A C2HC zinc finger is essential for the RING-E2 interaction of the ubiquitin ligase RNF125-Reference-Cited by-同舟云学术

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A C2HC zinc finger is essential for the RING-E2 interaction of the ubiquitin ligase RNF125

Published:2016-07-14 Issue:1 Volume:6 Page:
ISSN:2045-2322
Container-title:Scientific Reports
language:en
Short-container-title:Sci Rep

Author:

Bijlmakers Marie-José,Teixeira João M. C.,Boer Roeland,Mayzel Maxim,Puig-Sàrries Pilar,Karlsson Göran,Coll Miquel,Pons Miquel,Crosas Bernat

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/srep29232.pdf

Reference57 articles.

1. Komander, D. & Rape, M. The ubiquitin code. Annu. Rev. Biochem. 81, 203–229 (2012).

2. Pickart, C. M. & Eddins, M. J. Ubiquitin: structures, functions, mechanisms. Biochim. Biophys. Acta. 1695, 55–72 (2004).

3. Berndsen, C. E. & Wolberger, C. New insights into ubiquitin E3 ligase mechanism. Nat. Struct. Mol. Biol. 21, 301–307 (2014).

4. Deshaies, R. J. & Joazeiro, C. A. P. RING domain E3 ubiquitin ligases. Annu. Rev. Biochem. 78, 399–434 (2009).

5. Dou, H., Buetow, L., Sibbet, G. J., Cameron, K. & Huang, D. T. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. Nat. Struct. Mol. Biol. 19, 876–883 (2012).

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3. A novel RNF125 variant associated with Tenorio syndrome alters ubiquitin chain binding;Clinical Genetics;2023-11-20

4. Multiple E3 ligases control tankyrase stability and function;Nature Communications;2023-11-08

5. Zinc finger 1 of the RING E3 ligase, RNF125, interacts with the E2 to enhance ubiquitylation;Structure;2023-10

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