ArticleMolecular biology of the cell2005
Vertebrate Nup53 interacts with the nuclear lamina and is required for the assembly of a Nup93-containing complex.
Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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Who cites it
70 citing papers in PubMed, 133 citations in OpenAlex.
- Mechanotransduction by nuclear envelope tension.Nucleus (Austin, Tex.) · 2026Review
- Ultrastructure Expansion Microscopy applied tomicroPublication biology · 2024Article
- ADAD1 is required for normal translation of nuclear pore and transport protein transcripts in spermatids of Mus musculus†.Biology of reproduction · 2023Article
- Differentially Expressed Genes Regulating Glutathione Metabolism, Protein-Folding, and Unfolded Protein Response in Pancreatic β-Cells in Type 2 Diabetes Mellitus.International journal of molecular sciences · 2023Article
- Mechanisms of nuclear pore complex disassembly by the mitotic Polo-like kinase 1 (PLK-1) inScience advances · 2023Article
- Nuclear F-actin and Lamin A antagonistically modulate nuclear shape.Journal of cell science · 2022Article
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- Nuclear Morphological Abnormalities in Cancer: A Search for Unifying Mechanisms.Results and problems in cell differentiation · 2022Article
- Review
- A single-molecule localization microscopy method for tissues reveals nonrandom nuclear pore distribution in Drosophila.Journal of cell science · 2021Article
- Review
- Regulation of diverse nuclear shapes: pathways working independently, together.Communicative & integrative biology · 2021Review
- Biallelic loss of function NEK3 mutations deacetylate α-tubulin and downregulate NUP205 that predispose individuals to cilia-related abnormal cardiac left-right patterning.Cell death & disease · 2020Article
- Article
- The Quest for the Blueprint of the Nuclear Pore Complex.The protein journal · 2019Review
- The Biology of the Nuclear Envelope and Its Implications in Cancer Biology.International journal of molecular sciences · 2019Review
- Article
- Lamin A mutation impairs interaction with nucleoporin NUP155 and disrupts nucleocytoplasmic transport in atrial fibrillation.Human mutation · 2019Article
- Moonlighting nuclear pore proteins: tissue-specific nucleoporin function in health and disease.Histochemistry and cell biology · 2018Review
- Mitotic Disassembly of Nuclear Pore Complexes Involves CDK1- and PLK1-Mediated Phosphorylation of Key Interconnecting Nucleoporins.Developmental cell · 2017Article
10 more citing papers are in PubMed but not listed here.
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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
The nuclear pore complex (NPC) is an evolutionarily conserved structure that mediates exchange of macromolecules across the nuclear envelope (NE). It is comprised of approximately 30 proteins termed nucleoporins that are each present in multiple copies. We have investigated the function of the human nucleoporin Nup53, the ortholog of Saccharomyces cerevisiae Nup53p. Both cell fractionation and in vitro binding data suggest that Nup53 is tightly associated with the NE membrane and the lamina where it interacts with lamin B. We have also shown that Nup53 is capable of physically interacting with a group of nucleoporins including Nup93, Nup155, and Nup205. Consistent with this observation, depletion of Nup53 using small interfering RNAs causes a decrease in the cellular levels of these nucleoporins as well as the spindle checkpoint protein Mad1, likely due to destabilization of Nup53-containing complexes. The cellular depletion of this group of nucleoporins, induced by depleting either Nup53 or Nup93, severely alters nuclear morphology producing phenotypes similar to that previously observed in cells depleted of lamin A and Mad1. On basis of these data, we propose a model in which Nup53 is positioned near the pore membrane and the lamina where it anchors an NPC subcomplex containing Nup93, Nup155, and Nup205.
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