The Action of Molecular Chaperones in the Early Secretory Pathway
- 1 December 2001
- journal article
- review article
- Published by Annual Reviews in Annual Review of Genetics
- Vol. 35 (1) , 149-191
- https://doi.org/10.1146/annurev.genet.35.102401.090313
Abstract
The endoplasmic reticulum (ER) serves as a way-station during the biogenesis of nearly all secreted proteins, and associated with or housed within the ER are factors required to catalyze their import into the ER and facilitate their folding. To ensure that only properly folded proteins are secreted and to temper the effects of cellular stress, the ER can target aberrant proteins for degradation and/or adapt to the accumulation of misfolded proteins. Molecular chaperones play critical roles in each of these phenomena.Keywords
This publication has 313 references indexed in Scilit:
- Sec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivoThe EMBO Journal, 2001
- Regulated Intramembrane ProteolysisCell, 2000
- Mechanism of non-spliceosomal mRNA splicing in the unfolded protein response pathwayThe EMBO Journal, 1999
- Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein.Molecular Biology of the Cell, 1996
- tRNA Ligase Is Required for Regulated mRNA Splicing in the Unfolded Protein ResponseCell, 1996
- A Novel Mechanism for Regulating Activity of a Transcription Factor That Controls the Unfolded Protein ResponseCell, 1996
- Lactacystin, an Inhibitor of the Proteasome, Blocks the Degradation of a Mutant Precursor of Glycosylphosphatidylinositol-Linked Protein in a Pre-Golgi CompartmentBiochemical and Biophysical Research Communications, 1996
- A transmembrane protein with a cdc 2+ CDC 28 - related kinase activity is required for signaling from the ER to the nucleusPublished by Elsevier ,1993
- Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinaseCell, 1993
- 70K heat shock related proteins stimulate protein translocation into microsomesNature, 1988