ArticleMolecular biology of the cell2007
Dynein light chain association sequences can facilitate nuclear protein import.
Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 82 citations in OpenAlex.
- Conformational dynamics, RNA binding, and phase separation regulate the multifunctionality of rabies virus P protein.Nature communications · 2025Article
- Structural insights into the multifunctionality of rabies virus P3 protein.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Prospects of Using Protein Engineering for Selective Drug Delivery into a Specific Compartment of Target Cells.Pharmaceutics · 2023Review
- Microtubules in Influenza Virus Entry and Egress.Viruses · 2020Review
- Microtubules: Evolving roles and critical cellular interactions.Experimental biology and medicine (Maywood, N.J.) · 2019Review
- Exportin-1-Dependent Nuclear Export of DEAD-box Helicase DDX3X is Central to its Role in Antiviral Immunity.Cells · 2019Article
- Dynein Light Chain DLC-1 Facilitates the Function of the Germline Cell Fate Regulator GLD-1 inGenetics · 2019Article
- Recognition by host nuclear transport proteins drives disorder-to-order transition in Hendra virus V.Scientific reports · 2018Article
- Peptides mediating DNA transport on microtubules and their impact on non-viral gene transfer efficiency.Bioscience reports · 2017Review
- C3G shows regulated nucleocytoplasmic exchange and represses histone modifications associated with euchromatin.Molecular biology of the cell · 2017Article
- The importance of immune evasion in the pathogenesis of rabies virus.The Journal of veterinary medical science · 2016Review
- Article
- Wongabel rhabdovirus accessory protein U3 targets the SWI/SNF chromatin remodeling complex.Journal of virology · 2015Article
- Rabies virus envelope glycoprotein targets lentiviral vectors to the axonal retrograde pathway in motor neurons.The Journal of biological chemistry · 2014Article
- Bovine ephemeral fever rhabdovirus α1 protein has viroporin-like properties and binds importin β1 and importin 7.Journal of virology · 2014Article
- Cytoplasmic retention of a nucleocytoplasmic protein TBC1D3 by microtubule network is required for enhanced EGFR signaling.PloS one · 2014Article
- Strategies on the nuclear-targeted delivery of genes.Journal of drug targeting · 2013Review
- Particle tracking analysis for the intracellular trafficking of nanoparticles modified with African swine fever virus protein p54-derived peptide.Molecular therapy : the journal of the American Society of Gene Therapy · 2013Article
- Conservation of a unique mechanism of immune evasion across the Lyssavirus genus.Journal of virology · 2012Article
- A novel nuclear trafficking module regulates the nucleocytoplasmic localization of the rabies virus interferon antagonist, P protein.The Journal of biological chemistry · 2012Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nuclear localization sequence (NLS)-dependent nuclear protein import is not conventionally held to require interaction with microtubules (MTs) or components of the MT motor, dynein. Here we report for the first time the role of sequences conferring association with dynein light chains (DLCs) in NLS-dependent nuclear accumulation of the rabies virus P-protein. We find that P-protein nuclear accumulation is significantly enhanced by its dynein light chain association sequence (DLC-AS), dependent on MT integrity and association with DLCs, and that P-protein-DLC complexes can associate with MT cytoskeletal structures. We also find that P-protein DLC-AS, as well as analogous sequences from other proteins, acts as an independent module that can confer enhancement of nuclear accumulation to proteins carrying the P-protein NLS, as well as several heterologous NLSs. Photobleaching experiments in live cells demonstrate that the MT-dependent enhancement of NLS-mediated nuclear accumulation by the P-protein DLC-AS involves an increased rate of nuclear import. This is the first report of DLC-AS enhancement of NLS function, identifying a novel mechanism regulating nuclear transport with relevance to viral and cellular protein biology. Importantly, this data indicates that DLC-ASs represent versatile modules to enhance nuclear delivery with potential therapeutic application.
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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.