Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation.

By P. Xu, D. Duong, N. Seyfried, Dongmei Cheng, Yang Xie, J. Robert, John Rush, M. Hochstrasser, D. Finley, Junmin Peng. Cell, 2009

1,173 citations recorded by the source corpus.

Subfields: Cell Biology, Epidemiology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/59fb1cd7b122188fc7037a616f39ed0423cfa654

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In Cell Biology

1. Ivan Dikic
2. Gabriel Lander
3. A. Goldberg
4. Sharad Kumar
5. M. Rapé
6. G. Collins
7. D. Komander

In Epidemiology

1. Ivan Dikic
2. D. Komander
3. A. Goldberg
4. Sharad Kumar
5. M. Rapé
6. G. Collins
7. I. Slaninová

In Molecular Biology

1. D. Komander
2. M. Rapé
3. Ivan Dikic
4. S. Urbé
5. M. J. Clague
6. Gabriel Lander
7. Soichi Wakatsuki
8. Wenyi Wei

Citations in the corpus

• The Logic of the 26S Proteasome. (2017, positive): “Because ESCRT proteins are not in the nucleus, the fates of nuclear K63-linked proteins remain unknown, although proteasomal degradation seems likely considering the high concentrations of 26S in nuclei (Wójcik and DeMartino, 2003).”
• The ubiquitin code. (2012, background): “Alternatively, ubiquitylation can occur at endosomal membranes to control localization after internalization.”
• Insights in Post-Translational Modifications: Ubiquitin and SUMO (2022, background): “Together with K48 linkages, K11 and K63 linkages are known as the most abundant ubiquitin chains in cells, being K48 the canonical ubiquitin chains for protein degradation by the proteasome [67,68].”
• Breaking the chains: structure and function of the deubiquitinases (2009, background): “, whereas Lys48-linked polyubiquitin chains and probably most other ubiquitin linkages can target the protein for proteasomal degradatio”
• Ubiquitin-binding domains — from structures to functions (2009, background): “In yeast, an increase was observed upon proteasome inhibition for all ubiquitin linkages except Lys63, which was shown to be the only linkage that does not have a role in proteasomal degradatio”
• Physiological functions of the HECT family of ubiquitin ligases (2009, background): “A recent report demonstrates that polyubiquitin chains through all Lys residues in ubiquitin, except Lys63, may target proteins for degradation by the proteasome, and Lys11-linked substrates are specifically involved in the endoplasmic reticulum-associated degradation (ERAD) pathwa”
• The role of ubiquitination in tumorigenesis and targeted drug discovery (2020, background): “With the deepening of research, scientists have realized that K48-type polyubiquitination is only the tip of the ubiquitination iceberg.(23,38,39) To date, eight types of polyubiquitin linkages have been identified (K6, K11, K27, K29, K33, K48, K63 and Met1) with specific functions.”
• Complete subunit architecture of the proteasome regulatory particle (2012, positive): “While it has been shown that efficient degradation depends on the length, linkage type, and placement of an ubiquitin chain, as well as the presence of an unstructured initiation site on a substrate 3,18,19 , we are missing the topological information needed to explain these requirements.”