ArticlePloS one2014
The interaction of CRM1 and the nuclear pore protein Tpr.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Intrinsically disordered regions facilitate Mlp1-Nab2 recognition in mRNA quality control.Nucleus (Austin, Tex.) · 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
- Spelling out the roles of individual nucleoporins in nuclear export of mRNA.Nucleus (Austin, Tex.) · 2022Review
- On the nuclear pore complex and its emerging role in cellular mechanotransduction.APL bioengineering · 2022Review
- Enhanced Nucleocytoplasmic Transport due to Competition for Elastic Binding Sites.Biophysical journal · 2018Article
- Modeling of the mechano-chemical behaviour of the nuclear pore complex: current research and perspectives.Integrative biology : quantitative biosciences from nano to macro · 2016Review
- Rapid Brownian Motion Primes Ultrafast Reconstruction of Intrinsically Disordered Phe-Gly Repeats Inside the Nuclear Pore Complex.Scientific reports · 2016Article
- Dynamic Regulation of α-Actinin's Calponin Homology Domains on F-Actin.Biophysical journal · 2016Article
- Insights into the Structural Dynamics of Nucleocytoplasmic Transport of tRNA by Exportin-t.Biophysical journal · 2016Article
- Evolutionarily Conserved Sequence Features Regulate the Formation of the FG Network at the Center of the Nuclear Pore Complex.Scientific reports · 2015Article
- Review
- The interaction of RNA helicase DDX3 with HIV-1 Rev-CRM1-RanGTP complex during the HIV replication cycle.PloS one · 2015Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
While much has been devoted to the study of transport mechanisms through the nuclear pore complex (NPC), the specifics of interactions and binding between export transport receptors and the NPC periphery have remained elusive. Recent work has demonstrated a binding interaction between the exportin CRM1 and the unstructured carboxylic tail of Tpr, on the nuclear basket. Strong evidence suggests that this interaction is vital to the functions of CRM1. Using molecular dynamics simulations and a newly refined method for determining binding regions, we have identified nine candidate binding sites on CRM1 for C-Tpr. These include two adjacent to RanGTP--from which one is blocked in the absence of RanGTP--and three next to the binding region of the cargo Snurportin. We report two additional interaction sites between C-Tpr and Snurportin, suggesting a possible role for Tpr import into the nucleus. Using bioinformatics tools we have conducted conservation analysis and functional residue prediction investigations to identify which parts of the obtained binding sites are inherently more important and should be highlighted. Also, a novel measure based on the ratio of available solvent accessible surface (RASAS) is proposed for monitoring the ligand/receptor binding process.
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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.