Cell Structure and Function
Online ISSN : 1347-3700
Print ISSN : 0386-7196
ISSN-L : 0386-7196
Hrd1-dependent Degradation of the Unassembled PIGK Subunit of the GPI Transamidase Complex
Kohei KawaguchiMiki Yamamoto-HinoYoshiko MurakamiTaroh KinoshitaSatoshi Goto
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Supplementary material

2021 Volume 46 Issue 2 Pages 65-71


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

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