RESETing ER proteostasis: Selective stress pathway hidden in the secretory route
Author
dc.contributor.author
Couve Correa, Andrés
Author
dc.contributor.author
Hetz Flores, Claudio
Admission date
dc.date.accessioned
2019-03-18T11:52:08Z
Available date
dc.date.available
2019-03-18T11:52:08Z
Publication date
dc.date.issued
2014
Cita de ítem
dc.identifier.citation
The EMBO Journal Vol 33 | No 21 | 2014
Identifier
dc.identifier.issn
14602075
Identifier
dc.identifier.issn
02614189
Identifier
dc.identifier.other
10.15252/embj.201489845
Identifier
dc.identifier.uri
https://repositorio.uchile.cl/handle/2250/166456
Abstract
dc.description.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) (SatputeKrishnan et al, 2014). RESET involves the
export of misfolded GPI proteins to the
plasma membrane for subsequent degradation by the lysosome.