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
Y1 - 2013/3/8
N2 - 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.
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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U2 - 10.1074/jbc.M112.417576
DO - 10.1074/jbc.M112.417576
M3 - Article
C2 - 23293021
AN - SCOPUS:84874871591
SN - 0021-9258
VL - 288
SP - 6998
EP - 7011
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 10
ER -