The interferon-inducible ubiquitin-protein isopeptide ligase (E3) EFP also functions as an ISG15 E3 ligase

被引:216
作者
Zou, WG [1 ]
Zhang, DE [1 ]
机构
[1] Scripps Res Inst, Dept Mol & Expt Med, La Jolla, CA 92037 USA
关键词
D O I
10.1074/jbc.M510787200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The expression of the ubiquitin-like protein ISG15 and protein modification by ISG15 (ISGylation) are strongly activated by interferons. Accordingly, ISG15 expression and protein ISGylation are strongly activated upon viral and bacterial infections and during other stress conditions, suggesting important roles for the ISG15 system in innate immune responses. Here, we report the identification of the ubiquitin-protein isopeptide ligase (E3) EFP (estrogen-responsive finger protein) as the ISG15 E3 ligase for 14-3-3 sigma protein. Like other known components of the protein ISGylation system (ISG15, UBE1L, UBP43, and UBC8), EFP is also an interferon-inducible protein. Expression of EFP small interfering RNA decreased the ISGylation of 14-3-3 sigma in the 293T cell ISGylation system as well as in MCF-7 cells upon interferon treatment. Furthermore, the ISGylation enzyme activity of EFP was RING domain-dependent. These findings indicate that EFP is an ISG15 E3 ligase for 14-3-3 sigma in vivo. The fact that both UBC8 and EFP are common components in the ubiquitin and ISG15 conjugation pathways suggests a mechanism whereby a limited set of enzymes accomplishes diverse post-translational modifications of their substrates in response to changes in environmental stimulations.
引用
收藏
页码:3989 / 3994
页数:6
相关论文
共 50 条
[1]   RING domains: Master builders of molecular scaffolds? [J].
Borden, KLB .
JOURNAL OF MOLECULAR BIOLOGY, 2000, 295 (05) :1103-1112
[2]  
BRIDGES D, 2004, SCI STKE, pRE10
[3]   A system for stable expression of short interfering RNAs in mammalian cells [J].
Brummelkamp, TR ;
Bernards, R ;
Agami, R .
SCIENCE, 2002, 296 (5567) :550-553
[4]   Staring, a novel E3 ubiquitin-protein ligase that targets syntaxin 1for degradation [J].
Chin, LS ;
Vavalle, JP ;
Li, L .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (38) :35071-35079
[5]   ISG15: A ubiquitin-like enigma [J].
Dao, CT ;
Zhang, DE .
FRONTIERS IN BIOSCIENCE-LANDMARK, 2005, 10 :2701-2722
[6]   JAK-STAT PATHWAYS AND TRANSCRIPTIONAL ACTIVATION IN RESPONSE TO IFNS AND OTHER EXTRACELLULAR SIGNALING PROTEINS [J].
DARNELL, JE ;
KERR, IM ;
STARK, GR .
SCIENCE, 1994, 264 (5164) :1415-1421
[7]   ACCUMULATION OF AN MESSENGER-RNA AND PROTEIN IN INTERFERON-TREATED EHRLICH ASCITES TUMOR-CELLS [J].
FARRELL, PJ ;
BROEZE, RJ ;
LENGYEL, P .
NATURE, 1979, 279 (5713) :523-525
[8]   Crystal structure of an IRF-DNA complex reveals novel DNA recognition and cooperative binding to a tandem repeat of core sequences [J].
Fujii, Y ;
Shimizu, T ;
Kusumoto, M ;
Kyogoku, Y ;
Taniguchi, T ;
Hakoshima, T .
EMBO JOURNAL, 1999, 18 (18) :5028-5041
[9]   Proteomic identification of proteins conjugated to ISG15 in mouse and human cells [J].
Giannakopoulos, NV ;
Luo, JK ;
Papov, V ;
Zou, WG ;
Lenschow, DJ ;
Jacobs, BS ;
Borden, EC ;
Li, J ;
Virgin, HW ;
Zhang, DE .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2005, 336 (02) :496-506
[10]  
HAAS AL, 1987, J BIOL CHEM, V262, P11315