The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Quantitative Analysis of global Ubiquitination in HeLa Cells by Mass Spectrometry
Open accessAbstract
Ubiquitination regulates a host of cellular processes by labeling proteins for degradation, but also by functioning as a regulatory, nonproteolytic posttranslational modification. Proteome-wide strategies to monitor changes in ubiquitination profiles are important to obtain insight into the various cellular functions of ubiquitination. Here we describe generation of stable cell lines expressing a tandem hexahistidine-biotin tag (HB-tag) fused to ubiquitin for two-step purification of the ubiquitinated proteome under fully denaturing conditions. Using this approach we identified 669 ubiquitinated proteins from HeLa cells, including 44 precise ubiquitin attachment sites on substrates and all seven possible ubiquitin chain-linkage types. To probe the dynamics of ubiquitination in response to perturbation of the ubiquitin/proteasome pathway, we combined ubiquitin profiling with quantitative mass spectrometry using the stable isotope labeling with amino acids in cell culture (SILAC) strategy. We compared untreated cells and cells treated with the proteasome inhibitor MG132 to identify ubiquitinated proteins that are targeted to the proteasome for degradation. A number of proteasome substrates were identified. In addition, the quantitative approach allowed us to compare proteasome targeting by different ubiquitin chain topologies in vivo. The tools and strategies described here can be applied to detect changes in ubiquitination dynamics in response to various changes in growth conditions and cellular stress and will contribute to our understanding of the ubiquitin/proteasome system.
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HIFα Targeted for VHL-Mediated Destruction by Proline Hydroxylation: Implications for O 2 Sensing
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Interaction of the Fanconi Anemia Proteins and BRCA1 in a Common Pathway
Garcia-Higuera, I., Taniguchi, T., Ganesan, S., Meyn, M. S., Timmers, C., Hejna, J., Grompe, M., & D'Andrea, A. D. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00173-3 · Cited by 1,198
Global changes to the ubiquitin system in Huntington's disease
Bennett, E. J., Shaler, T. A., Woodman, B., Ryu, K.-Y., Zaitseva, T. S., Becker, C. H., Bates, G. P., Schulman, H., & Kopito, R. R. (2007) · Nature · doi:10.1038/nature06022 · Cited by 497
Mass Spectrometric Characterization of the Affinity-Purified Human 26S Proteasome Complex
Wang, X., Chen, C.-F., Baker, P. R., Chen, P.-L., Kaiser, P., & Huang, L. (2007) · Biochemistry · doi:10.1021/bi061994u · Cited by 260
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The 26S proteasome and initiation of gene transcription.
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Self-citationQuantitative proteomics for the analysis of spatio-temporal protein dynamics during autophagy
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Metadata
- Authors
- Meierhofer, D., Wang, X., Huang, L., & Kaiser, P.
- Venue
- Journal of Proteome Research
- Publisher
- American Chemical Society (ACS)
- Published
- 2008-09-10
- Volume
- 7
- Issue
- 10
- Pages
- 4566-4576
- ISSN
- 1535-3893 (ISSN-L)
- 1535-3907
- OpenAlex
- W1978720506
- Cited by
- 194
- References
- 5
- FWCI
- 7.20
- Type
- journal article
- Language
- en
- Open access
- green
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