2011
DOI: 10.1074/jbc.m111.248856
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Ubiquitin Ligase Substrate Identification through Quantitative Proteomics at Both the Protein and Peptide Levels

Abstract: Background: Identification of ubiquitin ligase substrates remains an unmet challenge. Results: Two proteomic strategies were used to identify novel substrates of the E3 ligase HRD1. Conclusion: These methods identified populations of substrates enriched for potential targets of endoplasmic reticulumassociated degradation. Significance: This approach should be broadly useful for E3 ligase substrate identification, and the identified substrates provide insight into the role of HRD1 in disease.

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Cited by 78 publications
(63 citation statements)
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“…2D and E), it appears that these proteins may not be positioned appropriately in infected cell nuclei to be conjugated to substrates recruited by the E4-ORF3 protein. Table S3 displays all of the E4-ORF-induced K-ε-GG conjugation sites identified in the present study with overlapping sites within these proteins known to be sites of ubiquitin conjugation identified in large-scale proteomic analyses (22,53,54). The latter two referenced studies utilized the K-ε-GG antibody from Cell Signaling Technology to identify proteins conjugated to ubiquitin and conjugation sites.…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…2D and E), it appears that these proteins may not be positioned appropriately in infected cell nuclei to be conjugated to substrates recruited by the E4-ORF3 protein. Table S3 displays all of the E4-ORF-induced K-ε-GG conjugation sites identified in the present study with overlapping sites within these proteins known to be sites of ubiquitin conjugation identified in large-scale proteomic analyses (22,53,54). The latter two referenced studies utilized the K-ε-GG antibody from Cell Signaling Technology to identify proteins conjugated to ubiquitin and conjugation sites.…”
Section: Discussionmentioning
confidence: 99%
“…Trypsin cleavage of sumoylated substrates linked to this SUMO1 variant resulted in the release of a signature peptide containing a diglycine remnant attached to the amine group of the target lysine residue (K-ε-GG) (21). An antibody was recently described that recognizes the same remnant motif of ubiquitin site conjugation following trypsin digestion, K-ε-GG (22). We engineered a cell line that constitutively expresses His 6 -tagged SUMO3 in which the threonine at position 90 was changed to an arginine residue, SUMO3(T90R).…”
mentioning
confidence: 99%
“…1B) (57)(58)(59)(60)(61)(62)(63). The method is based on a similar strategy originally described for enriching low abundance tyrosine phosphorylated peptides (64) and initially shown to be successful using polyclonal antibodies generated against the -GG signature of ubiquitin (65).…”
Section: Fig 1 Identification Of K-gg Peptidesmentioning
confidence: 99%
“…In patients with lung cancer and thymic carcinoma, the expression level of CTEN mRNA is positively correlated with tumor stage, and high expression is closely related to tumor stage and lymphatic metastasis (Kim et al, 2011;Lee et al, 2011). However, CTEN barely affected the proliferation of SGC7901 cells in this study, as evidenced by the slight influence of the transfecting CTEN-siRNA-1.…”
Section: Discussionmentioning
confidence: 43%