Complex of fas-associated Factor 1 (FAF1) with valosin-containing protein (VCP)-Npl4-Ufd1 and polyubiquitinated proteins promotes endoplasmic reticulum-associated degradation (ERAD)S

Jae Jin Lee, Joon Kyu Park, Jaeho Jeong, Hyesung Jeon, Jong Bok Yoon, Eunice Eun Kyeong Kim, Kong Joo Lee

Research output: Contribution to journalArticle

32 Citations (Scopus)

Abstract

Background: FAF1, which has multiple ubiquitin-like domains, interacts with various proteins (VCP, Hsp70, and polyubiquitinated proteins). Results: Association of FAF1 UBX with VCP-Npl4-Ufd1 complex regulates ubiquitin binding to FAF1 UBA domain and promotes CD3 degradation in ERAD. Conclusion: FAF1 is a ubiquitin receptor that promotes ERAD by delivering polyubiquitinated proteins from UBX domain to UBA domain. Significance: FAF1 plays a role in ERAD by modulating domain-domain interaction.

Original languageEnglish
Pages (from-to)6998-7011
Number of pages14
JournalJournal of Biological Chemistry
Volume288
Issue number10
DOIs
Publication statusPublished - 2013 Mar 8

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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