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doi: 10.1016/j.str.2008.02.005.Terminal regions of beta-catenin come into view
- PMID:18334207
- PMCID: PMC2329800
- DOI: 10.1016/j.str.2008.02.005
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Comment
Terminal regions of beta-catenin come into view
Cara J Gottardi et al. Structure.2008 Mar.
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Abstract
β-catenin is remarkably multifunctional, acting in adhesion, cytoskeletal regulation, and Wnt signaling. In this issue, Xing et al. (2008) present the full-length structure of β-catenin, providing a clearer picture of how these terminal regions modulate β-catenin activities.
Figures
(A) Line diagram of β-catenin arm repeat and terminal regions with key binding partners. (B) Structure of full-length β-catenin revealing HelixC (red); unstructured N- and C-terminal regions shown as dotted lines. See Xing et al. (2008) for details.
Comment on
- Crystal structure of a full-length beta-catenin.Xing Y, Takemaru K, Liu J, Berndt JD, Zheng JJ, Moon RT, Xu W.Xing Y, et al.Structure. 2008 Mar;16(3):478-87. doi: 10.1016/j.str.2007.12.021.Structure. 2008.PMID:18334222Free PMC article.
References
- Bellipanni G, Varga M, Maegawa S, Imai Y, Kelly C, Myers AP, Chu F, Talbot WS, Weinberg ES. Development. 2006;133:1299–1309. - PubMed
- Castano J, Raurell I, Piedra JA, Miravet S, Dunach M, Garcia de Herreros A. J. Biol. Chem. 2002;277:31541–31550. - PubMed
- Choi HJ, Huber AH, Weis WI. J. Biol. Chem. 2006;281:1027–1038. - PubMed
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