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

31 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

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Endoplasmic Reticulum-Associated Degradation
Ubiquitin
Degradation
Proteins
CDC48 protein

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

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title = "Complex of fas-associated Factor 1 (FAF1) with valosin-containing protein (VCP)-Npl4-Ufd1 and polyubiquitinated proteins promotes endoplasmic reticulum-associated degradation (ERAD)S",
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.",
author = "Lee, {Jae Jin} and Park, {Joon Kyu} and Jaeho Jeong and Hyesung Jeon and Jong-Bok Yoon and Kim, {Eunice Eun Kyeong} and Lee, {Kong Joo}",
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Complex of fas-associated Factor 1 (FAF1) with valosin-containing protein (VCP)-Npl4-Ufd1 and polyubiquitinated proteins promotes endoplasmic reticulum-associated degradation (ERAD)S. / Lee, Jae Jin; Park, Joon Kyu; Jeong, Jaeho; Jeon, Hyesung; Yoon, Jong-Bok; Kim, Eunice Eun Kyeong; Lee, Kong Joo.

In: Journal of Biological Chemistry, Vol. 288, No. 10, 08.03.2013, p. 6998-7011.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Complex of fas-associated Factor 1 (FAF1) with valosin-containing protein (VCP)-Npl4-Ufd1 and polyubiquitinated proteins promotes endoplasmic reticulum-associated degradation (ERAD)S

AU - Lee, Jae Jin

AU - Park, Joon Kyu

AU - Jeong, Jaeho

AU - Jeon, Hyesung

AU - Yoon, Jong-Bok

AU - Kim, Eunice Eun Kyeong

AU - Lee, Kong Joo

PY - 2013/3/8

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AB - 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.

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