Ethylin Jabs

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Receptor tyrosine kinases activate canonical WNT/β-catenin signaling via MAP kinase/LRP6 pathway and direct β-catenin phosphorylation.

Pavel Krejci; Anie Aklian; Marketa Kaucka; Eva Sevcikova; Jirina Prochazkova; Jan Kukla Masek; Pavol Mikolka; Tereza Pospisilova; Tereza Spoustova; MaryAnn Weis; et al. (Profiled Author: Ethylin Jabs)

Medical Genetics Institute, Cedars-Sinai Medical Center, Los Angeles, California, United States of America. krejcip@sci.muni.cz
PloS one 2012;7(4):e35826.

Receptor tyrosine kinase signaling cooperates with WNT/β-catenin signaling in regulating many biological processes, but the mechanisms of their interaction remain poorly defined. We describe a potent activation of WNT/β-catenin by FGFR2, FGFR3, EGFR and TRKA kinases, which is independent of the PI3K/AKT pathway. Instead, this phenotype depends on ERK MAP kinase-mediated phosphorylation of WNT co-receptor LRP6 at Ser1490 and Thr1572 during its Golgi network-based maturation process. This phosphorylation dramatically increases the cellular response to WNT. Moreover, FGFR2, FGFR3, EGFR and TRKA directly phosphorylate β-catenin at Tyr142, which is known to increase cytoplasmic β-catenin concentration via release of β-catenin from membranous cadherin complexes. We conclude that signaling via ERK/LRP6 pathway and direct β-catenin phosphorylation at Tyr142 represent two mechanisms used by various receptor tyrosine kinase systems to activate canonical WNT signaling.

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