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C-Terminal End-Directed Protein Elimination by CRL2 Ubiquitin Ligases

Molecular Cell, ISSN: 1097-2765, Vol: 70, Issue: 4, Page: 602-613.e3
2018
  • 116
    Citations
  • 0
    Usage
  • 214
    Captures
  • 0
    Mentions
  • 286
    Social Media
Metric Options:   Counts1 Year3 Year

Metrics Details

  • Citations
    116
  • Captures
    214
  • Social Media
    286
    • Shares, Likes & Comments
      286
      • Facebook
        286

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

Lin, Hsiu-Chuan; Yeh, Chi-Wei; Chen, Yen-Fu; Lee, Ting-Ting; Hsieh, Pei-Yun; Rusnac, Domnita V; Lin, Sung-Ya; Elledge, Stephen J; Zheng, Ning; Yen, Hsueh-Chi S

Elsevier BV

Biochemistry, Genetics and Molecular Biology

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