ArticleMolecular biology of the cell2011
Evolutionary development of redundant nuclear localization signals in the mRNA export factor NXF1.
Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 28 citations in OpenAlex.
- Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023Review
- A new Karyopherin-β2 binding PY-NLS epitope of HNRNPH2 linked to neurodevelopmental disorders.Structure (London, England : 1993) · 2023Article
- Augmin is a Ran-regulated spindle assembly factor.The Journal of biological chemistry · 2023Article
- Heterozygous frameshift variants in HNRNPA2B1 cause early-onset oculopharyngeal muscular dystrophy.Nature communications · 2022Article
- Measuring and Interpreting Nuclear Transport in Neurodegenerative Disease-The Example of C9orf72 ALS.International journal of molecular sciences · 2021Review
- Article
- Recognition Elements in the Histone H3 and H4 Tails for Seven Different Importins.The Journal of biological chemistry · 2016Article
- Importin β2 Mediates the Spatio-temporal Regulation of Anillin through a Noncanonical Nuclear Localization Signal.The Journal of biological chemistry · 2015Article
- Evolutionary conservation of a molecular machinery for export and expression of mRNAs with retained introns.RNA (New York, N.Y.) · 2015Article
- Enriching the pore: splendid complexity from humble origins.Traffic (Copenhagen, Denmark) · 2014Review
- A multifunctional, multi-pathway intracellular localization signal in Huntingtin.Communicative & integrative biology · 2013Article
- Identification of cargo proteins specific for the nucleocytoplasmic transport carrier transportin by combination of an in vitro transport system and stable isotope labeling by amino acids in cell culture (SILAC)-based quantitative proteomics.Molecular & cellular proteomics : MCP · 2013Article
- Identification of a karyopherin β1/β2 proline-tyrosine nuclear localization signal in huntingtin protein.The Journal of biological chemistry · 2012Article
- Structural and energetic basis of ALS-causing mutations in the atypical proline-tyrosine nuclear localization signal of the Fused in Sarcoma protein (FUS).Proceedings of the National Academy of Sciences of the United States of America · 2012Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
In human cells, the mRNA export factor NXF1 resides in the nucleoplasm and at nuclear pore complexes. Karyopherin β2 or transportin recognizes a proline-tyrosine nuclear localization signal (PY-NLS) in the N-terminal tail of NXF1 and imports it into the nucleus. Here biochemical and cellular studies to understand the energetic organization of the NXF1 PY-NLS reveal unexpected redundancy in the nuclear import pathways used by NXF1. Human NXF1 can be imported via importin β, karyopherin β2, importin 4, importin 11, and importin α. Two NLS epitopes within the N-terminal tail, an N-terminal basic segment and a C-terminal R-X(2-5)-P-Y motif, provide the majority of binding energy for all five karyopherins. Mutation of both NLS epitopes abolishes binding to the karyopherins, mislocalized NXF1 to the cytoplasm, and significantly compromised its mRNA export function. The understanding of how different karyopherins recognize human NXF1, the examination of NXF1 sequences from divergent eukaryotes, and the interactions of NXF1 homologues with various karyopherins reveals the evolutionary development of redundant NLSs in NXF1 of higher eukaryotes. Redundancy of nuclear import pathways for NXF1 increases progressively from fungi to nematodes and insects to chordates, potentially paralleling the increasing complexity in mRNA export regulation and the evolution of new nuclear functions for NXF1.
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