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A more recent version of this article appeared on February 17, 2006
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Papers In Press, published online ahead of print December 13, 2005
J. Biol. Chem, 10.1074/jbc.M510787200
Submitted on October 3, 2005
Revised on December 1, 2005
Accepted on December 13, 2005

Interferon-inducible ubiqitin E3 ligase efp also functions as an ISG15 E3 ligase

Weiguo Zou and Dong-Er Zhang

Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA 92037

Corresponding Author: dzhang{at}scripps.edu

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 of ISG15 system in innate immune responses. Here, we report the identification of ubiquitin E3 ligase Efp (estrogen-responsive finger protein) as the ISG15 E3 ligase for 14-3-3 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 siRNA decreases the ISGylation of 14-3-3 in the 293T cells ISGylation system as well as in the MCF-7 cells upon interferon treatment. Furthermore, ISGylation enzyme activity of Efp is RING domain dependent. These findings indicate that Efp is an ISG15 E3 ligase for 14-3-3 in vivo. The fact that both UBC8 and Efp are common components in the ubiquitin and ISG15 conjugation pathway suggests a mechanism whereby a limited set of enzymes accomplishes diverse post-translational modifications of their substrates in response to the change of environmental stimulations.


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