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      Defining the Human Deubiquitinating Enzyme Interaction Landscape

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      Cell

      Elsevier BV

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          Abstract

          Deubiquitinating enzymes (Dubs) function to remove covalently attached ubiquitin from proteins, thereby controlling substrate activity and/or abundance. For most Dubs, their functions, targets, and regulation are poorly understood. To systematically investigate Dub function, we initiated a global proteomic analysis of Dubs and their associated protein complexes. This was accomplished through the development of a software platform called CompPASS, which uses unbiased metrics to assign confidence measurements to interactions from parallel nonreciprocal proteomic data sets. We identified 774 candidate interacting proteins associated with 75 Dubs. Using Gene Ontology, interactome topology classification, subcellular localization, and functional studies, we link Dubs to diverse processes, including protein turnover, transcription, RNA processing, DNA damage, and endoplasmic reticulum-associated degradation. This work provides the first glimpse into the Dub interaction landscape, places previously unstudied Dubs within putative biological pathways, and identifies previously unknown interactions and protein complexes involved in this increasingly important arm of the ubiquitin-proteasome pathway.

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          Author and article information

          Journal
          Cell
          Cell
          Elsevier BV
          00928674
          July 2009
          July 2009
          : 138
          : 2
          : 389-403
          Article
          10.1016/j.cell.2009.04.042
          2716422
          19615732
          362cfc6e-a3df-4e82-a3ba-ae297c5d6f64
          © 2009

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