Introduction

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.

Publications

  1. Defining the human deubiquitinating enzyme interaction landscape.
    Cite this
    Sowa ME, Bennett EJ, Gygi SP, Harper JW, 2009-07-01 - Cell

Credits

  1. Mathew E Sowa
    Developer

    Department of Pathology, Harvard Medical School, United States of America

  2. Eric J Bennett
    Developer

  3. Steven P Gygi
    Developer

  4. J Wade Harper
    Investigator

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Summary
AccessionBT006385
Tool TypeApplication
Category
PlatformsLinux/Unix
TechnologiesR
User InterfaceTerminal Command Line
Download Count0
Submitted ByJ Wade Harper