| Identification of a polymorphism in the RING finger of human Bmi-1 that causes its degradation by the ubiquitin-proteasome system. | |
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MedLine Citation:
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PMID: 19233177 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Bmi-1 is a polycomb protein that plays an important role in tumor cell development and maintaining stem cell populations of many cell lineages. Here we identify a polymorphism in human Bmi-1 that changes a cysteine within its RING domain to tyrosine. This C18Y polymorphism is associated with a significant decrease in Bmi-1 level and its elevated ubiquitination, suggesting that it is being destroyed by the ubiquitin-proteasome system. Consistent with this, treating cells with the proteasome inhibitor MG-132 significantly increases C18Y Bmi-1 levels. This is the first example of a polymorphism in Bmi-1 that reduces levels of this important protein. |
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Authors:
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Jie Zhang; Kevin D Sarge |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural Date: 2009-02-20 |
Journal Detail:
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Title: FEBS letters Volume: 583 ISSN: 1873-3468 ISO Abbreviation: FEBS Lett. Publication Date: 2009 Mar |
Date Detail:
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Created Date: 2009-03-16 Completed Date: 2009-04-13 Revised Date: 2011-09-26 |
Medline Journal Info:
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Nlm Unique ID: 0155157 Medline TA: FEBS Lett Country: Netherlands |
Other Details:
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Languages: eng Pagination: 960-4 Citation Subset: IM |
Affiliation:
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Graduate Center for Toxicology, Chandler Medical Center, University of Kentucky, Lexington, KY 40536, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Cells, Cultured Cysteine / genetics, metabolism Cysteine Proteinase Inhibitors / pharmacology Humans Leupeptins / pharmacology Nuclear Proteins / chemistry, genetics*, metabolism* Polymorphism, Single Nucleotide* / physiology Proteasome Endopeptidase Complex / metabolism* Protein Denaturation / genetics Protein Processing, Post-Translational / drug effects, genetics Proto-Oncogene Proteins / chemistry, genetics*, metabolism* RING Finger Domains / genetics* Repressor Proteins / chemistry, genetics*, metabolism* Transfection Tyrosine / genetics Ubiquitin / metabolism |
| Grant Support | |
ID/Acronym/Agency:
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GM64606/GM/NIGMS NIH HHS; R01 GM064606-02/GM/NIGMS NIH HHS; R01 GM064606-03/GM/NIGMS NIH HHS; R01 GM064606-04/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Cysteine Proteinase Inhibitors; 0/Leupeptins; 0/Nuclear Proteins; 0/Proto-Oncogene Proteins; 0/Repressor Proteins; 0/Ubiquitin; 133407-82-6/benzyloxycarbonylleucyl-leucyl-leucine aldehyde; 138791-04-5/BMI1 protein, human; 52-90-4/Cysteine; 55520-40-6/Tyrosine; EC 3.4.25.1/Proteasome Endopeptidase Complex |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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