The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Defining the Human Deubiquitinating Enzyme Interaction Landscape
Open accessAbstract
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
BioGRID: a general repository for interaction datasets
Stark, C. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkj109 · Cited by 3,960
One step at a time: endoplasmic reticulum-associated degradation
Vembar, S. S., & Brodsky, J. L. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2546 · Cited by 1,299
Toward a Comprehensive Atlas of the Physical Interactome of Saccharomyces cerevisiae
Collins, S. R., Kemmeren, P., Zhao, X.-C., Greenblatt, J. F., Spencer, F., Holstege, F. C. P., Weissman, J. S., & Krogan, N. J. (2007) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m600381-mcp200 · Cited by 795
Abraxas and RAP80 Form a BRCA1 Protein Complex Required for the DNA Damage Response
Wang, B., Matsuoka, S., Ballif, B. A., Zhang, D., Smogorzewska, A., Gygi, S. P., & Elledge, S. J. (2007) · Science · doi:10.1126/science.1139476 · Cited by 695
Self-citationZhang, X.-Y., Varthi, M., Sykes, S. M., Phillips, C., Warzecha, C., Zhu, W., Wyce, A., Thorne, A. W., Berger, S. L., & McMahon, S. B. (2008) · Molecular Cell · doi:10.1016/j.molcel.2007.12.015 · Cited by 427
Cope, G. A., & Deshaies, R. J. (2003) · Cell · doi:10.1016/s0092-8674(03)00722-0 · Cited by 409
Kikkert, M., Doolman, R., Dai, M., Avner, R., Hassink, G., van Voorden, S., Thanedar, S., Roitelman, J., Chau, V., & Wiertz, E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307453200 · Cited by 384
Wang, B., Hurov, K., Hofmann, K., & Elledge, S. J. (2009) · Genes & Development · doi:10.1101/gad.1770309 · Cited by 172
Research works printed but not linked: 36
- Bellare, 2008, A role for ubiquitin in the spliceosome assembly pathway, Nat. Struct. Mol. Biol., 15, 444, 10.1038/nsmb.1401 · DOI
- Bennett, 2005, Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation, Mol. Cell, 17, 351, 10.1016/j.molcel.2004.12.021 · DOI · Paper page
- Braun, 2009, An experimentally derived confidence score for binary protein-protein interactions, Nat. Methods, 6, 91, 10.1038/nmeth.1281 · DOI · Paper page
- Cohn, 2007, A UAF1-containing multisubunit protein complex regulates the Fanconi anemia pathway, Mol. Cell, 28, 786, 10.1016/j.molcel.2007.09.031 · DOI · Paper page
- Cohn, 2008, UAF1 is a subunit of multiple deubiquitinating enzyme complexes, J. Biol. Chem.
- Cusick, 2009, Literature-curated protein interaction datasets, Nat. Methods, 6, 39, 10.1038/nmeth.1284 · DOI · Paper page
- DeLaBarre, 2006, Central pore residues mediate the p97/VCP activity required for ERAD, Mol. Cell, 22, 451, 10.1016/j.molcel.2006.03.036 · DOI · Paper page
- Ewing, 2007, Large-scale mapping of human protein-protein interactions by mass spectrometry, Mol. Syst. Biol., 3, 89, 10.1038/msb4100134 · DOI · Paper page
- Futschik, 2007, Comparison of human protein-protein interaction maps, Bioinformatics, 23, 605, 10.1093/bioinformatics/btl683 · DOI
- Gavin, 2002, Functional organization of the yeast proteome by systematic analysis of protein complexes, Nature, 415, 141, 10.1038/415141a · DOI · Paper page
- Jeronimo, 2007, Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme, Mol. Cell, 27, 262, 10.1016/j.molcel.2007.06.027 · DOI · Paper page
- Kraft, 2008, Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease, Nat. Cell Biol., 10, 602, 10.1038/ncb1723 · DOI · Paper page
- Krogan, 2006, Global landscape of protein complexes in the yeast Saccharomyces cerevisiae, Nature, 440, 637, 10.1038/nature04670 · DOI · Paper page
- Liu, 2004, A model for random sampling and estimation of relative protein abundance in shotgun proteomics, Anal. Chem., 76, 4193, 10.1021/ac0498563 · DOI · Paper page
- Lu, 2009, USP19 deubiquitinating enzyme supports cell proliferation by stabilizing KPC1, a ubiquitin ligase for p27Kip1, Mol. Cell. Biol., 29, 547, 10.1128/MCB.00329-08 · DOI
- Malhotra, 2007, The endoplasmic reticulum and the unfolded protein response, Semin. Cell Dev. Biol., 18, 716, 10.1016/j.semcdb.2007.09.003 · DOI · Paper page
- Mendoza, 2007, PHLPPing it off: phosphatases get in the Akt, Mol. Cell, 25, 798, 10.1016/j.molcel.2007.03.007 · DOI
- Nicassio, 2007, Human USP3 is a chromatin modifier required for S phase progression and genome stability, Curr. Biol., 17, 1972, 10.1016/j.cub.2007.10.034 · DOI · Paper page
- Nijman, 2005, The deubiquitinating enzyme USP1 regulates the Fanconi anemia pathway, Mol. Cell, 17, 331, 10.1016/j.molcel.2005.01.008 · DOI · Paper page
- Nijman, 2005, A genomic and functional inventory of deubiquitinating enzymes, Cell, 123, 773, 10.1016/j.cell.2005.11.007 · DOI · Paper page
- Pickart, 2004, Proteasomes and their kin: proteases in the machine age, Nat. Rev. Mol. Cell Biol., 5, 177, 10.1038/nrm1336 · DOI · Paper page
- Pijnappel, 2008, Dubbing SAGA unveils new epigenetic crosstalk, Mol. Cell, 29, 152, 10.1016/j.molcel.2008.01.007 · DOI
- Rumpf, 2006, Functional division of substrate processing cofactors of the ubiquitin-selective Cdc48 chaperone, Mol. Cell, 21, 261, 10.1016/j.molcel.2005.12.014 · DOI · Paper page
- Sardiu, 2008, Probabilistic assembly of human protein interaction networks from label-free quantitative proteomics, Proc. Natl. Acad. Sci. USA, 105, 1454, 10.1073/pnas.0706983105 · DOI · Paper page
- Sobhian, 2007, RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage sites, Science, 316, 1198, 10.1126/science.1139516 · DOI · Paper page
- Stegmeier, 2007, Anaphase initiation is regulated by antagonistic ubiquitination and deubiquitination activities, Nature, 446, 876, 10.1038/nature05694 · DOI · Paper page
- Stegmeier, 2007, The tumor suppressor CYLD regulates entry into mitosis, Proc. Natl. Acad. Sci. USA, 104, 8869, 10.1073/pnas.0703268104 · DOI
- Sun, 2008, Deubiquitylation and regulation of the immune response, Nat. Rev. Immunol., 8, 501, 10.1038/nri2337 · DOI · Paper page
- Trippe, 2006, Identification, cloning, and functional analysis of the human U6 snRNA-specific terminal uridylyl transferase, RNA, 12, 1494, 10.1261/rna.87706 · DOI
- Uchiyama, 2002, VCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivo, J. Cell Biol., 159, 855, 10.1083/jcb.200208112 · DOI · Paper page
- Ventii, 2008, Protein partners of deubiquitinating enzymes, Biochem. J., 414, 161, 10.1042/BJ20080798 · DOI · Paper page
- Wang, 2006, Regulation of retrotranslocation by p97-associated deubiquitinating enzyme ataxin-3, J. Cell Biol., 174, 963, 10.1083/jcb.200605100 · DOI · Paper page
- Wang, 2008, Inhibition of p97-dependent Protein Degradation by Eeyarestatin I, J. Biol. Chem., 283, 7445, 10.1074/jbc.M708347200 · DOI · Paper page
- Zhang, 2006, A Role for the Deubiquitinating Enzyme USP28 in Control of the DNA-Damage Response, Cell, 126, 529, 10.1016/j.cell.2006.06.039 · DOI · Paper page
- Zhang, 2003, Transcriptional regulation by histone ubiquitination and deubiquitination, Genes Dev., 17, 2733, 10.1101/gad.1156403 · DOI · Paper page
- Zhao, 2008, A TFTC/STAGA module mediates histone H2A and H2B deubiquitination, coactivates nuclear receptors, and counteracts heterochromatin silencing, Mol. Cell, 29, 92, 10.1016/j.molcel.2007.12.011 · DOI · Paper page
Cited by
Komander, D., & Rape, M. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060310-170328 · Cited by 3,679
Quantitative proteomics identifies NCOA4 as the cargo receptor mediating ferritinophagy
Mancias, J. D., Wang, X., Gygi, S. P., Harper, J. W., & Kimmelman, A. C. (2014) · Nature · doi:10.1038/nature13148 · Cited by 2,084
Self-citationBreaking the chains: structure and function of the deubiquitinases
Komander, D., Clague, M. J., & Urbé, S. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2731 · Cited by 1,969
Network organization of the human autophagy system
Behrends, C., Sowa, M. E., Gygi, S. P., & Harper, J. W. (2010) · Nature · doi:10.1038/nature09204 · Cited by 1,554
Self-citationThe Molecular Mechanisms Regulating the KEAP1-NRF2 Pathway
Baird, L., & Yamamoto, M. (2020) · Molecular and Cellular Biology · doi:10.1128/mcb.00099-20 · Cited by 1,542
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
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 1477 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Defining the Human Deubiquitinating Enzyme Interaction Landscape. https://app.cochat.ai/papers/10.1016/j.cell.2009.04.042
- The paper
- 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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.