Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction-Reference-Cited by-同舟云学术

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Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction

Published:2008-05 Issue:7194 Volume:453 Page:548-552
ISSN:0028-0836
Container-title:Nature
language:en
Short-container-title:Nature

Author:

Schreiner Patrick,Chen Xiang,Husnjak Koraljka,Randles Leah,Zhang Naixia,Elsasser Suzanne,Finley Daniel,Dikic Ivan,Walters Kylie J.,Groll Michael

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/nature06924.pdf

Reference29 articles.

1. Deveraux, Q., Ustrell, V., Pickart, C. & Rechsteiner, M. A 26 S protease subunit that binds ubiquitin conjugates. J. Biol. Chem. 269, 7059–7061 (1994)

2. Fu, H. et al. Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26 S proteasome subunit Mcb1. J. Biol. Chem. 273, 1970–1981 (1998)

3. Jorgensen, J. P. et al. Adrm1, a putative cell adhesion regulating protein, is a novel proteasome-associated factor. J. Mol. Biol. 360, 1043–1052 (2006)

4. Yao, T. et al. Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1. Nature Cell Biol. 8, 994–1002 (2006)

5. Hamazaki, J. et al. A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes. EMBO J. 25, 4524–4536 (2006)

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