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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

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
Authors
Lee J.-J.Park J.K.Jeong J.Jeon H.Yoon J.-B.Kim E.E.Lee K.-J.
Ewha Authors
이공주
SCOPUS Author ID
이공주scopus
Issue Date
2013
Journal Title
Journal of Biological Chemistry
ISSN
0021-9258JCR Link
Citation
vol. 288, no. 10, pp. 6998 - 7011
Indexed
SCI; SCIE; SCOPUS WOS 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. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
DOI
10.1074/jbc.M112.417576
Appears in Collections:
약학대학 > 약학과 > Journal papers
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