期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 285, 期 33, 页码 25831-25840出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M110.112128
关键词
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资金
- Fonds de la Recherche Scientifique (FNRS)
- TELEVIE
- Belgian Federation Against Cancer
- University of Liege [04/09-323]
- Federal Ministry of Science
- Centre Anti-Cancereux
- Leon Fredericq Foundation (ULg)
- King Baudouin Foundation (Brussels, Belgium)
The oncogenic protein BCL-3 activates or represses gene transcription through binding with the NF-kappa B proteins p50 and p52 and is degraded through a phospho-and GSK3-dependent pathway. However, the mechanisms underlying its degradation remain poorly understood. Yeast two-hybrid analysis led to the identification of the proteasome subunit PSMB1 as a BCL-3-associated protein. The binding of BCL-3 to PSMB1 is required for its degradation through the proteasome. Indeed, PSMB1-depleted cells are defective in degrading polyubiquitinated BCL-3. The N-terminal part of BCL-3 includes lysines 13 and 26 required for the Lys(48)-linked polyubiquitination of BCL-3. Moreover, the E3 ligase FBW7, known to polyubiquitinate a variety of substrates phosphorylated by GSK3, is dispensable for BCL-3 degradation. Thus, our data defined a unique motif of BCL-3 that is needed for its recruitment to the proteasome and identified PSMB1 as a key protein required for the proteasome-mediated degradation of a nuclear and oncogenic I kappa B protein.
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