An unexpected role for the yeast nucleotide exchange factor Sil1 as a reductant acting on the molecular chaperone BiP
Unfavorable redox conditions in the endoplasmic reticulum (ER) can decrease the capacity for protein secretion, altering vital cell functions. While systems to manage reductive stress are well-established, how cells cope with an overly oxidizing ER remains largely undefined. In previous work (Wang e...
Main Authors: | Kevin D Siegenthaler, Kristeen A Pareja, Jie Wang, Carolyn S Sevier |
---|---|
Format: | Article |
Language: | English |
Published: |
eLife Sciences Publications Ltd
2017-03-01
|
Series: | eLife |
Subjects: | |
Online Access: | https://elifesciences.org/articles/24141 |
Similar Items
-
Redox signaling via the molecular chaperone BiP protects cells against endoplasmic reticulum-derived oxidative stress
by: Jie Wang, et al.
Published: (2014-07-01) -
Role of the HSP70 Co-Chaperone SIL1 in Health and Disease
by: Viraj P. Ichhaporia, et al.
Published: (2021-02-01) -
BiP Negatively Affects Ricin Transport
by: Kirsten Sandvig, et al.
Published: (2013-05-01) -
Calcium depletion challenges endoplasmic reticulum proteostasis by destabilising BiP-substrate complexes
by: Steffen Preissler, et al.
Published: (2020-12-01) -
Physiological modulation of BiP activity by trans-protomer engagement of the interdomain linker
by: Steffen Preissler, et al.
Published: (2015-10-01)