We found a match
Your institution may have rights to this item. Sign in to continue.
- Title
Roles of 17-AAG-induced molecular chaperones and Rma1 E3 ubiquitin ligase in folding and degradation of Pendrin
- Authors
Lee, Kanghyun; Hong, Tae-Joon; Hahn, Ji-Sook
- Abstract
Abstract: Pendrin is a transmembrane chloride/anion exchanger highly expressed in thyroid, kidney, and inner ear. Endoplasmic reticulum (ER)-retention of improperly folded Pendrin mutants is considered as the major cause for Pendred syndrome. However, the folding and degradation mechanisms of Pendrin are poorly understood. Here, we report that treatment of 17-AAG, an Hsp90 inhibitor, facilitates the folding of Pendrin through heat shock transcription factor 1 (Hsf1)-dependent induction of molecular chaperones. Furthermore, we demonstrate that Rma1, an E3 ubiquitin ligase localized in the ER membrane, is involved in Pendrin degradation.
- Subjects
UBIQUITIN ligases; CHLORIDES; MOLECULAR chaperones; ION exchange (Chemistry); ENDOPLASMIC reticulum; ENZYME inhibitors; HEAT shock proteins
- Publication
FEBS Letters, 2012, Vol 586, Issue 16, p2535
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2012.06.023