The DOI matches its Crossref record; 81 of the 82 references it cites were found in a registry or an index.
Actin Mediates the Nanoscale Membrane Organization of the Clustered Membrane Protein Influenza Hemagglutinin
Open accessAbstract
The influenza viral membrane protein hemagglutinin (HA) is required at high concentrations on virion and host-cell membranes for infectivity. Because the role of actin in membrane organization is not completely understood, we quantified the relationship between HA and host-cell actin at the nanoscale. Results obtained using superresolution fluorescence photoactivation localization microscopy (FPALM) in nonpolarized cells show that HA clusters colocalize with actin-rich membrane regions (ARMRs). Individual molecular trajectories in live cells indicate restricted HA mobility in ARMRs, and actin disruption caused specific changes to HA clustering. Surprisingly, the actin-binding protein cofilin was excluded from some regions within several hundred nanometers of HA clusters, suggesting that HA clusters or adjacent proteins within the same clusters influence local actin structure. Thus, with the use of imaging, we demonstrate a dynamic relationship between glycoprotein membrane organization and the actin cytoskeleton at the nanoscale.
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“Lastly, the actin cytoskeleton is known to mediate receptor positioning (Gudheti et al., 2013) and its depolymerization was shown to reduce glutamate receptor accumulations in spines (Allison et al., 2000).”
From Barriers in the brain: resolving dendritic spine morphology and compartmentalization (2014) · cites this paper as Gudheti et al., 2013
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Cites
Cellular Motility Driven by Assembly and Disassembly of Actin Filaments
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Ultra-High Resolution Imaging by Fluorescence Photoactivation Localization Microscopy
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Self-citationRegulation of actin dynamics through phosphorylation of cofilin by LIM-kinase
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Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization
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A Role for Lipid Shells in Targeting Proteins to Caveolae, Rafts, and Other Lipid Domains
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Lipid rafts: at a crossroad between cell biology and physics
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Proteins of the ADF/Cofilin Family: Essential Regulators of Actin Dynamics
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The Application of Computers to Taxonomy
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Metadata
- Authors
- Gudheti, M. V., Curthoys, N. M., Gould, T. J., Kim, D., Gunewardene, M. S., Gabor, K. A., Gosse, J. A., Kim, C. H., Zimmerberg, J., & Hess, S. T.
- Affiliations
- University of Maine (US)
- National Institutes of Health (US)
- Corresponding author
- Hess, Samuel T.
- Venue
- Biophysical Journal
- Publisher
- Elsevier BV
- Published
- 2013-05
- Volume
- 104
- Issue
- 10
- Pages
- 2182-2192
- ISSN
- 0006-3495 (ISSN-L)
- PMC
- PMC3660645
- OpenAlex
- W1985357723
- Cited by
- 106
- References
- 82
- Citations by year
- 2026: 5 · 2025: 4 · 2024: 5 · 2023: 7 · 2022: 8 · 2021: 10 · 2020: 5 · 2019: 3 · 2018: 3 · 2017: 10 · 2016: 11 · 2015: 10 · 2014: 18 · 2013: 7
- FWCI
- 11.19
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biophysical Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM087308, R15GM094713, P20GM103534)
- National Institute of Allergy and Infectious Diseases (K25AI065459, K25-AI65459)
- Topics
- Health Sciences › Medicine › Epidemiology › Influenza Virus Research Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Keywords
- influenza hemagglutinin, actin, protein clustering, membrane organization, cofilin, actin cytoskeleton, viral membrane proteins, host cell membrane
- MeSH terms
- Actins, Animals, Cell Membrane, Actin Cytoskeleton, Hemagglutinin Glycoproteins, Influenza Virus, NIH 3T3 Cells, Actin Depolymerizing Factors, Mice, Influenza A Virus, H2N2 Subtype, Protein Multimerization
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