ArticleThe Journal of cell biology1992
The single transmembrane segment of gp210 is sufficient for sorting to the pore membrane domain of the nuclear envelope.
Article in The Journal of cell biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 117 citations in OpenAlex.
- The nuclear envelope protein TMEM209 is an integral component of the nuclear pore complex and interacts with Nup210.Journal of cell science · 2026Article
- Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026Review
- Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025Review
- Advances in the understanding of nuclear pore complexes in human diseases.Journal of cancer research and clinical oncology · 2024Review
- Article
- Loss of Nup210 results in muscle repair delays and age-associated alterations in muscle integrity.Life science alliance · 2022Article
- Structure, Maintenance, and Regulation of Nuclear Pore Complexes: The Gatekeepers of the Eukaryotic Genome.Cold Spring Harbor perspectives in biology · 2022Review
- Characterization of nuclear pore complex targeting domains in Pom152 in Saccharomyces cerevisiae.Biology open · 2021Article
- The Quest for the Blueprint of the Nuclear Pore Complex.The protein journal · 2019Review
- Identification of Epigenetic Biomarkers of Lung Adenocarcinoma through Multi-Omics Data Analysis.PloS one · 2016Article
- The nucleoporin gp210/Nup210 controls muscle differentiation by regulating nuclear envelope/ER homeostasis.The Journal of cell biology · 2015Article
- Role of the Ndc1 interaction network in yeast nuclear pore complex assembly and maintenance.The Journal of cell biology · 2009Article
- Distinct functions of the Drosophila Nup153 and Nup214 FG domains in nuclear protein transport.The Journal of cell biology · 2007Article
- Dependence of diffusional mobility of integral inner nuclear membrane proteins on A-type lamins.Biochemistry · 2006Article
- The AAA+ protein torsinA interacts with a conserved domain present in LAP1 and a novel ER protein.The Journal of cell biology · 2005Article
- Interference with the cytoplasmic tail of gp210 disrupts "close apposition" of nuclear membranes and blocks nuclear pore dilation.The Journal of cell biology · 2002Article
- Nuclear pore complexes form immobile networks and have a very low turnover in live mammalian cells.The Journal of cell biology · 2001Article
- Identification of a new vertebrate nucleoporin, Nup188, with the use of a novel organelle trap assay.Molecular biology of the cell · 2000Article
- Charged residues in the transmembrane domains of hepatitis C virus glycoproteins play a major role in the processing, subcellular localization, and assembly of these envelope proteins.Journal of virology · 2000Article
- Localization of ribophorin II to the endoplasmic reticulum involves both its transmembrane and cytoplasmic domains.European journal of cell biology · 2000Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The glycoprotein gp210 is located in the "pore membrane," a specialized domain of the nuclear envelope to which the nuclear pore complex (NPC) is anchored. gp210 contains a large cisternal domain, a single transmembrane segment (TM), and a COOH-terminal, 58-amino acid residue cytoplasmic tail (CT) (Wozniak, R. W., E. Bartnik, and G. Blobel. 1989. J. Cell Biol. 108:2083-2092; Greber, U. F., A. Senior, and L. Gerace. 1990. EMBO (Eur. Mol. Biol. Organ.) J. 9:1495-1502). To locate determinants for sorting of gp210 to the pore membrane, we constructed various cDNAs coding for wild-type, mutant, and chimeric gp210, and monitored localization of the expressed protein in 3T3 cells by immunofluorescence microscopy using appropriate antibodies. The large cisternal domain of gp210 (95% of its mass) did not reveal any sorting determinants. Surprisingly, the TM of gp210 is sufficient for sorting to the pore membrane. The CT also contains a sorting determinant, but it is weaker than that of the TM. We propose specific lateral association of the transmembrane helices of two proteins to yield either a gp210 homodimer or a heterodimer of gp210 and another protein. The cytoplasmically oriented tails of these dimers may bind cooperatively to the adjacent NPCs. In addition, we demonstrate that gp210 co-localizes with cytoplasmically dispersed nucleoporins, suggesting a cytoplasmic association of these components.
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