Mammalian cells secrete a large number of small proteins, but their mode of translocation
into the endoplasmic reticulum is not fully understood. Cotranslational translocation was …

Protein transport into the mammalian endoplasmic reticulum (ER) is mediated by the
heterotrimeric Sec61 channel. The signal recognition particle (SRP) and TRC systems and …

Increasing evidence indicates that many small secretory preproteins can undergo post-
translational translocation across the membrane of the endoplasmic reticulum. Although the …

Protein transport into the mammalian endoplasmic reticulum (ER) used to be seen as strictly
cotranslational, that is temporarily and mechanistically coupled to protein synthesis. In the …

The evolutionarily conserved Sec61 protein complex mediates the translocation of secretory
proteins into the endoplasmic reticulum. To investigate the role of Sec61p, which is the main …

Precursors of secretory proteins are targeted to the membrane of the endoplasmic reticulum
by specific protein complexes that recognize their signal sequence. All eukaryotic cells …

The metazoan Sec61 translocon transports polypeptides into and across the membrane of
the endoplasmic reticulum via two major routes, a well-established co-translational pathway …

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

ABSTRACT The Sec62–Sec63 complex mediates post-translational translocation of a
subset of primarily secretory proteins into the endoplasmic reticulum (ER) in yeast …

When affinity‐purified proOmpA was diluted out of 8 M urea into a sample of yeast
microsomes, it was translocated and processed in the absence of any cytosolic factors; an …