Display Settings:

Format

Send to:

Choose Destination
    Biochem Biophys Res Commun. 2011 Nov 25;415(3):515-8. Epub 2011 Nov 2.

    Role of ubiquitination in PCSK9-mediated low-density lipoprotein receptor degradation.

    Source

    Department of Endocrine Research, Lilly Research Laboratories, Eli Lilly & Company, Indianapolis, IN 46285, USA.

    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.

    Copyright © 2011 Elsevier Inc. All rights reserved.

    PMID:
    22074827
    [PubMed - indexed for MEDLINE]

      Supplemental Content

      Icon for Elsevier Science

      Save items

      loading

      Recent activity

      Your browsing activity is empty.

      Activity recording is turned off.

      Turn recording back on

      See more...
      Write to the Help Desk