The proteasome activator PA28 functions in collaboration with Hsp90 in vivo
2006
Abstract We have previously shown that the proteasome activator PA28 is essential to
Hsp90-dependent protein refolding in vitro, where PA28 mediates transfer of the
Hsp90-bound substrate protein to the Hsc70/Hsp40 chaperone machine for its correct refolding. This observation suggests that PA28 may also collaborate with
Hsp90in cells. To examine this possibility, here we have used double-stranded
RNA interference(RNAi) against PA28 in
Caenorhabditis elegansmutants of daf-21 , which encodes
Hsp90. We show that C. elegans PA28 facilitates
Hsp90-initiated protein refolding, albeit with an activity lower than that of mouse PA28 proteins. RNAi-mediated knockdown of PA28 significantly suppresses the Daf-c (dauer formation constitutive) phenotype of the daf-21 mutant, but it has no affect on the distinct defects of this mutant in sensing odorants. Taking these results together, we conclude that PA28 is likely to function in collaboration with
Hsp90in vivo.
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