Complex of Fas-associated Factor 1 (FAF1) with Valosin-containing Protein (VCP)-Npl4-Ufd1 and Polyubiquitinated Proteins Promotes Endoplasmic Reticulum-associated Degradation (ERAD) *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 288, Issue: 10, Page: 6998-7011
2013
- 47Citations
- 56Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations47
- Citation Indexes47
- 47
- CrossRef35
- Captures56
- Readers56
- 56
Article Description
Fas-associated factor 1 (FAF1) is a ubiquitin receptor containing multiple ubiquitin-related domains including ubiquitin-associated (UBA), ubiquitin-like (UBL) 1, UBL2, and ubiquitin regulatory X (UBX). We previously showed that N-terminal UBA domain recognizes Lys 48 -ubiquitin linkage to recruit polyubiquitinated proteins and that a C-terminal UBX domain interacts with valosin-containing protein (VCP). This study shows that FAF1 interacts only with VCP complexed with Npl4-Ufd1 heterodimer, a requirement for the recruitment of polyubiquitinated proteins to UBA domain. Intriguingly, VCP association to C-terminal UBX domain regulates ubiquitin binding to N-terminal UBA domain without direct interaction between UBA and UBX domains. These interactions are well characterized by structural and biochemical analysis. VCP-Npl4-Ufd1 complex is known as the machinery required for endoplasmic reticulum-associated degradation. We demonstrate here that FAF1 binds to VCP-Npl4-Ufd1 complex via UBX domain and polyubiquitinated proteins via UBA domain to promote endoplasmic reticulum-associated degradation. 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 CD3δ 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.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925819623781; http://dx.doi.org/10.1074/jbc.m112.417576; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84874871591&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/23293021; https://linkinghub.elsevier.com/retrieve/pii/S0021925819623781; http://www.jbc.org/lookup/doi/10.1074/jbc.M112.417576; https://syndication.highwire.org/content/doi/10.1074/jbc.M112.417576; https://dx.doi.org/10.1074/jbc.m112.417576
Elsevier BV
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