ArticleBiophysical journal2005
Nuclear localization signal peptides induce molecular delivery along microtubules.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 108 citations in OpenAlex.
- Reversing drug resistance of soft tumor-repopulating cells by tumor cell-derived chemotherapeutic microparticles.Cell research · 2016Trial
- Modelling nano-particle-PEG-NLS complexes for nucleus-targeted drug delivery: revisiting the multi-dynein nano-cargo transport on microtubules.Drug delivery · 2026Article
- Myosin VIII and XI isoforms interact with the Agrobacterium VirE2 protein and facilitate its transport from the plasma membrane to the perinuclear region during plant transformation.Plant communications · 2026Article
- Discovering the nuclear localization signal universe through a deep learning model with interpretable attention units.Patterns (New York, N.Y.) · 2025Article
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- Polymer Chemistry in Living Cells.Accounts of chemical research · 2022Article
- Nano-Particles Carried by Multiple Dynein Motors Self-Regulate Their Number of Actively Participating Motors.International journal of molecular sciences · 2021Article
- Wake-sleep cycles are severely disrupted by diseases affecting cytoplasmic homeostasis.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Live cell imaging reveals 3'-UTR dependent mRNA sorting to synapses.Nature communications · 2019Article
- Cytoplasmic transport and nuclear import of plasmid DNA.Bioscience reports · 2017Review
- Article
- Agrobacterium-mediated plant transformation: biology and applications.The arabidopsis book · 2017Article
- Triggering signaling pathways using F-actin self-organization.Scientific reports · 2016Article
- Yeast Actin-Related Protein ARP6 Negatively Regulates Agrobacterium-Mediated Transformation of Yeast Cell.BioMed research international · 2015Article
- Visualization of VirE2 protein translocation by the Agrobacterium type IV secretion system into host cells.MicrobiologyOpen · 2014Article
- Perturbing microtubule integrity blocks AMP-activated protein kinase-induced meiotic resumption in cultured mouse oocytes.Zygote (Cambridge, England) · 2014Article
- Kinesin KIFC1 actively transports bare double-stranded DNA.Nucleic acids research · 2013Article
- Article
- The roles of bacterial and host plant factors in Agrobacterium-mediated genetic transformation.The International journal of developmental biology · 2013Review
- Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many essential processes in eukaryotic cells depend on regulated molecular exchange between its two major compartments, the cytoplasm and the nucleus. In general, nuclear import of macromolecular complexes is dependent on specific peptide signals and their recognition by receptors that mediate translocation through the nuclear pores. Here we address the question of how protein products bearing such nuclear localization signals arrive at the nuclear membrane before import, i.e., by simple diffusion or perhaps with assistance of cytoskeletal elements or cytoskeleton-associated motor proteins. Using direct single-particle tracking and detailed statistical analysis, we show that the presence of nuclear localization signals invokes active transport along microtubules in a cell-free Xenopus egg extract. Chemical and antibody inhibition of minus-end directed cytoplasmic dynein blocks this active movement. In the intact cell, where microtubules project radially from the centrosome, such an interaction would effectively deliver nuclear-targeted cargo to the nuclear envelope in preparation for import.
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Registered trials
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.