Hrd1-dependent Degradation of the Unassembled PIGK Subunit of the GPI Transamidase Complex

• Kawaguchi Kohei

  Department of Life Science, Rikkyo University

• Yamamoto-Hino Miki

  Department of Life Science, Rikkyo University

• Murakami Yoshiko

  Research Institute for Microbial Diseases, Osaka University

• Kinoshita Taroh

  Research Institute for Microbial Diseases, Osaka University

• Goto Satoshi

  Department of Life Science, Rikkyo University

抄録

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

収録刊行物

• Cell Structure and Function

  Cell Structure and Function 46 (2), 65-71, 2021

  日本細胞生物学会

キーワード

• Glycosylphosphatidylinositol
• GPI transamidase complex
• protein stability
• transamidation
• ERAD

詳細情報

• CRID: 1390289254683567872
• NII論文ID: 130008083701
• NII書誌ID: AA0060007X
• DOI: 10.1247/csf.21019
• ISSN: 13473700
• ISSN: 03867196
• NDL書誌ID: 032032610
• PubMed: 34193731
• Web Site: http://id.ndl.go.jp/bib/032032610
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I032032610
• Web Site: https://www.jstage.jst.go.jp/article/csf/46/2/46_21019/_pdf
• Web Site: https://search.jamas.or.jp/link/ui/2023116182
• 本文言語コード: en
• データソース種別:
  • JaLC
  • NDL
  • Crossref
  • PubMed
  • CiNii Articles
  • KAKEN
• 抄録ライセンスフラグ: 使用不可