Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 407, Issue 1, Pages 254-259Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2011.03.016
Keywords
Protein ubiquitination; Proteasomal degradation; Ubiquitin ligase; KLF2; Smurf1
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Funding
- Chinese National Basic Research Programs [2011CB910602, 2007CB914601, 2010CB912202]
- Chinese National Natural Science Foundation [30830029, 30970601, 31070693]
- National Key Technologies R&D Program for New Drugs [2009ZX09503-002, 2009ZX09301-002]
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Kruppel-like factor 2 (KLF2) has been demonstrated to be essential for normal lung development, erythroid differentiation, T-cell differentiation, migration and homing. However, the mechanisms underlying the regulation of KLF2, in particular its responsible E3 ligase is still unclear. Here we show that the homologous to E6AP carboxyl terminus (HECT)-type ubiquitin ligase Smad ubiquitination regulatory factor 1 (Smurf1) interacts with and targets KLF2 for poly-ubiquitination and proteasomal degradation specifically in lung cancer H1299 cells. The catalytic ligase activity of Smurf1 is required for it to regulate KLF2. Consequently, Smurf1 represses the transcriptional factor activity of KLF2 and regulates the expression its downstream genes such as CD62L and Wee1. This study provided the first evidence that Smurf1 functions as an E3 ligase to promote the ubiquitination and proteasomal degradation of KLF2. (C) 2011 Elsevier Inc. All rights reserved.
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