DUBs, the regulation of cell identity and disease.

作者: Johanna Heideker , Ingrid E Wertz , None

DOI: 10.1042/BJ20140496

关键词: UbiquitinGeneticsDNA repairDrug discoverySignallingComputational biologyBiologyUbiquitin-Specific ProteasesFunction (biology)Cell signalingProteolysis

摘要: The post-translational modification of proteins with ubiquitin represents a complex signalling system that co-ordinates essential cellular functions, including proteolysis, DNA repair, receptor and cell communication. DUBs (deubiquitinases), the enzymes disassemble chains remove from proteins, are central to this system. Reflecting complexity versatility signalling, DUB activity is controlled in multiple ways. Although several lines evidence indicate aberrant function may promote human disease, underlying molecular mechanisms often unclear. Notwithstanding, considerable interest as potential drug targets has emerged over past years. future success DUB-based therapy development will require connecting basic science enzymology discovery. In present review, we discuss new insights into regulation their links focusing on role regulators identity differentiation, emerging targets.

参考文章(322)
David Komander, Mechanism, Specificity and Structure of the Deubiquitinases Sub-cellular biochemistry. ,vol. 54, pp. 69- 87 ,(2010) , 10.1007/978-1-4419-6676-6_6
Régine Mariage-Samson, Jana Hillova, Leslie Boghosian-Sell, Kay Huebner, Miroslav Hill, Carlo M. Croce, Tatsuya Nakamura, Myriam Onno, Linda A. Cannizzaro, A novel transcriptional unit of the tre oncogene widely expressed in human cancer cells. Oncogene. ,vol. 7, pp. 733- 741 ,(1992)
Fumiyo Ikeda, Simin Rahighi, Soichi Wakatsuki, Ivan Dikic, Selective Binding of Linear Ubiquitin Chains to NEMO in NF-kappaB Activation Advances in Experimental Medicine and Biology. ,vol. 691, pp. 107- 114 ,(2011) , 10.1007/978-1-4419-6612-4_11
Muthu K. Shanmugam, Gautam Sethi, Role of Epigenetics in Inflammation-Associated Diseases Subcellular Biochemistry. ,vol. 61, pp. 627- 657 ,(2013) , 10.1007/978-94-007-4525-4_27
Conjugation and deconjugation of ubiquitin family modifiers Landes Bioscience , Springer Science+Business Media. ,(2010) , 10.1007/978-1-4419-6676-6
Graham R Bignell, William Warren, Sheila Seal, Meiko Takahashi, Elizabeth Rapley, Rita Barfoot, Helen Green, Carolanne Brown, Patrick J Biggs, Sunil R Lakhani, Christopher Jones, Juliana Hansen, Edward Blair, Benedikt Hofmann, Reiner Siebert, Gwen Turner, D Gareth Evans, Connie Schrander-Stumpel, Frits A Beemer, Ans Van Den Ouweland, Dicky Halley, Bertrand Delpech, Mark G Cleveland, Irene Leigh, Jaakko Leisti, Sonja Rasmussen, Margaret R Wallace, Christiane Fenske, Piu Banerjee, Naoki Oiso, Ranbir Chaggar, Samantha Merrett, Niamh Leonard, Marcel Huber, Daniel Hohl, Pam Chapman, John Burn, Sally Swift, Anna Smith, Alan Ashworth, Michael R Stratton, None, Identification of the familial cylindromatosis tumour-suppressor gene. Nature Genetics. ,vol. 25, pp. 160- 165 ,(2000) , 10.1038/76006
Anthony C. Bishop, Jeffrey A. Ubersax, Dejah T. Petsch, Dina P. Matheos, Nathanael S. Gray, Justin Blethrow, Eiji Shimizu, Joe Z. Tsien, Peter G. Schultz, Mark D. Rose, John L. Wood, David O. Morgan, Kevan M. Shokat, A chemical switch for inhibitor-sensitive alleles of any protein kinase Nature. ,vol. 407, pp. 395- 401 ,(2000) , 10.1038/35030148
Vered Maytal-Kivity, Noa Reis, Kay Hofmann, Michael H Glickman, MPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function BMC Biochemistry. ,vol. 3, pp. 28- 28 ,(2002) , 10.1186/1471-2091-3-28
Beatrice Coornaert, Mathijs Baens, Karen Heyninck, Tine Bekaert, Mira Haegman, Jens Staal, Lijun Sun, Zhijian J Chen, Peter Marynen, Rudi Beyaert, T cell antigen receptor stimulation induces MALT1 paracaspase–mediated cleavage of the NF-κB inhibitor A20 Nature Immunology. ,vol. 9, pp. 263- 271 ,(2008) , 10.1038/NI1561