Degradation of human Lipin-1 by BTRC E3 ubiquitin ligase
Degradation of human Lipin-1 by BTRC E3 ubiquitin ligase
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DOI：
10.1016/j.bbrc.2017.04.159
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发表时间：
2017-06-17
影响因子：
3.1
通讯作者：
Doi, Takefumi
中科院分区：
文献类型：
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作者：
Ishimoto, Kenji;Hayase, Ayaka;Doi, Takefumi
脂蛋白-1根据其在细胞内的定位，具有调节脂质和能量代谢的双重功能，并受到严格的调控。然而，目前尚不清楚Lipin-1的降解是如何受到调控的。在这里，我们证明了Lipin-1是通过其DSGXXS基序降解的。我们发现Lipin-1与两个E3泛素连接酶BTRC或FBXW11中的任何一个相互作用，并且这种相互作用是DSGXXS依赖的，并介导了多泛素链的附着。此外，我们证明了脂类-1的降解是由BTRC在细胞质和膜上调节的。这些对人类脂蛋白-1稳定性调节的新见解将有助于计划进一步研究以阐明其代谢过程。(C)2017 Elsevier Inc.保留所有权利。
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.