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DAXX Interacts with Heat Shock Factor 1 during Stress Activation and Enhances Its Transcriptional Activity
Frank Boellmann, Toumy Guettouche, Yongle Guo, Mary Fenna, Laila Mnayer, Richard Voellmy and Robert G. Roeder
Proceedings of the National Academy of Sciences of the United States of America
Vol. 101, No. 12 (Mar. 23, 2004), pp. 4100-4105
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/3371569
Page Count: 6
You can always find the topics here!Topics: Cell lines, Heat stress disorders, Repression, Apoptosis, Heat shock proteins, Heat treatment, Transactivation, Transfection, Social interaction, Shock heating
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DAXX, a modulator of apoptosis and a repressor of basal transcription, was identified in a two-hybrid screen as a protein capable of interacting with a trimeric form of human heat shock factor 1 (HSF1). In human cells, DAXX interacted with HSF1 essentially only during stress, i.e., when factor trimerization occurred. Several lines of experimentation suggested that DAXX is an important mediator of HSF1 activation: (i) overexpression of DAXX enhanced basal transactivation competence of HSF1 in the absence of a stress; (ii) a DAXX fragment exerted dominant-negative effects on HSF1 activation by different types of stress; (iii) induction of heat shock or stress protein (HSP)70 by heat stress was defective in a cell line lacking functional DAXX; and (iv) RNA interference depletion of DAXX also substantially reduced heat induction of HSF1 activity and HSP70 expression. HSF1 transactivation competence is repressed by an HSP90-containing multichaperone complex that interacts with trimeric factor. Overexpressed HSF1, known to be largely trimeric, only marginally increased HSF1 activity on its own but potentiated the activating effect of DAXX overexpression. Expression of a nonnative protein capable of competing for multichaperone complex also synergistically enhanced activation of HSF1 by DAXX. These observations suggest a model in which DAXX released from its nuclear stores during stress opposes repression of HSF1 transactivation competence by multichaperone complex through its interaction with trimerized HSF1. Our identification of DAXX as a mediator of HSF1 activation raises the question whether DAXX produces some of its pleiotropic effects through modulation of HSP levels.
Proceedings of the National Academy of Sciences of the United States of America © 2004 National Academy of Sciences