The trimerization domain of human heat shock factor 2 is able to interact with nucleoporin p62.

Heat shock factor 2 (HSF2) acquires DNA binding activity during hemin-induced differentiation of human K562 erythroleukemia cells. To investigate the mechanisms responsible for the regulation of HSF2 activity, we searched for proteins that can associate with HSF2 by the yeast two-hybrid system. Nucleoporin p62, a major component of the nuclear pore complex, was cloned from cDNA libraries of K562 cells. We demonstrated physical interaction between HSF2 and p62 both by a glutathione S-transferase (GST) pull-down assay in vitro and by a two-hybrid assay in K562 cells. HSF1 is also able to interact with p62 on a GST pull-down assay, but not on a mammalian two-hybrid system. Furthermore, it was shown that this interaction occurred between the trimerization domain of HSF2 and the C-terminal alpha-helical coiled-coil domain of p62. These data suggest the possibility that p62 is involved in the activation or regulation of HSF2.