Regulation of Sam68 activity by small heat shock protein 22
- 22 June 2006
- journal article
- Published by Wiley in Journal of Cellular Biochemistry
- Vol. 99 (5), 1353-1362
- https://doi.org/10.1002/jcb.21004
Abstract
Sam68 associates with c‐Src kinase during mitosis. We previously demonstrated that Sam68 functionally replaces and/or synergizes with HIV‐1 Rev in rev response element (RRE)‐mediated gene expression and virus production. Furthermore, we reported that knockdown of Sam68 inhibited Rev‐mediated RNA export and it is absolutely required for HIV‐1 production. In the present study, we identified small heat shock protein, hsp22, as a novel interacting partner of Sam68. Hsp22 binds to Sam68 in vitro and in vivo. Overexpression of hsp22 significantly inhibits Sam68‐mediated RRE‐ as well as CTE (constitutive transport element)‐dependent reporter gene expression. Furthermore, exposing 293T cells to heat shock inhibits Sam68/RRE function by virtue of elevating hsp22. The critical domain of hsp22 that interacts with Sam68 resides between amino acids 62 and 133. Our studies provide evidence for the first time that hsp22 specifically binds to Sam68 and modulates its activity, thus playing a role in the post‐transcriptional regulation of gene expression. J. Cell. Biochem. 99: 1353–1362, 2006.This publication has 35 references indexed in Scilit:
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