ben‐Neriah1, Irit Alkalay1
1The Lautenberg Center for Immunology, The Hebrew University-Hadassah Medical School Jerusalem 91120 Israel
2Protein Interaction Laboratory, University of Southern Denmark, DK-5230 Odense M, Denmark

Tóm tắt

The Wnt pathway controls numerous developmental processes via the β-catenin–TCF/LEF transcription complex. Deregulation of the pathway results in the aberrant accumulation of β-catenin in the nucleus, often leading to cancer. Normally, cytoplasmic β-catenin associates with APC and axin and is continuously phosphorylated by GSK-3β, marking it for proteasomal degradation. Wnt signaling is considered to prevent GSK-3β from phosphorylating β-catenin, thus causing its stabilization. However, the Wnt mechanism of action has not been resolved. Here we study the regulation of β-catenin phosphorylation and degradation by the Wnt pathway. Using mass spectrometry and phosphopeptide-specific antibodies, we show that a complex of axin and casein kinase I (CKI) induces β-catenin phosphorylation at a single site: serine 45 (S45). Immunopurified axin and recombinant CKI phosphorylate β-catenin in vitro at S45; CKI inhibition suppresses this phosphorylation in vivo. CKI phosphorylation creates a priming site for GSK-3β and is both necessary and sufficient to initiate the β-catenin phosphorylation–degradation cascade. Wnt3A signaling and Dvl overexpression suppress S45 phosphorylation, thereby precluding the initiation of the cascade. Thus, a single, CKI-dependent phosphorylation event serves as a molecular switch for the Wnt pathway.

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