Article ID Journal Published Year Pages File Type
1929950 Biochemical and Biophysical Research Communications 2011 4 Pages PDF
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.

► PCSK9 treatment can lead to ubiquitination of LDLR. ► Proteasome inhibitor MG132 prevents PCSK9-mediated LDLR degradation. ► Mutant LDLR in the ubiquitination sites is resistant to PCSK9-mediated degradation.

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