Document Detail

From rabbit reticulocytes to clam oocytes: in search of the system that targets mitotic cyclins for degradation.
MedLine Citation:
PMID:  20335505     Owner:  NLM     Status:  MEDLINE    
By the late 1980s, the basic biochemistry of ubiquitin-mediated protein degradation had already been elucidated by studies that used reticulocyte lysates. However, the scope and biological functions of this system remained largely obscure. Therefore, I became interested at that time in the mechanisms by which mitotic cyclins are degraded in exit from mitosis. Using a cell-free system from clam oocytes that faithfully reproduced cell cycle stage-specific degradation of cyclins, we identified in 1995 a large ubiquitin ligase complex that targets mitotic cyclins for degradation. Subsequent studies in many laboratories showed that this ubiquitin ligase, now called the anaphase-promoting complex/cyclosome, has centrally important roles in many aspects of cell cycle control.
Avram Hershko
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Publication Detail:
Type:  Biography; Historical Article; Journal Article; Review     Date:  2010-03-24
Journal Detail:
Title:  Molecular biology of the cell     Volume:  21     ISSN:  1939-4586     ISO Abbreviation:  Mol. Biol. Cell     Publication Date:  2010 May 
Date Detail:
Created Date:  2010-05-14     Completed Date:  2010-08-30     Revised Date:  2010-09-30    
Medline Journal Info:
Nlm Unique ID:  9201390     Medline TA:  Mol Biol Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1645-7     Citation Subset:  IM    
Unit of Biochemistry, the Rappaport Faculty of Medicine, Technion-Israel Institute of Technology, Haifa, Israel.
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MeSH Terms
Bivalvia / metabolism*
Cell Cycle
Cell-Free System / metabolism
Cyclins / history*,  metabolism*
History, 20th Century
History, 21st Century
Ligases / history,  metabolism
Oocytes / cytology,  metabolism
Reticulocytes / metabolism
Ubiquitin / history,  metabolism
Ubiquitin-Protein Ligase Complexes
Reg. No./Substance:
0/Cyclins; 0/Ubiquitin; EC 6.-/Ligases; EC Ligase Complexes; EC complex
Personal Name Subject
Personal Name Subject:
Avram Hershko

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