Phosphorylation-dependent activity of the deubiquitinase DUBA
- 15 January 2012
- journal article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 19 (2) , 171-175
- https://doi.org/10.1038/nsmb.2206
Abstract
Protease phosphorylation has been reported to affect many signaling pathways connected to proteolytic activity, but the underlying mechanisms have not been clearly elucidated. Structural and biochemical analyses of the deubiquitinase DUBA reveal that phosphorylation is necessary for productive ubiquitin substrate recognition and for enzyme activity.Keywords
This publication has 25 references indexed in Scilit:
- Absent in melanoma 2 is required for innate immune recognition of Francisella tularensisProceedings of the National Academy of Sciences, 2010
- The regulatory crosstalk between kinases and proteases in cancerNature Reviews Cancer, 2010
- Pattern Recognition Receptors and InflammationCell, 2010
- MolProbity: all-atom structure validation for macromolecular crystallographyActa Crystallographica Section D-Biological Crystallography, 2009
- Caspases and Kinases in a Death GripCell, 2009
- Defining the Human Deubiquitinating Enzyme Interaction LandscapeCell, 2009
- Structure of the A20 OTU domain and mechanistic insights into deubiquitinationBiochemical Journal, 2007
- Ubiquitin-binding domainsBiochemical Journal, 2006
- Quantitative production of macrophages or neutrophils ex vivo using conditional Hoxb8Nature Methods, 2006
- Chemistry-Based Functional Proteomics Reveals Novel Members of the Deubiquitinating Enzyme FamilyChemistry & Biology, 2002