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dc.contributor.authorLuo, W
dc.contributor.authorZou, HY
dc.contributor.authorJin, LH
dc.contributor.authorLin, SY
dc.contributor.author林舒勇
dc.contributor.authorLi, QX
dc.contributor.authorYe, ZY
dc.contributor.authorRui, HL
dc.contributor.authorLin, SC
dc.contributor.author林圣彩
dc.date.accessioned2011-10-07T07:36:48Z
dc.date.available2011-10-07T07:36:48Z
dc.date.issued2005
dc.identifier.citationJ Biol Chem. 2005 Feb 11;280(6):5054-60. Epub 2004 Dec 5.zh_CN
dc.identifier.issn0305-4470
dc.identifier.urihttp://dx.doi.org/doi:10.1074/jbc.M412340200
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/10861
dc.description.abstractAxin is a major scaffold protein, interacting with diverse molecules involved in a number of signaling pathways. Axin can undergo dimer/oligomerization via its DIX domain. Here we show that whereas deletion of the DIX domain at the C terminus rendered Axin incapable of forming dimer, a larger deletion of the C-terminal region restored the ability of Axin to form dimers. Detailed analyses revealed that Axin actually contains two separate domains (D and 1) in addition to the DIX domain for homodimerization. The D,I, and DIX domains alone can form homodimers. Interestingly, D and I domains strongly interact with each other, suggesting that Axin can form an intramolecular structure through D and I interaction in the absence of DIX. We also found that DIX-DIX homodimeric interaction is weak but that point mutations in the DIX domain abolished Axin homodimerization. We propose a model to suggest that Axin forms homodimeric interactions through three domains, D, I, and DIX. More importantly, lack of DIX-DIX interaction caused by point mutations in the DIX domain or deletion causes Axin to form an intramolecular loop through the D and I domains, disallowing homodimer formation. Ccd1 interacts with Axin D domain yet fails to interact with AxinDeltaDIX, confirming that D is masked after D-I looping. The Axin mutants that are defective in homodimer formation fail to activate JNK but have no effect on beta-catenin signaling. Our findings have thus provided a structural basis of conformational changes in Axin, which may underlie the diversity of Axin functions.zh_CN
dc.language.isoenzh_CN
dc.publisherAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INCzh_CN
dc.titleAxin contains three separable domains that confer intramolecular, homodimeric, and heterodimeric interactions involved in distinct functionszh_CN
dc.typeArticlezh_CN


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