The Hsp90/CDC37 chaperone complex is required for signaling by type I and II interferons

doi:10.1074/jbc.M509901200

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Papers In Press, published online ahead of print November 9, 2005
J. Biol. Chem, 10.1074/jbc.M509901200
Submitted on September 8, 2005
Revised on October 25, 2005
Accepted on November 9, 2005

The Hsp90/CDC37 chaperone complex is required for signaling by type I and II interferons

Limin Shang and Thomas B. Tomasi

Immunology Dept., Roswell Park Cancer Institute, Buffalo, NY 14263

Corresponding Author: thomas.tomasi{at}roswellpark.org

Interferon signaling pathways are critical to both innate and adaptive immunity. We demonstrate here that inhibition of Hsp90 function by siRNAs or chemical inhibitors blocked interferon-induced gene expression. Hsp90 was required for STAT1 phosphorylation and in its absence JAK1/2 were degraded by the proteosome. JAK1 interacts with Hsp90 and the CDC37 cochaperone and both interactions are destabilized by Hsp90 inhibitors. The biological consequences were suggested by experiments showing that T cell activation by IFN- $gamma$ -primed macrophages and the antiviral response of interferons required Hsp90. We conclude that JAK1/2 are client proteins of Hsp90 and that Hsp90 and CDC37 play a critical role in type I and II interferon pathways.

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