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Identification of a polymorphism in the RING finger of human Bmi-1 that causes its degradation by the ubiquitin-proteasome system.
- Source :
-
FEBS letters [FEBS Lett] 2009 Mar 18; Vol. 583 (6), pp. 960-4. Date of Electronic Publication: 2009 Feb 20. - Publication Year :
- 2009
-
Abstract
- 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.
- Subjects :
- Amino Acid Sequence
Cells, Cultured
Cysteine genetics
Cysteine metabolism
Cysteine Proteinase Inhibitors pharmacology
Humans
Leupeptins pharmacology
Nuclear Proteins chemistry
Polycomb Repressive Complex 1
Protein Denaturation genetics
Protein Processing, Post-Translational drug effects
Protein Processing, Post-Translational genetics
Proto-Oncogene Proteins chemistry
Repressor Proteins chemistry
Transfection
Tyrosine genetics
Ubiquitin metabolism
Nuclear Proteins genetics
Nuclear Proteins metabolism
Polymorphism, Single Nucleotide physiology
Proteasome Endopeptidase Complex metabolism
Proto-Oncogene Proteins genetics
Proto-Oncogene Proteins metabolism
RING Finger Domains genetics
Repressor Proteins genetics
Repressor Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1873-3468
- Volume :
- 583
- Issue :
- 6
- Database :
- MEDLINE
- Journal :
- FEBS letters
- Publication Type :
- Academic Journal
- Accession number :
- 19233177
- Full Text :
- https://doi.org/10.1016/j.febslet.2009.02.023