期刊
TRENDS IN CELL BIOLOGY
卷 24, 期 6, 页码 352-359出版社
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tcb.2013.12.003
关键词
ubiquitin proteasome system; proteolysis; E1-activating; E2-conjugating; E3-ligase
类别
资金
- Natural Sciences and Engineering Research Council of Canada
- Canada Institutes of Health Research (CIHR)
- CIHR
- Michael Smith Foundation for Health Research
- National Center for Research Resources [5P20RR016464-11]
- National Institute of General Medical Sciences of the National Institutes of Health [8 P20 GM103440-11]
Eukaryotic cells are equipped to degrade proteins via the ubiquitin proteasome system (UPS). Proteins become degraded upon their conjugation to chains of ubiquitin where they are then directed to the 26S proteasome, a macromolecular protease. The transfer of ubiquitin to proteins and their subsequent degradation are highly complex processes, and new research is beginning to uncover the molecular details of how ubiquitination and degradation take place in the cell. We review some of the new data providing insights into how these processes occur. Although distinct mechanisms are often observed, some common themes are emerging for how the UPS guides protein substrates through their final journey.
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