ArticleMolecular biology of the cell1997
Functional domains in nuclear import factor p97 for binding the nuclear localization sequence receptor and the nuclear pore.
Article in Molecular biology of the cell, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 86 citations in OpenAlex.
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- A Novel Mutation in Cse1l Disrupts Brain and Eye Development with Specific Effects on Pax6 Expression.Journal of developmental biology · 2021Article
- Importin-9 regulates chromosome segregation and packaging in Drosophila germ cells.Journal of cell science · 2021Article
- Importin-11 is Essential for Normal Embryonic Development in Mice.International journal of medical sciences · 2020Article
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- The nuclear pore complex and nuclear transport.Cold Spring Harbor perspectives in biology · 2010Review
- Notch1 signaling is mediated by importins alpha 3, 4, and 7.Cellular and molecular life sciences : CMLS · 2010Article
- The design of Förster (fluorescence) resonance energy transfer (FRET)-based molecular sensors for Ran GTPase.Methods (San Diego, Calif.) · 2010Review
- Avian reovirus sigmaA localizes to the nucleolus and enters the nucleus by a nonclassical energy- and carrier-independent pathway.Journal of virology · 2009Article
- Functionalization of a nanopore: the nuclear pore complex paradigm.Biochimica et biophysica acta · 2009Review
- Cargo surface hydrophobicity is sufficient to overcome the nuclear pore complex selectivity barrier.The EMBO journal · 2009Article
- The Nup358-RanGAP complex is required for efficient importin alpha/beta-dependent nuclear import.Molecular biology of the cell · 2008Article
- Nucleocytoplasmic shuttling by nucleoporins Nup153 and Nup214 and CRM1-dependent nuclear export control the subcellular distribution of latent Stat1.The Journal of cell biology · 2004Article
- Importin beta contains a COOH-terminal nucleoporin binding region important for nuclear transport.The Journal of cell biology · 2003Article
- Steady-state nuclear localization of exportin-t involves RanGTP binding and two distinct nuclear pore complex interaction domains.Molecular and cellular biology · 2002Article
- Transport into and out of the nucleus.Microbiology and molecular biology reviews : MMBR · 2001Review
- Cse1l is essential for early embryonic growth and development.Molecular and cellular biology · 2001Article
- Gradient of increasing affinity of importin beta for nucleoporins along the pathway of nuclear import.The Journal of cell biology · 2001Article
- Importin-beta-like nuclear transport receptors.Genome biology · 2001Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The interaction of the nuclear protein import factor p97 with the nuclear localization sequence (NLS) receptor, the nuclear pore complex, and Ran/TC4 is important for coordinating the events of protein import to the nucleus. We have mapped the binding domains on p97 for the NLS receptor and the nuclear pore. The NLS receptor-binding domain of p97 maps to the C-terminal 60% of the protein between residues 356 and 876. The pore complex-binding domain of p97 maps to residues 152-352. The pore complex-binding domain overlaps the Ran-GTP- and Ran-GDP-binding domains on p97, but only Ran-GTP competes for docking in permeabilized cells. The N-ethylmaleimide sensitivity of the p97 for docking was investigated and found to be due to inhibition of p97 binding to the pore complex and to the NLS receptor. Site-directed mutagenesis of conserved cysteine residues in the pore- and receptor-binding domains identified two cysteines, C223 and C228, that were required for p97 to bind the nuclear pore. Inhibition studies on docking and accumulation of a NLS protein provided additional evidence that the domains identified biochemically are the functional domains involved in protein import. Together, these results suggest that Ran-GTP dissociates the receptor complex and prevents p97 binding to the pore by inducing a conformational change in the structure of p97 rather than simple competition for binding sites.
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