ArticleMolecular biology of the cell1998
Immunoisolation and characterization of a subdomain of the endoplasmic reticulum that concentrates proteins involved in COPII vesicle biogenesis.
Article in Molecular biology of the cell, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
18 citing papers in PubMed, 49 citations in OpenAlex.
- The Sar1 GTPase is dispensable for COPII-dependent cargo export from the ER.Cell reports · 2023Article
- In vitro reconstitution of COPII vesicles from Arabidopsis thaliana suspension-cultured cells.Nature protocols · 2023Review
- TFG facilitates outer coat disassembly on COPII transport carriers to promote tethering and fusion with ER-Golgi intermediate compartments.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Regulation of ER-Golgi Transport Dynamics by GTPases in Budding Yeast.Frontiers in cell and developmental biology · 2017Review
- COPII machinery cooperates with ER-localized Hsp40 to sequester misfolded membrane proteins into ER-associated compartments.Molecular biology of the cell · 2013Article
- Unconventional secretion of tissue transglutaminase involves phospholipid-dependent delivery into recycling endosomes.PloS one · 2011Article
- hNOA1 interacts with complex I and DAP3 and regulates mitochondrial respiration and apoptosis.The Journal of biological chemistry · 2009Article
- CDC2/SPDY transiently associates with endoplasmic reticulum exit sites during oocyte maturation.BMC developmental biology · 2009Article
- Analysis of the selective advantage conferred by a C-E1 fusion protein synthesized by rubella virus DI RNAs.Virology · 2007Article
- Intracellular localization of Crimean-Congo Hemorrhagic Fever (CCHF) virus glycoproteins.Virology journal · 2005Article
- Cdc2 kinase-dependent disassembly of endoplasmic reticulum (ER) exit sites inhibits ER-to-Golgi vesicular transport during mitosis.Molecular biology of the cell · 2004Article
- A striking quality control subcompartment in Saccharomyces cerevisiae: the endoplasmic reticulum-associated compartment.Molecular biology of the cell · 2004Article
- Structural organization of the endoplasmic reticulum.EMBO reports · 2002Review
- Dynamics of transitional endoplasmic reticulum sites in vertebrate cells.Molecular biology of the cell · 2000Article
- Characterization of the coronavirus mouse hepatitis virus strain A59 small membrane protein E.Journal of virology · 2000Article
- Peroxisomal membrane ascorbate peroxidase is sorted to a membranous network that resembles a subdomain of the endoplasmic reticulum.The Plant cell · 1999Article
- Markers for trans-Golgi membranes and the intermediate compartment localize to induced membranes with distinct replication functions in flavivirus-infected cells.Journal of virology · 1999Article
- Role of rubella virus glycoprotein domains in assembly of virus-like particles.Journal of virology · 1999Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Rubella virus E1 glycoprotein normally complexes with E2 in the endoplasmic reticulum (ER) to form a heterodimer that is transported to and retained in the Golgi complex. In a previous study, we showed that in the absence of E2, unassembled E1 subunits accumulate in a tubular pre-Golgi compartment whose morphology and biochemical properties are distinct from both rough ER and Golgi. We hypothesized that this compartment corresponds to hypertrophied ER exit sites that have expanded in response to overexpression of E1. In the present study we constructed BHK cells stably expressing E1 protein containing a cytoplasmically disposed epitope and isolated the pre-Golgi compartment from these cells by cell fractionation and immunoisolation. Double label indirect immunofluorescence in cells and immunoblotting of immunoisolated tubular networks revealed that proteins involved in formation of ER-derived transport vesicles, namely p58/ERGIC 53, Sec23p, and Sec13p, were concentrated in the E1-containing pre-Golgi compartment. Furthermore, budding structures were evident in these membrane profiles, and a highly abundant but unknown 65-kDa protein was also present. By comparison, marker proteins of the rough ER, Golgi, and COPI vesicles were not enriched in these membranes. These results demonstrate that the composition of the tubular networks corresponds to that expected of ER exit sites. Accordingly, we propose the name SEREC (smooth ER exit compartment) for this structure.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.