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XB-ART-7309
Cell. March 22, 2002; 108 (6): 837-47.

Control of beta-catenin phosphorylation/degradation by a dual-kinase mechanism.

Liu C , Li Y , Semenov M , Han C , Baeg GH , Tan Y , Zhang Z , Lin X , He X .


Abstract
Wnt regulation of beta-catenin degradation is essential for development and carcinogenesis. beta-catenin degradation is initiated upon amino-terminal serine/threonine phosphorylation, which is believed to be performed by glycogen synthase kinase-3 (GSK-3) in complex with tumor suppressor proteins Axin and adnomatous polyposis coli (APC). Here we describe another Axin-associated kinase, whose phosphorylation of beta-catenin precedes and is required for subsequent GSK-3 phosphorylation of beta-catenin. This "priming" kinase is casein kinase Ialpha (CKIalpha). Depletion of CKIalpha inhibits beta-catenin phosphorylation and degradation and causes abnormal embryogenesis associated with excessive Wnt/beta-catenin signaling. Our study uncovers distinct roles and steps of beta-catenin phosphorylation, identifies CKIalpha as a component in Wnt/beta-catenin signaling, and has implications to pathogenesis/therapeutics of human cancers and diabetes.

PubMed ID: 11955436
Article link: Cell.

Genes referenced: gsk3b gys1
Antibodies referenced:

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