Role of ubiquitination in PCSK9-mediated low-density lipoprotein receptor degradation.
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Chen Y, Wang H, Yu L, Yu X, Qian YW, Cao G, Wang J
Role of ubiquitination in PCSK9-mediated low-density lipoprotein receptor degradation.
Biochem Biophys Res Commun. 2011 Nov 25;415(3):515-8. doi: 10.1016/j.bbrc.2011.10.110. Epub 2011 Nov 2.
- PubMed ID
- 22074827 [ View in PubMed]
- Abstract
The proprotein convertases subtilisin kexin 9 (PCSK9) binds to the epidermal growth factor domain A (EGF-A) of low-density lipoprotein receptor (LDLR) and leads to its destruction. However, the intracellular processes leading to LDLR degradation have not been fully delineated. In this report, we show that PCSK9 treatment can lead to ubiquitination of LDLR, which was enhanced in the presence of proteasome inhibitor MG132. Furthermore, LDLR protein carrying mutations in the C-terminal ubiquitination sites was resistant to PCSK9-mediated degradation. Our data suggest that the ubiquitination system is involved in PCSK9-induced LDLR degradation.