Structural basis for recruitment of glycogen synthase kinase 3beta to the axin-APC scaffold complex

Dajani, Rana, Fraser, Elizabeth, Roe, S. Mark, Yeo, Margaret, Good, Valerie M., Thompson, Vivienne, Dale, Trevor Clive ORCID: https://orcid.org/0000-0002-4880-9963 and Pearl, Laurence H. 2003. Structural basis for recruitment of glycogen synthase kinase 3beta to the axin-APC scaffold complex. The EMBO Journal 22 (3) , pp. 494-501. 10.1093/emboj/cdg068

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Abstract

Glycogen synthase kinase 3[beta](GSK3[beta]) is a serine/ threonine kinase involved in insulin, growth factor and Wnt signalling. In Wnt signalling, GSK3[beta] is recruited to a multiprotein complex via interaction with axin, where it hyperphosphorylates b-catenin, marking it for ubiquitylation and destruction. We have now determined the crystal structure of GSK3[beta]in complex with a minimal GSK3[beta]-binding segment of axin, at 2.4 A[superscript o] resolution. The structure confirms the co-localization of the binding sites for axin and FRAT in the C-terminal domain of GSK3[beta], but reveals significant differences in the interactions made by axin and FRAT, mediated by conformational plasticity of the 285

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Biosciences European Cancer Stem Cell Research Institute (ECSCRI)
Subjects:	Q Science > QH Natural history > QH301 Biology
Uncontrolled Keywords:	Beta-catenin ; insulin signalling ; phosphorylation ; signal transduction ; Wnt signalling
ISSN:	14602075
Last Modified:	22 Jun 2023 10:01
URI:	https://orca.cardiff.ac.uk/id/eprint/1090

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