H2N2V1, Ncbi, Merge, bibRecord, 000909

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

Identifieur interne : 000909 ( Ncbi/Merge ); précédent : 000908; suivant : 000910

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

Auteurs : Manasa V. Gudheti [États-Unis] ; Nikki M. Curthoys ; Travis J. Gould ; Dahan Kim ; Mudalige S. Gunewardene ; Kristin A. Gabor ; Julie A. Gosse ; Carol H. Kim ; Joshua Zimmerberg ; Samuel T. Hess

Source :

Biophysical journal [ 1542-0086 ] ; 2013.

RBID : pubmed:23708358

Descripteurs français

English descriptors

KwdEn :
- Actin Cytoskeleton (metabolism), Actin Depolymerizing Factors (metabolism), Actins (metabolism), Animals, Cell Membrane (metabolism), Cell Membrane (ultrastructure), Hemagglutinin Glycoproteins, Influenza Virus (chemistry), Hemagglutinin Glycoproteins, Influenza Virus (metabolism), Hemagglutinin Glycoproteins, Influenza Virus (ultrastructure), Influenza A Virus, H2N2 Subtype (chemistry), Influenza A Virus, H2N2 Subtype (metabolism), Mice, NIH 3T3 Cells, Protein Multimerization.
MESH :
- chemical , chemistry : Hemagglutinin Glycoproteins, Influenza Virus.
- chemical , metabolism : Actin Depolymerizing Factors, Actins, Hemagglutinin Glycoproteins, Influenza Virus.
- chemistry : Influenza A Virus, H2N2 Subtype.
- metabolism : Actin Cytoskeleton, Cell Membrane, Influenza A Virus, H2N2 Subtype.
- ultrastructure : Cell Membrane, Hemagglutinin Glycoproteins, Influenza Virus.
- Animals, Mice, NIH 3T3 Cells, Protein Multimerization.

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.

DOI: 10.1016/j.bpj.2013.03.054
PubMed: 23708358

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Links to Exploration step

pubmed:23708358

Le document en format XML

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<term>Influenza A Virus, H2N2 Subtype (metabolism)</term>
<term>Mice</term>
<term>NIH 3T3 Cells</term>
<term>Protein Multimerization</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Actines (métabolisme)</term>
<term>Animaux</term>
<term>Cellules NIH 3T3</term>
<term>Cytosquelette d'actine (métabolisme)</term>
<term>Facteurs de dépolymérisation de l'actine (métabolisme)</term>
<term>Glycoprotéine hémagglutinine du virus influenza ()</term>
<term>Glycoprotéine hémagglutinine du virus influenza (métabolisme)</term>
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<term>Membrane cellulaire (ultrastructure)</term>
<term>Multimérisation de protéines</term>
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<term>Sous-type H2N2 du virus de la grippe A ()</term>
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<front><div type="abstract" xml:lang="en">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.</div>
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<Abstract><AbstractText>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.</AbstractText>
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Actin mediates the nanoscale membrane organization of the clustered membrane protein influenza hemagglutinin.

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

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