RESETing ER proteostasis: selective stress pathway hidden in the secretory route

couve, a; Hetz C.

Abstract

The efficient folding of membrane and secreted proteins relies on the unfolded protein response (UPR) to buffer fluctuations in the load of misfolded proteins. Although the UPR is thought to operate on a generic manner to maintain ER proteostasis, a recent study revealed the existence of a novel mechanism to eliminate misfolded GPI-anchored proteins via the secretory pathway, termed rapid ER stress-induced export' (RESET) (Satpute-Krishnan etal, ). RESET involves the export of misfolded GPI proteins to the plasma membrane for subsequent degradation by the lysosome.

Más información

Título según WOS: RESETing ER proteostasis: selective stress pathway hidden in the secretory route
Título según SCOPUS: RESETing ER proteostasis: Selective stress pathway hidden in the secretory route
Título de la Revista: EMBO JOURNAL
Volumen: 33
Número: 21
Editorial: Wiley
Fecha de publicación: 2014
Página de inicio: 2444
Página final: 2446
Idioma: English
DOI:

10.15252/embj.201489845

Notas: ISI, SCOPUS