The mechanisms of integral membrane protein biogenesis

RS Hegde, RJ Keenan - Nature reviews Molecular cell biology, 2022 - nature.com
Roughly one quarter of all genes code for integral membrane proteins that are inserted into
the plasma membrane of prokaryotes or the endoplasmic reticulum membrane of …

Targeting of proteins for translocation at the endoplasmic reticulum

MR Pool - International journal of molecular sciences, 2022 - mdpi.com
The endoplasmic reticulum represents the gateway to the secretory pathway. Here, proteins
destined for secretion, as well as soluble and membrane proteins that reside in the …

Take me home, protein roads: Structural insights into signal peptide interactions during ER translocation

AM Liaci, F Förster - International Journal of Molecular Sciences, 2021 - mdpi.com
Cleavable endoplasmic reticulum (ER) signal peptides (SPs) and other non-cleavable
signal sequences target roughly a quarter of the human proteome to the ER. These short …

The molecular biodiversity of protein targeting and protein transport related to the endoplasmic reticulum

A Tirincsi, M Sicking, D Hadzibeganovic… - International journal of …, 2021 - mdpi.com
Looking at the variety of the thousands of different polypeptides that have been focused on
in the research on the endoplasmic reticulum from the last five decades taught us one …

Emerging view on the molecular functions of Sec62 and Sec63 in protein translocation

S Jung, H Kim - International Journal of Molecular Sciences, 2021 - mdpi.com
Most secreted and membrane proteins are targeted to and translocated across the
endoplasmic reticulum (ER) membrane through the Sec61 protein-conducting channel …

Role of a holo-insertase complex in the biogenesis of biophysically diverse ER membrane proteins

KR Page, VN Nguyen, T Pleiner, GP Tomaleri… - Molecular Cell, 2023 - cell.com
Mammalian membrane proteins perform essential physiologic functions that rely on their
accurate insertion and folding at the endoplasmic reticulum (ER). Using forward and arrayed …

Signal peptide features determining the substrate specificities of targeting and translocation components in human ER protein import

S Lang, D Nguyen, P Bhadra, M Jung, V Helms… - Frontiers in …, 2022 - frontiersin.org
In human cells, approximately 30% of all polypeptides enter the secretory pathway at the
level of the endoplasmic reticulum (ER). This process involves cleavable amino-terminal …

Effector secretion and stability in the maize anthracnose pathogen Colletotrichum graminicola requires N‐linked protein glycosylation and the ER chaperone pathway

J Mei, Z Li, S Zhou, XL Chen, RA Wilson… - New Phytologist, 2023 - Wiley Online Library
N‐linked protein glycosylation is a conserved and essential modification mediating protein
processing and quality control in the endoplasmic reticulum (ER), but how this contributes to …

Dual topology of co-chaperones at the membrane of the endoplasmic reticulum

L Daverkausen-Fischer, F Pröls - Cell Death Discovery, 2021 - nature.com
Dual topologies of proteins at the ER membrane are known for a variety of proteins allowing
the same protein to exert different functions according to the topology adopted. A dual …

Regulation of translation, translocation, and degradation of proteins at the membrane of the endoplasmic reticulum

L Daverkausen-Fischer, M Draga, F Pröls - International Journal of …, 2022 - mdpi.com
The endoplasmic reticulum (ER) of mammalian cells is the central organelle for the
maturation and folding of transmembrane proteins and for proteins destined to be secreted …