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Originally published In Press as doi:10.1074/jbc.C000129200 on March 20, 2000
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J Biol Chem, Vol. 275, Issue 19, 14255-14259, May 12, 2000

A Gain-of-function Mutation in STAT6*

Carla Daniel, Anupama Salvekar, and Ulrike SchindlerDagger

From Tularik Inc., South San Francisco, California 94080

Interleukin-4 (IL-4) is a cytokine that plays a crucial role in the pathophysiology of asthma and allergic diseases. IL-4-induced gene expression is largely mediated through the activation of the latent transcription factor STAT6. We identified a STAT6 mutant (STAT6VT)) that is activated independently of IL-4 stimulation. STAT6VT carries two amino acid changes in the SH2 domain that affect the overall structure and stability of the monomeric and dimeric protein. When overexpressed in mammalian cells, STAT6VT undergoes tyrosine phosphorylation, binds DNA, and activates transcription in the absence of IL-4 stimulation. Using the Jak1- and Jak3-deficient fibroblast line U4A, we demonstrate that phosphorylation is mediated by an IL-4-independent tyrosine kinase that is not able to activate the wild-type STAT6 protein. These results suggest that small changes in STAT6 could result in hyperactivation of the protein and constitutive expression of STAT6-dependent genes. Such a mutation, if found in vivo, could cause genetic predisposition for atopic diseases.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Tularik Inc., Two Corporate Dr., South San Francisco, CA 94080. Tel.: 650-825-7482; Fax: 650-825-7400; E-mail: uli@tularik.com.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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