ArticleThe Journal of cell biology1996
Molecular and functional characterization of the p62 complex, an assembly of nuclear pore complex glycoproteins.
Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.
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Who cites it
81 citing papers in PubMed, 175 citations in OpenAlex.
- 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
- Modeling HIV-1 nuclear entry with nucleoporin-gated DNA-origami channels.Nature structural & molecular biology · 2023Article
- Nuclear Import of HIV-1.Viruses · 2021Review
- Cellular Importin-α3 Expression Dynamics in the Lung Regulate Antiviral Response Pathways against Influenza A Virus Infection.Cell reports · 2020Article
- Nuclear Export of Cyclin B Mediated by the Nup62 Complex Is Required for Meiotic Initiation inCells · 2020Article
- Article
- Porcine Reproductive and Respiratory Syndrome Virus Nonstructural Protein 1 Beta Interacts with Nucleoporin 62 To Promote Viral Replication and Immune Evasion.Journal of virology · 2019Article
- Extensive Identification and In-depth Validation of Importin 13 Cargoes.Molecular & cellular proteomics : MCP · 2018Article
- In vivo analysis of protein crowding within the nuclear pore complex in interphase and mitosis.Scientific reports · 2017Article
- Expansion of divergent SEA domains in cell surface proteins and nucleoporin 54.Protein science : a publication of the Protein Society · 2017Article
- Structure Determination of the Nuclear Pore Complex with Three-Dimensional Cryo electron Microscopy.Journal of molecular biology · 2016Review
- Article
- Architecture of the fungal nuclear pore inner ring complex.Science (New York, N.Y.) · 2015Article
- Ordered Regions of Channel Nucleoporins Nup62, Nup54, and Nup58 Form Dynamic Complexes in Solution.The Journal of biological chemistry · 2015Article
- Nucleoporin 62-like protein activates canonical Wnt signaling through facilitating the nuclear import of β-catenin in zebrafish.Molecular and cellular biology · 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
- The stoichiometry of the nucleoporin 62 subcomplex of the nuclear pore in solution.Molecular biology of the cell · 2014Article
- Nucleoporin Nup62 maintains centrosome homeostasis.Cell cycle (Georgetown, Tex.) · 2013Article
- Behavioral effects of SQSTM1/p62 overexpression in mice: support for a mitochondrial role in depression and anxiety.Behavioural brain research · 2013Article
21 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Macromolecular trafficking across the nuclear envelope involves interactions between cytosolic transport factors and nuclear pore complex proteins. The p62 complex, an assembly of 62, 58, 54, and 45-kD O-linked glycoproteins-localized near the central gated channel of the nuclear pore complex, has been directly implicated in nuclear protein import. The cDNA cloning of rat p62 was reported previously. We have now carried out cDNA cloning of rat p58, p54, and p45. We found that p58 contains regions with FG (Phe, Gly) and PA (Pro, Ala) repeats at both its NH2 and COOH termini separated by a predicted alpha-helical coiled-coil region, while p54 has an NH2-terminal FG and PA repeat region and a COOH-terminal predicted coiled-coil region. p45 and p58 appear to be generated by alternative splicing, with p45 containing the NH2-terminal FG repeat region and the coiled-coil region of p58. Using immunogold electron microscopy, we found that p58/p45 and p54 are localized on both sides of the nuclear pore complex, like p62. Previous studies have shown that immobilized recombinant p62 can bind the cytosolic nuclear import factor NTF2 and thereby deplete transport activity from cytosol. We have now found that immobilized recombinant p58 and p54 also can deplete nuclear transport activity from cytosol, and that p62, p58, and p54 bind directly to the cytosolic nuclear import factors p97 and NTF2. At least in the case of p58, this involves FG repeat regions. Moreover, p58 can bind to a complex containing transport ligand, the nuclear localization sequence receptor (Srp1 alpha) and p97. These data support a model in which the p62 complex binds to a multicomponent particle consisting of transport ligand and cytosolic factors to achieve accumulation of ligand near the central gated channel of the nuclear pore complex.
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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.