Cell Structure and Function
Online ISSN : 1347-3700
Print ISSN : 0386-7196
ISSN-L : 0386-7196
Advance online publication
Showing 1-1 articles out of 1 articles from Advance online publication
  • Kohei Kawaguchi, Miki Yamamoto-Hino, Yoshiko Murakami, Taroh Kinoshita ...
    Article ID: 21019
    Published: 2021
    [Advance publication] Released: June 30, 2021
    JOURNALS OPEN ACCESS ADVANCE PUBLICATION
    Glycosylphosphatidylinositol (GPI)-anchored proteins are post-transcriptionally modified with GPI and anchored to the plasma membrane. GPI is attached to nascent proteins in the endoplasmic reticulum by the GPI transamidase complex, which consists of PIGT, PIGK, GPAA1, PIGU, and PIGS. Of these, PIGK is a catalytic subunit that is unstable without PIGT. This study investigated the pathway by which unassembled PIGK not incorporated into the complex is degraded. We showed that unassembled PIGK was degraded via the proteasome-dependent pathway and that Hrd1 (also known as SYVN1), a ubiquitin ligase involved in the endoplasmic reticulum-associated degradation pathway, was responsible for degradation of unassembled PIGK.
    Key words: Glycosylphosphatidylinositol, GPI transamidase complex, protein stability, transamidation, ERAD
    Download PDF (3314K)
feedback
Top