A Flat Protein Complex Shapes Rough ER Membrane Sheets
Sawyer, E. M.; Jensen, L. E.; Meehl, J. B.; Larsen, K. P.; Petito, D. A.; Hurley, J. H.; Voeltz, G. K.
Show abstract
Rough ER sheets are a fundamental domain of the ER and the gateway into the secretory pathway. While reticulon proteins stabilize high-curvature ER tubules, it is unclear if other proteins scaffold the flat membranes of rough ER sheets. Through a proteomics screen using ER sheet localized RNA-binding proteins as bait, we identify the Sigma-1 receptor (SigmaR1) as an ER sheet shaping factor. High-resolution live cell imaging and electron tomography assign SigmaR1 as an ER sheet-localized factor whose levels determine the amount of rough ER sheets in cells. Structure-guided mutagenesis and in vitro reconstitution on giant unilamellar vesicles further support a mechanism whereby SigmaR1 oligomers use their extended arrays of amphipathic helices to bind and flatten the lumenal leaflet of ER membranes. Our results demonstrate an unexpected way for proteins to sense and propagate flat membrane sheets.
Matching journals
The top 5 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- The Dsc ubiquitin ligase complex identifies transmembrane degrons to degrade orphaned proteins at the Golgi 96%
- Cavin1 intrinsically disordered domains are essential for fuzzy electrostatic interactions and caveola formation 96%
- UBE2J2 sensitizes the ERAD ubiquitination cascade to changes in membrane lipid saturation 96%
Similar papers in this journal
- A Myosin-7B dependent endocytosis pathway mediates cellular entry of α-Synuclein fibrils and polycation-bearing cargos 95%
- Structure and mechanism of the human CTDNEP1-NEP1R1 membrane protein phosphatase complex necessary to maintain ER membrane morphology 95%
- Split-TurboID enables contact-dependent proximity labeling in cells 95%
Similar papers in this journal
Similar papers in this journal
- C-terminal tagging, transmembrane domain hydrophobicity, and an ER retention motif influence the secretory trafficking of the inner nuclear membrane protein emerin 97%
- Prominin 1 and Tweety Homology 1 both induce extracellular vesicle formation 95%
- The KASH5 protein involved in meiotic chromosomal movements is a novel dynein activating adaptor 95%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.