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Defining the Human Deubiquitinating Enzyme Interaction Landscape

Open access
Sowa, Mathew E., Bennett, Eric J., Gygi, Steven P., Harper, J. Wade·2009·Cell

Abstract

Summary 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 non-reciprocal proteomic datasets. We identified 774 candidate interacting proteins associated with 75 Dubs. Using Gene Ontology, interactome topology classification, sub-cellular 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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Metadata

Authors
Sowa, M. E., Bennett, E. J., Gygi, S. P., & Harper, J. W.
Venue
Cell
Publisher
Elsevier BV
Published
2009-07
Volume
138
Issue
2
Pages
389-403
ISSN
0092-8674 (ISSN-L)
OpenAlex
W2106969933
Cited by
1,512
References
8
FWCI
40.33
Type
journal article
Language
en
Open access
bronze

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Sowa, M. E., Bennett, E. J., Gygi, S. P., & Harper, J. W. (2009). Defining the Human Deubiquitinating Enzyme Interaction Landscape. Cell. https://doi.org/10.1016/j.cell.2009.04.042

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