ArticleThe Journal of cell biology1991
A complex of nuclear pore proteins required for pore function.
Article in The Journal of cell biology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.
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Who cites it
99 citing papers in PubMed, 233 citations in OpenAlex.
- NUP62 Elevates USP10 Expression and Promotes Tamoxifen Resistance of Breast Cancer by Deubiquitinating ERα.Annals of surgical oncology · 2026Article
- Nuclear pore and nucleocytoplasmic transport impairment in oxidative stress-induced neurodegeneration: relevance to molecular mechanisms in Pathogenesis of Parkinson's and other related neurodegenerative diseases.Molecular neurodegeneration · 2024Review
- Transport of Acrosomal Enzymes by KIFC1 via the Acroframosomal Cytoskeleton during Spermatogenesis inAnimals : an open access journal from MDPI · 2022Article
- Structure, Maintenance, and Regulation of Nuclear Pore Complexes: The Gatekeepers of the Eukaryotic Genome.Cold Spring Harbor perspectives in biology · 2022Review
- Molecular and structural analysis of central transport channel in complex with Nup93 of nuclear pore complex.Protein science : a publication of the Protein Society · 2020Article
- The Structure of the Nuclear Pore Complex (An Update).Annual review of biochemistry · 2019Review
- Nucleoporin 54 contributes to homologous recombination repair and post-replicative DNA integrity.Nucleic acids research · 2018Article
- Valproic acid disrupts the oscillatory expression of core circadian rhythm transcription factors.Toxicology and applied pharmacology · 2018Article
- A statistical image analysis framework for pore-free islands derived from heterogeneity distribution of nuclear pore complexes.Scientific reports · 2017Article
- In vivo analysis of protein crowding within the nuclear pore complex in interphase and mitosis.Scientific reports · 2017Article
- The nuclear pore complex: understanding its function through structural insight.Nature reviews. Molecular cell biology · 2017Review
- Systematic Protein-Protein Interaction Analysis Reveals Intersubcomplex Contacts in the Nuclear Pore Complex.Molecular & cellular proteomics : MCP · 2016Article
- The Structure Inventory of the Nuclear Pore Complex.Journal of molecular biology · 2016Review
- Gated entry into the ciliary compartment.Cellular and molecular life sciences : CMLS · 2016Review
- Article
- Ordered Regions of Channel Nucleoporins Nup62, Nup54, and Nup58 Form Dynamic Complexes in Solution.The Journal of biological chemistry · 2015Article
- The nuclear pore complex--structure and function at a glance.Journal of cell science · 2015Review
- Analysis of the initiation of nuclear pore assembly by ectopically targeting nucleoporins to chromatin.Nucleus (Austin, Tex.) · 2015Article
- An assay for clogging the ciliary pore complex distinguishes mechanisms of cytosolic and membrane protein entry.Current biology : CB · 2014Article
- Probing nuclear pore complex architecture with proximity-dependent biotinylation.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
39 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
A family of proteins bearing novel N-acetylglucosamine residues has previously been found to be required to form functional nuclear pores. To begin to determine which of the proteins in this family are essential for pore function, antisera were raised to each of three members of the family, p62, p58, and p54. With these antisera, it was possible to deplete nuclear reconstitution extracts of the proteins and to test the depleted nuclei for nuclear transport. In the course of the experiments, it was found that the three proteins exist as a complex; antisera to any one, while specific on a protein blot, coimmunoprecipitated all three proteins. This complex of pore proteins is stable to 2 M salt, 2 M urea, and the detergent Mega 10, indicating the presence of specific and tight protein-protein interactions. By gel filtration, the complex has a molecular mass of 550-600 kD. Nuclei containing pores depleted of the complex are found to be defective for nuclear transport; moreover, we observe a strict linear correlation between the amount of complex present in nuclei and the amount of nuclear transport of which those nuclei are capable. Thus, the p62-p58-p54 complex defines a group of proteins with strong protein-protein interactions that form a unit of pore structure essential for pore function.
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Registered trials
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.