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| [[Image:1t08.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1t08| PDB=1t08 | SCENE= }} | | {{STRUCTURE_1t08| PDB=1t08 | SCENE= }} |
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| '''Crystal structure of beta-catenin/ICAT helical domain/unphosphorylated APC R3'''
| | ===Crystal structure of beta-catenin/ICAT helical domain/unphosphorylated APC R3=== |
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| ==Overview==
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| The transcriptional coactivator beta-catenin mediates Wnt growth factor signaling. In the absence of a Wnt signal, casein kinase 1 (CK1) and glycogen synthase kinase-3beta (GSK-3beta) phosphorylate cytosolic beta-catenin, thereby flagging it for recognition and destruction by the ubiquitin/proteosome machinery. Phosphorylation occurs in a multiprotein complex that includes the kinases, beta-catenin, axin, and the Adenomatous Polyposis Coli (APC) protein. The role of APC in this process is poorly understood. CK1epsilon and GSK-3beta phosphorylate APC, which increases its affinity for beta-catenin. Crystal structures of phosphorylated and nonphosphorylated APC bound to beta-catenin reveal a phosphorylation-dependent binding motif generated by mutual priming of CK1 and GSK-3beta substrate sequences. Axin is shown to act as a scaffold for substrate phosphorylation by these kinases. Phosphorylated APC and axin bind to the same surface of, and compete directly for, beta-catenin. The structural and biochemical data suggest a novel model for how APC functions in beta-catenin degradation. | | The line below this paragraph, {{ABSTRACT_PUBMED_15327768}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15327768 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15327768}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Wnt signal]] | | [[Category: Wnt signal]] |
| [[Category: Wnt signaling]] | | [[Category: Wnt signaling]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:20:30 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:32:31 2008'' |
