Ubiquitin-binding domains — from structures to functions

作者: Ivan Dikic , Soichi Wakatsuki , Kylie J. Walters

DOI: 10.1038/NRM2767

关键词: UbiquitinCell biologyUbiquitin bindingProtein structureContext (language use)Structure–activity relationshipSequence (biology)Proteins metabolismExtramuralBiochemistryBiology

摘要: Ubiquitin-binding domains (UBDs) are modular elements that bind non-covalently to the protein modifier ubiquitin. Recent atomic-level resolution structures of ubiquitin-UBD complexes have revealed some mechanisms underlie versatile functions ubiquitin in vivo. The preferences UBDs for chains specific length and linkage central these functions. These originate from multimeric interactions, whereby synergistically multiple molecules, contacts with regions link molecules into a polymer. sequence context conformational changes follow their binding also contribute signalling. new structure-based insights provide strategies controlling cellular processes by targeting interfaces.

参考文章(123)
Pier Paolo Di Fiore, Simona Polo, Kay Hofmann, When ubiquitin meets ubiquitin receptors: a signalling connection Nature Reviews Molecular Cell Biology. ,vol. 4, pp. 491- 497 ,(2003) , 10.1038/NRM1124
Q. Deveraux, V. Ustrell, C. Pickart, M. Rechsteiner, A 26 S protease subunit that binds ubiquitin conjugates. Journal of Biological Chemistry. ,vol. 269, pp. 7059- 7061 ,(1994) , 10.1016/S0021-9258(17)37244-7
Tatiana G. Ortolan, Prasad Tongaonkar, David Lambertson, Li Chen, Cherylene Schauber, Kiran Madura, The DNA repair protein rad23 is a negative regulator of multi-ubiquitin chain assembly. Nature Cell Biology. ,vol. 2, pp. 601- 608 ,(2000) , 10.1038/35023547
Bonnie L. Bertolaet, Duncan J. Clarke, Meira Wolff, Mark H. Watson, Martha Henze, Gilles Divita, Steven I. Reed, UBA domains of DNA damage-inducible proteins interact with ubiquitin. Nature Structural & Molecular Biology. ,vol. 8, pp. 417- 422 ,(2001) , 10.1038/87575
Masato Kawasaki, Tomoo Shiba, Yoko Shiba, Yoshiki Yamaguchi, Naohiro Matsugaki, Noriyuki Igarashi, Mamoru Suzuki, Ryuichi Kato, Koichi Kato, Kazuhisa Nakayama, Soichi Wakatsuki, Molecular mechanism of ubiquitin recognition by GGA3 GAT domain. Genes to Cells. ,vol. 10, pp. 639- 654 ,(2005) , 10.1111/J.1365-2443.2005.00865.X
Yasushi Saeki, Aki Saitoh, Akio Toh-e, Hideyoshi Yokosawa, Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis. Biochemical and Biophysical Research Communications. ,vol. 293, pp. 986- 992 ,(2002) , 10.1016/S0006-291X(02)00340-6
Errol C. Friedberg, Alan R. Lehmann, Robert P.P. Fuchs, Trading places: how do DNA polymerases switch during translesion DNA synthesis? Molecular Cell. ,vol. 18, pp. 499- 505 ,(2005) , 10.1016/J.MOLCEL.2005.03.032
B. Sobhian, G. Shao, D. R. Lilli, A. C. Culhane, L. A. Moreau, B. Xia, D. M. Livingston, R. A. Greenberg, RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage sites. Science. ,vol. 316, pp. 1198- 1202 ,(2007) , 10.1126/SCIENCE.1139516
Richard S Kang, Cynthia M Daniels, Smitha A Francis, Susan C Shih, William J Salerno, Linda Hicke, Ishwar Radhakrishnan, Solution Structure of a CUE-Ubiquitin Complex Reveals a Conserved Mode of Ubiquitin Binding Cell. ,vol. 113, pp. 621- 630 ,(2003) , 10.1016/S0092-8674(03)00362-3
Hyoung Tae Kim, Kwang Pyo Kim, Fernando Lledias, Alexei F. Kisselev, K. Matthew Scaglione, Dorota Skowyra, Steven P. Gygi, Alfred L. Goldberg, Certain pairs of ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s) synthesize nondegradable forked ubiquitin chains containing all possible isopeptide linkages. Journal of Biological Chemistry. ,vol. 282, pp. 17375- 17386 ,(2007) , 10.1074/JBC.M609659200