▪ Abstract Cotranslational protein translocation across and integration into the membrane of
the endoplasmic reticulum (ER) occur at sites termed translocons. Translocons are …

▪ Abstract Helical membrane protein folding and oligomerization can be usefully
conceptualized as involving two energetically distinct stages—the formation and subsequent …

We have analyzed how the signal sequence of prepro-α-factor is recognized during the first
step of posttranslational protein transport into the yeast endoplasmic reticulum. Cross-linking …

In mammalian cells, signal peptide‐dependent protein transport into the endoplasmic
reticulum (ER) is mediated by a dynamic protein‐conducting channel, the Sec61 complex …

The major route of protein translocation in bacteria is the so-called general secretion
pathway (Sec-pathway). This route has been extensively studied in Escherichia coli and …

Lhs1p is an Hsp70‐related chaperone localized in the endoplasmic reticulum (ER) lumen.
Δlhs1 mutant cells are viable but are constitutively induced for the unfolded protein response …

In bacteria, the translocase mediates the translocation of proteins into or across the cytosolic
membrane. It consists of a membrane embedded protein-conducting channel and a …

Application of differential display to cultured rat astrocytes subjected to hypoxia allowed
cloning of a novel cDNA, termed stress-associated endoplasmic reticulum protein 1 …

Targeting of ribosome–nascent chain complexes to the translocon in the endoplasmic
reticulum is mediated by the concerted action of the signal recognition particle (SRP) and …

Misfolded secretory and transmembrane proteins are retained in the endoplasmic reticulum
(ER) and subsequently degraded. Degradation is primarily mediated by cytosolic …