Deubiquitinating enzymes

Soon after it was shown that ubiquitin is conjugated to proteins, it was determined that this was a reversible process and deubiquitinating enzymes, or DUBs, could remove ubiquitin from ubiquitinated proteins [18, 19]. As the genes for ubiquitin and ubiquitin-like proteins were identified it became clear that all ubiquitin family members were synthesized as proproteins and processed to reveal the C-terminal glycylglycine of the active proteins [20]. Based on this information, DUBs were defined as proteases that cleave at the C-terminus of ubiquitin or ubiquitin-like proteins to reverse conjugation to target proteins and also process the proproteins. 

Wilkinson, K. D. Regulation of ubiquitin-dependent processes by deubiquitinating enzymes, Faseb J, 1997, 3 3, 1245-56. 

Larsen, C. N., Krantz, B. A., and Wilkinson, K. D. Substrate specificity of deubiquitinating enzymes ubiquitin C-terminal hydrolases. Biochemistry, 1998, 37, 3358-68. 

Dang, L. C., Melandri, F. D., and Stein, R. L. Kinetic and mechanistic studies on the hydrolysis of ubiquitin C-terminal 7-amido-4-methylcoumarin by deubiquitinating enzymes. Biochemistry, 1998, 37, 1868—79. 

Wing, S. S. Deubiquitinating enzymes - the importance of driving in reverse along the ubiquitin-proteasome pathway, Int J Biochem Cell Biol, 2003, 35, 590-605. 

Borodovsky, A., OvAA, H., Kolli, N., Gan-Erdene, T., Wilkinson, K. D., Ploegh, H. L., and Kessler, B. M. Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme family, Chem Biol,... 

J. A. A specific protein substrate for a deubiquitinating enzyme Liquid facets is the substrate of Fat facets. Genes Dev, 2002, 36, 289-94. 

Kato, M., Miyazawa, K., and Kitamuea, N. a deubiquitinating enzyme UBPY interacts with the Src homology 3 domain of Hrs-binding protein via a novel binding motif PX(V/I)(D/N)RXXKP, J Biol Chem, 2000, 275, 37481-7. 

Kinner, a. and Rolling, R. The yeast deubiquitinating enzyme Ubpl6 is anchored to the outer mitochondrial membrane, FEES Lett, 2003, 549, 135-40. 

Wang, Y., Satoh, A., Warren, G., and Meyer, H. H. VGIP135 acts as a deubiquitinating enzyme during p97-p47-mediated reassembly of mitotic Golgi fragments, / CeU Biol, 2004, 164, 973-8. 

SWAMINATHAN, S., AmERIK, A. Y., and Hochstrasser, M. The Doa4 deubiquitinating enzyme is required for ubiquitin homeostasis in yeast. 

Moazed, D. and Johnson, D. A deubiquitinating enzyme interacts with SIR4 and regulates silencing in S. cerevisiae. Cell, 1996, 86, 667-77. 

The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the humun tre-2 oncogene. Nature 1993, 366, 313-319. 

Papa, F. R., Ameeik, A., and Hochsteassee, M. Interaction of the Doa4 deubiquitinating enzyme with the yeast 26S proteasome. Mol. Biol. Cell 1999, 10, 741-756. 

M. The Doa4 deubiquitinating enzyme is functionally linked to the vacuolar protein-sorting and endocytic pathways. Mol Biol. Cell 2000, 7 7, 3365-3380. 

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