The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
African Swine Fever Virus Protein p54 Interacts with the Microtubular Motor Complex through Direct Binding to Light-Chain Dynein
Open accessAbstract
Dynein is a minus-end-directed microtubule-associated motor protein involved in cargo transport in the cytoplasm. African swine fever virus (ASFV), a large DNA virus, hijacks the microtubule motor complex cellular transport machinery during virus infection of the cell through direct binding of virus protein p54 to the light chain of cytoplasmic dynein (LC8). Interaction of p54 and LC8 occurs both in vitro and in cells, and the two proteins colocalize at the microtubular organizing center during viral infection. p50/dynamitin, a dominant-negative inhibitor of dynein-dynactin function, impeded ASFV infection, suggesting an essential role for dynein during virus infection. A 13-amino-acid domain of p54 was sufficient for binding to LC8, an SQT motif within this domain being critical for this binding. Direct binding of a viral structural protein to LC8, a small molecule of the dynein motor complex, could constitute a molecular mechanism for microtubule-mediated virus transport.
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Citations
Cites
Dynein- and microtubule-mediated translocation of adenovirus serotype 5 occurs after endosomal lysis
Leopold, P. L., Kreitzer, G., Miyazawa, N., Rempel, S., Pfister, K. K., Rodriguez-Boulan, E., & Crystal, R. G. (2000) · Human Gene Therapy · doi:10.1089/10430340050016238 · Cited by 254
Cited by
The cytoplasmic dynein transport machinery and its many cargoes
Reck-Peterson, S. L., Redwine, W. B., Vale, R. D., & Carter, A. P. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0004-3 · Cited by 659
Dynein: An ancient motor protein involved in multiple modes of transport
Vallee, R. B., Williams, J. C., Varma, D., & Barnhart, L. E. (2004) · Journal of Neurobiology · doi:10.1002/neu.10314 · Cited by 411
A Superhighway to Virus Infection
Greber, U. F., & Way, M. (2006) · Cell · doi:10.1016/j.cell.2006.02.018 · Cited by 383
Metadata
- Authors
- Alonso, C., Miskin, J., Hernáez, B., Fernandez-Zapatero, P., Soto, L., Cantó, C., Rodrı́guez-Crespo, I., Dixon, L., & Escribano, J. M.
- Venue
- Journal of Virology
- Publisher
- American Society for Microbiology
- Published
- 2001-10-15
- Volume
- 75
- Issue
- 20
- Pages
- 9819-9827
- ISSN
- 0022-538X (ISSN-L)
- 1098-5514
- OpenAlex
- W2137115293
- Cited by
- 201
- References
- 1
- FWCI
- 20.97
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: African Swine Fever Virus Protein p54 Interacts with the Microtubular Motor Complex through Direct Binding to Light-Chain Dynein. https://app.cochat.ai/papers/10.1128/jvi.75.20.9819-9827.2001
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- Alonso, C., Miskin, J., Hernáez, B., Fernandez-Zapatero, P., Soto, L., Cantó, C., Rodrı́guez-Crespo, I., Dixon, L., & Escribano, J. M. (2001). African Swine Fever Virus Protein p54 Interacts with the Microtubular Motor Complex through Direct Binding to Light-Chain Dynein. Journal of Virology. https://doi.org/10.1128/jvi.75.20.9819-9827.2001
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
