2017年6月
Degradation of human Lipin-1 by BTRC E3 ubiquitin ligase
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- 巻
- 488
- 号
- 1
- 開始ページ
- 159
- 終了ページ
- 164
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/j.bbrc.2017.04.159
- 出版者・発行元
- ACADEMIC PRESS INC ELSEVIER SCIENCE
Lipin-1 has dual functions in the regulation of lipid and energy metabolism according to its subcellular localization, which is tightly controlled. However, it is unclear how Lipin-1 degradation is regulated. Here, we demonstrate that Lipin-1 is degraded through its DSGXXS motif. We show that Lipin-1 interacts with either of two E3 ubiquitin ligases, BTRC or FBXW11, and that this interaction is DSGXXS-dependent and mediates the attachment of polyubiquitin chains. Further, we demonstrate that degradation of Lipin-1 is regulated by BTRC in the cytoplasm and on membranes. These novel insights into the regulation of human Lipin-1 stability will be useful in planning further studies to elucidate its metabolic processes. (C) 2017 Elsevier Inc. All rights reserved.
- リンク情報
- ID情報
-
- DOI : 10.1016/j.bbrc.2017.04.159
- ISSN : 0006-291X
- eISSN : 1090-2104
- PubMed ID : 28483528
- Web of Science ID : WOS:000402587000025