Cited by 106Influenza Virus Research StudiesCellular transport and secretionCellular Mechanics and Interactions

Actin mediates the nanoscale membrane organization of the clustered membrane protein influenza hemagglutinin

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Gudheti, Manasa V., Curthoys, Nikki M., Gould, Travis J., Kim, Dahan, Gunewardene, Mudalige S., Gabor, Kristin A., Gosse, Julie A., Kim, Carol H. +2 more·2013·Biophysical Journal

Abstract

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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Crossref · 10.1016/j.bpj.2013.03.054

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  • The actin cytoskeleton mediates receptor positioning and its depolymerization reduces glutamate receptor accumulations in spines.

    “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

    The Introduction and the section on HA clusters show that actin affects the distribution and clustering of the membrane protein influenza hemagglutinin (HA). This supports the general idea of actin-mediated membrane-protein positioning, but the paper’s own findings concern HA, not receptor positioning specifically. The separate claim about glutamate receptors is attributed to Allison et al. (2000), not to this source. (LLM, conf=0.82)

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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)
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
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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