ArticleJournal of virology2009
Reovirus FAST protein transmembrane domains function in a modular, primary sequence-independent manner to mediate cell-cell membrane fusion.
Article in Journal of virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 49 citations in OpenAlex.
- Article
- Multiple rotavirus species encode fusion-associated small transmembrane (FAST) proteins with cell type-specific activity.Journal of virology · 2025Article
- Fusogenic vesicular stomatitis virus combined with natural killer T cell immunotherapy controls metastatic breast cancer.Breast cancer research : BCR · 2024Article
- Monocyte-Macrophage Lineage Cell Fusion.International journal of molecular sciences · 2022Review
- Review
- Polycistronic Genome Segment Evolution and Gain and Loss of FAST Protein Function during Fusogenic Orthoreovirus Speciation.Viruses · 2020Article
- Cell Fusion: Merging Membranes and Making Muscle.Trends in cell biology · 2019Review
- Rotavirus Species B Encodes a Functional Fusion-Associated Small Transmembrane Protein.Journal of virology · 2019Article
- Cell-cell fusion induced by reovirus FAST proteins enhances replication and pathogenicity of non-enveloped dsRNA viruses.PLoS pathogens · 2019Article
- Reovirus FAST Protein Enhances Vesicular Stomatitis Virus Oncolytic Virotherapy in Primary and Metastatic Tumor Models.Molecular therapy oncolytics · 2017Article
- Reovirus FAST Proteins Drive Pore Formation and Syncytiogenesis Using a Novel Helix-Loop-Helix Fusion-Inducing Lipid Packing Sensor.PLoS pathogens · 2015Article
- Bacterial-mediated knockdown of tumor resistance to an oncolytic virus enhances therapy.Molecular therapy : the journal of the American Society of Gene Therapy · 2014Article
- Efficient reovirus- and measles virus-mediated pore expansion during syncytium formation is dependent on annexin A1 and intracellular calcium.Journal of virology · 2014Article
- Reovirus-associated meningoencephalomyelitis in baboons.Veterinary pathology · 2014Article
- Golgi complex-plasma membrane trafficking directed by an autonomous, tribasic Golgi export signal.Molecular biology of the cell · 2014Article
- A compact, multifunctional fusion module directs cholesterol-dependent homomultimerization and syncytiogenic efficiency of reovirus p10 FAST proteins.PLoS pathogens · 2014Article
- Trimeric transmembrane domain interactions in paramyxovirus fusion proteins: roles in protein folding, stability, and function.The Journal of biological chemistry · 2013Article
- Cell-cell membrane fusion induced by p15 fusion-associated small transmembrane (FAST) protein requires a novel fusion peptide motif containing a myristoylated polyproline type II helix.The Journal of biological chemistry · 2012Article
- Discovery of an orthoreovirus in the aborted fetus of a Steller sea lion (Eumetopias jubatus).The Journal of general virology · 2011Article
- Helix-destabilizing, beta-branched, and polar residues in the baboon reovirus p15 transmembrane domain influence the modularity of FAST proteins.Journal of virology · 2011Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The FAST proteins are a unique family of virus-encoded cell-cell membrane fusion proteins. In the absence of a cleavable N-terminal signal peptide, a single-pass transmembrane domain (TMD) functions as a reverse signal-anchor to direct the FAST proteins into the plasma membrane in an N(exo)/C(cyt) topology. There is little information available on the role of the FAST protein TMD in the cell-cell membrane fusion reaction. We show that in the absence of conservation in the length or primary amino acid sequence, the p14 TMD can be functionally exchanged with the TMDs of the p10 and p15 FAST proteins. This is not the case for chimeric p14 proteins containing the TMDs of two different enveloped viral fusion proteins or a cellular membrane protein; such chimeric proteins were defective for both pore formation and syncytiogenesis. TMD structural features that are conserved within members of the FAST protein family presumably play direct roles in the fusion reaction. Molecular modeling suggests that the funnel-shaped architecture of the FAST protein TMDs may represent such a conserved structural and functional motif. Interestingly, although heterologous TMDs exert diverse influences on the trafficking of the p14 FAST protein, these TMDs are capable of functioning as reverse signal-anchor sequences to direct p14 into lipid rafts in the correct membrane topology. The FAST protein TMDs are therefore not primary determinants of type III protein topology, but they do play a direct, sequence-independent role in the membrane fusion reaction.
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