Phosphorylated Tyr142 β-catenin localizes to centrosomes and is regulated by Syk

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2018-04-01
Author
Bhardwaj, Deepshikha
Nàger Grifo, Mireia
Visa Pretel, Anna
Crespí Sallán, Marta
Coopman, PJ
Cantí Nicolás, Carles
Herreros Danés, Judit
Suggested citation
Bhardwaj, Deepshikha; Nàger Grifo, Mireia; Visa Pretel, Anna; Crespí Sallán, Marta; Coopman, PJ; Cantí Nicolás, Carles; Herreros Danés, Judit; . (2018) . Phosphorylated Tyr142 β-catenin localizes to centrosomes and is regulated by Syk. Journal of Cellular Biochemistry, 2018, vol. 119, núm. 4, p. 3632-3640. https://doi.org/10.1002/jcb.26571.
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Abstract
β-catenin is a central component of adherent junctions and a key effector of canonical Wnt signalling, in which dephosphorylated Ser/Thr β-catenin regulates gene transcription. β-catenin phosphorylation at Tyr142 (PTyr142 β-catenin), which is induced by receptor and Src family Tyr kinases, represents a previously described β- catenin switch from adhesive to migratory roles. In addition to classical β-catenin roles, phosphorylated Ser/Thr β-catenin and total β-catenin were involved in centrosomal functions, including mitotic spindle formation and centrosome separation. Here we find that PTyr142 β-catenin is present in centrosomes in non-transformed and glioblastoma cells and that, in contrast to the Ser/Thr phosphorylated β-catenin, PTyr142 β-catenin centrosomal levels drop in mitosis. Furthermore, we show that the inhibitor of Spleen Tyrosine Kinase (Syk) piceatannol decreases centrosomal PTyr142 β-catenin levels, indicating that Syk regulates centrosome PTyr142 β-catenin. Our findings suggest that PTyr142 β-catenin negatively regulates mitotic progression and highlight the contribution of different phosphorylated β-catenin forms in the coordination of the cell and centrosome cycles.
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http://hdl.handle.net/10459.1/67598
DOI
https://doi.org/10.1002/jcb.26571
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Journal of Cellular Biochemistry, 2018, vol. 119, núm. 4, p. 3632-3640
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