Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 419, Issue 3, Pages 550-555Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2012.02.058
Keywords
C/EBP beta; Phosphorylation; Degradation; Calpain
Categories
Funding
- National Natural Science Foundation [30700121, 30870510]
- Shanghai Rising Star Program [08QA14012]
- Program for New Century Excellent Talents [NCET-08-130]
- Shanghai New Excellent Medicine Talents Program [XYQ2011037]
- Shanghai Leading Academic Discipline Project [B110, 985 III-YFX0302]
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CCAAT/enhancer-binding protein (C/EBP) 13 plays an important role in proliferation and differentiation of 3T3-L1 preadipocytes. C/EBP beta is sequentially phosphorylated during the 3T3-L1 adipocyte differentiation program, first by MAPK/Cyclin A/cdk2 on Thr(188) and subsequently by GSK3 beta on Ser(184) or Thr(179). Dual phosphorylation is critical for the gain of DNA binding activity of C/EBP beta. In this manuscript, we found that phosphorylation also contributed to the stability of C/EBP beta. Both ex vivo and in vitro experiments showed that phosphorylation by MAPK/Cyclin A/cdk2 and GSK3 beta protected C/EBP beta from mu-calpain-mediated proteolysis, while phosphorylation on Thr(188) by MAPK/Cyclin A/cdk2 contributed more to the stabilization of C/EBP beta, Further studies indicated that phosphorylation mimic C/EBP beta was insensitive to both calpain accelerator and calpain inhibitor. Thus, phosphorylation might contribute to the stability as well as the gain of DNA binding activity of C/EBP beta. (C) 2012 Elsevier Inc. All rights reserved.
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