C-Terminal End-Directed Protein Elimination by CRL2 Ubiquitin Ligases
Molecular Cell, ISSN: 1097-2765, Vol: 70, Issue: 4, Page: 602-613.e3
2018
- 116Citations
- 214Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations116
- Citation Indexes116
- 116
- CrossRef106
- Captures214
- Readers214
- 214
Article Description
The proteolysis-assisted protein quality control system guards the proteome from potentially detrimental aberrant proteins. How miscellaneous defective proteins are specifically eliminated and which molecular characteristics direct them for removal are fundamental questions. We reveal a mechanism, DesCEND (destruction via C-end degrons), by which CRL2 ubiquitin ligase uses interchangeable substrate receptors to recognize the unusual C termini of abnormal proteins (i.e., C-end degrons). C-end degrons are mostly less than ten residues in length and comprise a few indispensable residues along with some rather degenerate ones. The C-terminal end position is essential for C-end degron function. Truncated selenoproteins generated by translation errors and the USP1 N-terminal fragment from post-translational cleavage are eliminated by DesCEND. DesCEND also targets full-length proteins with naturally occurring C-end degrons. The C-end degron in DesCEND echoes the N-end degron in the N-end rule pathway, highlighting the dominance of protein “ends” as indicators for protein elimination.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S1097276518302764; http://dx.doi.org/10.1016/j.molcel.2018.04.006; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85046790523&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/29775578; https://linkinghub.elsevier.com/retrieve/pii/S1097276518302764; https://dx.doi.org/10.1016/j.molcel.2018.04.006
Elsevier BV
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