ArticleThe Journal of cell biology1995
Macromolecular interactions in the nucleoporin p62 complex of rat nuclear pores: binding of nucleoporin p54 to the rod domain of p62.
Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 59 citations in OpenAlex.
- 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
- Ordered Regions of Channel Nucleoporins Nup62, Nup54, and Nup58 Form Dynamic Complexes in Solution.The Journal of biological chemistry · 2015Article
- The stoichiometry of the nucleoporin 62 subcomplex of the nuclear pore in solution.Molecular biology of the cell · 2014Article
- Article
- Specific cleavage of the nuclear pore complex protein Nup62 by a viral protease.The Journal of biological chemistry · 2010Article
- The Nsp1p carboxy-terminal domain is organized into functionally distinct coiled-coil regions required for assembly of nucleoporin subcomplexes and nucleocytoplasmic transport.Molecular and cellular biology · 2001Article
- Interaction of the influenza virus nucleoprotein with the cellular CRM1-mediated nuclear export pathway.Journal of virology · 2001Article
- The nuclear pore complex.Plant molecular biology · 1998Review
- Major binding sites for the nuclear import receptor are the internal nucleoporin Nup153 and the adjacent nuclear filament protein Tpr.The Journal of cell biology · 1998Article
- Involvement of p62 nucleoporin in angiotensin II-induced nuclear translocation of STAT3 in brain neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1998Article
- Nup93, a vertebrate homologue of yeast Nic96p, forms a complex with a novel 205-kDa protein and is required for correct nuclear pore assembly.Molecular biology of the cell · 1997Article
- Nup84, a novel nucleoporin that is associated with CAN/Nup214 on the cytoplasmic face of the nuclear pore complex.The Journal of cell biology · 1997Article
- In vitro reconstitution of a heterotrimeric nucleoporin complex consisting of recombinant Nsp1p, Nup49p, and Nup57p.Molecular biology of the cell · 1997Article
- Molecular and functional characterization of the p62 complex, an assembly of nuclear pore complex glycoproteins.The Journal of cell biology · 1996Article
- Nic96p is required for nuclear pore formation and functionally interacts with a novel nucleoporin, Nup188p.The Journal of cell biology · 1996Article
- Nuclear pore complex clustering and nuclear accumulation of poly(A)+ RNA associated with mutation of the Saccharomyces cerevisiae RAT2/NUP120 gene.The Journal of cell biology · 1995Article
- Structural analysis of the p62 complex, an assembly of O-linked glycoproteins that localizes near the central gated channel of the nuclear pore complex.Molecular biology of the cell · 1995Article
- A novel nuclear pore protein Nup82p which specifically binds to a fraction of Nsp1p.The Journal of cell biology · 1995Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nuclear pore complexes are constructed from a large number of different proteins, called collectively nucleoporins. One of these nucleoporins, p62, has an alpha-helical coiled-coil COOH-terminal rod domain linked to an NH2-terminal domain that contains a series of degenerate pentapeptide repeats. In nuclear pores p62 forms a tight complex with at least two other proteins, p58 and p54, which can be extracted from isolated rat liver nuclei (Finlay, D. R., E. Meier, P. Bradley, J. Horecka, and D. J. Forbes. 1991. J. Cell Biol. 114:169-183). We have used a range of methods to demonstrate a strong binding between p62 and p54 in this complex and show that the rod domain of p62 appears to constitute the principal binding site for p54. Whole p62 and its rod domain expressed in Escherichia coli both bind strongly to p54 in blot-overlay assays. Most of the epitopes on the p62 rod recognized by polyclonal antisera are masked in the complex, whereas epitopes on the NH2-terminal domain of p62 are still exposed, both in the isolated complex and also in nuclear pores stained in situ by immunofluorescence in isolated rat nuclei. Moreover, it has been possible to exchange recombinant p62 rod for some of the native p62 in complexes partially dissociated by 4 M urea. Overall these results suggest a key role for the p62 rod domain in maintaining the structural integrity of the complex and also suggest a molecular model for the complex. This model is consistent with data that indicate that the analogous coiled-coil region of yeast nucleoporin NSP1 may function in a similar way.
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