Mechanisms of Deubiquitinase Specificity and Regulation
作者： Tycho E.T. Mevissen , David Komander
DOI: 10.1146/ANNUREV-BIOCHEM-061516-044916
关键词: Biology 、 SUMO enzymes 、 Monoubiquitination 、 Ubiquitin ligase 、 Protein ubiquitination 、 Acetylation 、 Biochemistry 、 NEDD8 、 Ubiquitin 、 Cell biology 、 Deubiquitinating enzyme
摘要: Protein ubiquitination is one of the most powerful posttranslational modifications of proteins, as it regulates a plethora of cellular processes in distinct manners. Simple …
sci-hub.se 参考文章(197)
Tingting Yao, Ling Song, Jingji Jin, Yong Cai, Hidehisa Takahashi, Selene K. Swanson, Michael P. Washburn, Laurence Florens, Ronald C. Conaway, Robert E. Cohen, Joan W. Conaway, Distinct Modes of Regulation of the Uch37 Deubiquitinating Enzyme in the Proteasome and in the Ino80 Chromatin-Remodeling Complex Molecular Cell. ,vol. 31, pp. 909- 917 ,(2008) , 10.1016/J.MOLCEL.2008.08.027
Jessica E. Hutti, Rhine R. Shen, Derek W. Abbott, Alicia Y. Zhou, Kam M. Sprott, John M. Asara, William C. Hahn, Lewis C. Cantley, Phosphorylation of the Tumor Suppressor CYLD by the Breast Cancer Oncogene IKKɛ Promotes Cell Transformation Molecular Cell. ,vol. 34, pp. 461- 472 ,(2009) , 10.1016/J.MOLCEL.2009.04.031
Mary E Matyskiela, Gabriel C Lander, Andreas Martin, Conformational switching of the 26S proteasome enables substrate degradation Nature Structural & Molecular Biology. ,vol. 20, pp. 781- 788 ,(2013) , 10.1038/NSMB.2616
Yang Zhen, Philip A. Knobel, Travis H. Stracker, David Reverter, Regulation of USP28 Deubiquitinating Activity by SUMO Conjugation Journal of Biological Chemistry. ,vol. 289, pp. 34838- 34850 ,(2014) , 10.1074/JBC.M114.601849
Shinichiro Nakada, Ikue Tai, Stephanie Panier, Abdallah Al-Hakim, Shun-ichiro Iemura, Yu-Chi Juang, Lara O’Donnell, Ayako Kumakubo, Meagan Munro, Frank Sicheri, Anne-Claude Gingras, Tohru Natsume, Toshio Suda, Daniel Durocher, Non-canonical inhibition of DNA damage-dependent ubiquitination by OTUB1 Nature. ,vol. 466, pp. 941- 946 ,(2010) , 10.1038/NATURE09297
Lina Herhaus, Ana B. Perez-Oliva, Giorgio Cozza, Robert Gourlay, Simone Weidlich, David G. Campbell, Lorenzo A. Pinna, Gopal P. Sapkota, Casein kinase 2 (CK2) phosphorylates the deubiquitylase OTUB1 at Ser16 to trigger its nuclear localization. Science Signaling. ,vol. 8, ,(2015) , 10.1126/SCISIGNAL.AAA0441
Jonathan B. Schaefer, David O. Morgan, Protein-linked Ubiquitin Chain Structure Restricts Activity of Deubiquitinating Enzymes Journal of Biological Chemistry. ,vol. 286, pp. 45186- 45196 ,(2011) , 10.1074/JBC.M111.310094
C. H. Emmerich, A. Ordureau, S. Strickson, J. S. C. Arthur, P. G. A. Pedrioli, D. Komander, P. Cohen, Activation of the canonical IKK complex by K63/M1-linked hybrid ubiquitin chains Proceedings of the National Academy of Sciences of the United States of America. ,vol. 110, pp. 15247- 15252 ,(2013) , 10.1073/PNAS.1314715110
Mark Hochstrasser, Origin and function of ubiquitin-like proteins Nature. ,vol. 458, pp. 422- 429 ,(2009) , 10.1038/NATURE07958
N. L. Samara, A. B. Datta, C. E. Berndsen, X. Zhang, T. Yao, R. E. Cohen, C. Wolberger, Structural insights into the assembly and function of the SAGA deubiquitinating module. Science. ,vol. 328, pp. 1025- 1029 ,(2010) , 10.1126/SCIENCE.1190049