RBR ligase–mediated ubiquitin transfer: a tale with many twists and turns
Author:
Publisher
Springer Science and Business Media LLC
Subject
Molecular Biology,Structural Biology
Link
http://www.nature.com/articles/s41594-018-0063-3.pdf
Reference57 articles.
1. Berndsen, C. E. & Wolberger, C. New insights into ubiquitin E3 ligase mechanism. Nat. Struct. Mol. Biol. 21, 301–307 (2014).
2. Spratt, D. E., Walden, H. & Shaw, G. S. RBR E3 ubiquitin ligases: new structures, new insights, new questions. Biochem. J. 458, 421–437 (2014).
3. Marín, I., Lucas, J. I., Gradilla, A. C. & Ferrús, A. Parkin and relatives: the RBR family of ubiquitin ligases. Physiol. Genomics 17, 253–263 (2004).
4. Wenzel, D. M., Lissounov, A., Brzovic, P. S. & Klevit, R. E. UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. Nature 474, 105–108 (2011). This study was the first to find that the RBR ligase family operates through a catalytic cysteine. This pioneering study distinguished the RBRs as a class of their own and provided the basis for understanding RBR regulation.
5. Chaugule, V. K. et al. Autoregulation of Parkin activity through its ubiquitin-like domain. EMBO J. 30, 2853–2867 (2011).
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