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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 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
Subjects: Q Science > QH Natural history > QH301 Biology
Uncontrolled Keywords: Beta-catenin ; insulin signalling ; phosphorylation ; signal transduction ; Wnt signalling
ISSN: 14602075
Last Modified: 04 Jun 2017 01:38
URI: http://orca.cf.ac.uk/id/eprint/1090

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