NDLI: The first armadillo repeat is involved in the recognition and regulation of β-catenin phosphorylation by protein kinase CK1

Content Provider	PubMed Central
Author	Bustos, Victor H. Ferrarese, Anna Andrea, Venerando Marin, Oriano Allende, Jorge E. Pinna, Lorenzo A.
Copyright Year	2006
Abstract	Multiple phosphorylation of β-catenin by glycogen synthase kinase 3 (GSK3) in the Wnt pathway is primed by CK1 through phosphorylation of Ser-45, which lacks a typical CK1 canonical sequence. Synthetic peptides encompassing amino acids 38–64 of β-catenin are phosphorylated by CK1 on Ser-45 with low affinity (K m ≈1 mM), whereas intact β-catenin is phosphorylated at Ser-45 with very high affinity (K m ≈200 nM). Peptides extended to include a putative CK1 docking motif (FXXXF) at 70–74 positions or a F74AA mutation in full-length β-catenin had no significant effect on CK1 phosphorylation efficiency. β-Catenin C-terminal deletion mutants up to residue 181 maintained their high affinity, whereas removal of the 131–181 fragment, corresponding to the first armadillo repeat, was deleterious, resulting in a 50-fold increase in K m value. Implication of the first armadillo repeat in β-catenin targeting by CK1 is supported in that the Y142E mutation, which mimics phosphorylation of Tyr-142 by tyrosine kinases and promotes dissociation of β-catenin from α-catenin, further improves CK1 phosphorylation efficiency, lowering the K m value to <50 nM, approximating the physiological concentration of β-catenin. In contrast, α-catenin, which interacts with the N-terminal region of β-catenin, prevents Ser-45 phosphorylation of CK1 in a dose-dependent manner. Our data show that the integrity of the N-terminal region and the first armadillo repeat are necessary and sufficient for high-affinity phosphorylation by CK1 of Ser-45. They also suggest that β-catenin association with α-catenin and β-catenin phosphorylation by CK1 at Ser-45 are mutually exclusive.
Related Links	http://dx.doi.org/10.1073/pnas.0609424104
Starting Page	19725
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	52
Volume Number	103
Language	English
Publisher	National Academy of Sciences
Publisher Date	2006-12-26
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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