The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
Mass Spectrometric Analysis of Lysine Ubiquitylation Reveals Promiscuity at Site Level
Open accessAbstract
The covalent attachment of ubiquitin to proteins regulates numerous processes in eukaryotic cells. Here we report the identification of 753 unique lysine ubiquitylation sites on 471 proteins using higher-energy collisional dissociation on the LTQ Orbitrap Velos. In total 5756 putative ubiquitin substrates were identified. Lysine residues targeted by the ubiquitin-ligase system show no unique sequence feature. Surface accessible lysine residues located in ordered secondary regions, surrounded by smaller and positively charged amino acids are preferred sites of ubiquitylation. Lysine ubiquitylation shows promiscuity at the site level, as evidenced by low evolutionary conservation of ubiquitylation sites across eukaryotic species. Among lysine modifications a significant overlap (20%) between ubiquitylation and acetylation at site level highlights extensive competitive crosstalk among these modifications. This site-specific crosstalk is not prevalent among cell cycle ubiquitylations. Between SUMOylation and ubiquitylation the preferred interaction is through mixed-chain conjugation. Overall these data provide novel insights into the site-specific selection and regulatory function of lysine ubiquitylation.
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Cites
Cox, J., & Mann, M. (2008) · Nature Biotechnology · doi:10.1038/nbt.1511 · Cited by 14,855
Lysine acetylation targets protein complexes and co-regulates major cellular functions
Choudhary, C., Kumar, C., Gnad, F., Nielsen, M. L., Rehman, M., Walther, T. C., Olsen, J. V., & Mann, M. (2009) · Science · doi:10.1126/science.1175371 · Cited by 4,040
Self-citationMethylation of histone H3 lysine 9 creates a binding site for HP1 proteins
Lachner, M., O'Carroll, D., Rea, S., Mechtler, K., & Jenuwein, T. (2001) · Nature · doi:10.1038/35065132 · Cited by 2,868
RING Domain E3 Ubiquitin Ligases
Deshaies, R. J., & Joazeiro, C. A. P. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.101807.093809 · Cited by 2,679
How Proteolysis Drives the Cell Cycle
King, R. W., Deshaies, R. J., Peters, J.-M., & Kirschner, M. W. (1996) · Science · doi:10.1126/science.274.5293.1652 · Cited by 1,273
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
MDM2–HDAC1-mediated deacetylation of p53 is required for its degradation
Ito, A., Kawaguchi, Y., Lai, C., Kovacs, J. J., Higashimoto, Y., Appella, E., & Yao, T. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf616 · Cited by 570
Tabb, D. L., Vega-Montoto, L., Rudnick, P. A., Variyath, A. M., Ham, A.-J. L., Bunk, D. M., Kilpatrick, L. E., Billheimer, D. D., Blackman, R. K., Cardasis, H. L., et al. (2010) · Journal of Proteome Research · doi:10.1021/pr9006365 · Cited by 551
A dual pressure linear ion trap orbitrap instrument with very high sequencing speed
Olsen, J. V., Schwartz, J. C., Griep-Raming, J., Nielsen, M. L., Damoc, E., Denisov, E., Lange, O., Remes, P., Taylor, D., Splendore, M., et al. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m900375-mcp200 · Cited by 464
Self-citationMotegi, A., Liaw, H.-J., Lee, K.-Y., Roest, H. P., Maas, A., Wu, X., Moinova, H., Markowitz, S. D., Ding, H., Hoeijmakers, J. H. J., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805685105 · Cited by 304 · cited 1×
“Taken together, substrate recognition in the ubiquitin process relies upon the specificity of E2 and E3 enzymes (53), either through the substrate recognition specificity of E3 or through a gained specificity by combinatorial interactions between E2 and E3 (54).”
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Cited by
Systematic and Quantitative Assessment of the Ubiquitin-Modified Proteome
Kim, W., Bennett, E. J., Huttlin, E. L., Guo, A., Li, J., Possemato, A., Sowa, M. E., Rad, R., Rush, J., Comb, M. J., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.08.025 · Cited by 1,613
Wagner, S. A., Beli, P., Weinert, B. T., Nielsen, M. L., Cox, J., Mann, M., & Choudhary, C. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.013284 · Cited by 889
Self-citationQuantitative, High-Resolution Proteomics for Data-Driven Systems Biology
Cox, J., & Mann, M. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061308-093216 · Cited by 685
A comprehensive compilation of SUMO proteomics
Hendriks, I. A., & Vertegaal, A. C. O. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.81 · Cited by 514
Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation
Hendriks, I. A., Lyon, D., Young, C., Jensen, L. J., Vertegaal, A. C. O., & Nielsen, M. L. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3366 · Cited by 382
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Metadata
- Authors
- Danielsen, J. M. R., Sylvestersen, K. B., Bekker-Jensen, S., Szklarczyk, D., Poulsen, J. W., Horn, H., Jensen, L. J., Mailand, N., & Nielsen, M. L.
- Venue
- Molecular & Cellular Proteomics
- Publisher
- Elsevier BV
- Published
- 2011-03
- Volume
- 10
- Issue
- 3
- Pages
- M110.003590
- ISSN
- 1535-9476 (ISSN-L)
- OpenAlex
- W2169543816
- Cited by
- 318
- References
- 11
- FWCI
- 9.45
- Type
- journal article
- Language
- en
- Open access
- hybrid
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