Lysine 269 is essential for cyclin D1 ubiquitylation by the SCFFbx4/αB-crystallin ligase and subsequent proteasome-dependent degradation
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cancer Research,Genetics,Molecular Biology
Link
http://www.nature.com/articles/onc2009287.pdf
Reference26 articles.
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2. Barbash O, Zamfirova P, Lin DI, Chen X, Yang K, Nakagawa H et al. (2008). Mutations in Fbx4 inhibit dimerization of the SCF(Fbx4) ligase and contribute to cyclin d1 overexpression in human cancer. Cancer Cell 14: 68–78.
3. Benzeno S, Lu F, Guo M, Barbash O, Zhang F, Herman JG et al. (2006). Identification of mutations that disrupt phosphorylation-dependent nuclear export of cyclin D1. Oncogene 25: 6291–6303.
4. Bloom J, Amador V, Bartolini F, DeMartino G, Pagano M . (2003). Proteasome-mediated degradation of p21 via N-terminal ubiquitinylation. Cell 115: 71–82.
5. Breitschopf K, Bengal E, Ziv T, Admon A, Ciechanover A . (1998). A novel site for ubiquitination: the N-terminal residue, and not internal lysines of MyoD, is essential for conjugation and degradation of the protein. EMBO J 17: 5964–5973.
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