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- Title
Coactivator ASC-2 mediates heat shock factor 1-mediated transactivation dependent on heat shock
- Authors
Hong, SunHwa; Kim, Sun Hee; Heo, Mi Ae; Choi, Yoon Ha; Park, Min Jung; Yoo, Mi Ae; Kim, Han Do; Kang, Ho Sung; Cheong, JaeHun
- Abstract
Upon exposure to elevated temperatures, mammalian cells increase the expression of the heat shock proteins (HSP) through activation of the heat shock factor 1 (HSF1). Since most transcription factors require coactivators for efficient transcriptional activity, we tried to identify the coactivator(s) that interacts with and modulates the activities of HSF1. In vitro glutathione S-transferase (GST) pull-down assay revealed that HSF1 strongly interacts with activating signal cointegrator (ASC)-2 and weakly with cyclic adenosine monophosphate responsive element binding protein (CBP). We also show that cotransfection of ASC-2, but not CBP, potentiates HSF1-mediated transactivation based on its cognate element (heat shock element, HSE) linked to luciferase reporter. The molecular interaction of HSF1 and ASC-2 was stimulated by heat shock in cells and the overexpression of HSF1-interacting domain of ASC-2 inhibited the specific induced protein association and HSF1-mediated transactivation. Taking these results together, we suggest that ASC-2 in a novel coactivator for HSF1 and heat shock stress may contribute the strong active transcription complex through sequential recruitment of HSF1 and ASC-2.
- Subjects
HEAT shock proteins; GLUTATHIONE transferase; TRANSCRIPTION factors; CARRIER proteins
- Publication
FEBS Letters, 2004, Vol 559, Issue 1-3, p165
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/S0014-5793(04)00028-6