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J Biol Chem, Vol. 274, Issue 19, 12967-12970, May 7, 1999
From the Department of Biochemistry, University of Kentucky,
Chandler Medical Center, Lexington, Kentucky 40536-0084
Heat shock transcription factor (HSF) mediates
the stress-induced expression of heat shock protein genes
(hsp). However, HSF is required for normal cell function
even in the absence of stress and is important for cell cycle
progression, but the mechanism that mediates these effects of HSF is
unknown. Here, it is shown that a member of the HSF family, HSF2,
interacts with the PR65 (A) subunit of protein phosphatase 2A (PP2A).
HSF2 binding to PR65 blocks its interaction with the catalytic subunit,
due to competition between HSF2 and catalytic subunit for the same
binding site in PR65. In addition, overexpression of HSF2 stimulates
PP2A activity in cells, indicating the relevance of HSF2 as a regulator of PP2A in vivo. These results identify HSF2 as a dual
function protein, capable of regulating both hsp expression
and PP2A activity. This could function as a mechanism by which
hsp expression is integrated with the control of cell
division or other PP2A-regulated pathways.
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