Cell Structure and Function
Online ISSN : 1347-3700
Print ISSN : 0386-7196
ISSN-L : 0386-7196

This article has now been updated. Please use the final version.

Hrd1-dependent degradation of the unassembled PIGK subunit of the GPI transamidase complex
Kohei KawaguchiMiki Yamamoto-HinoYoshiko MurakamiTaroh KinoshitaSatoshi Goto
Author information
JOURNAL OPEN ACCESS Advance online publication

Article ID: 21019


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

Content from these authors
© 2021 The Author(s) CC-BY 4.0 (Submission before October 2016: Copyright © Japan Society for Cell Biology)