Journal
NATURE CELL BIOLOGY
Volume 10, Issue 8, Pages 955-963Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncb1755
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Funding
- NCI NIH HHS [P30 CA118100] Funding Source: Medline
- NCRR NIH HHS [S10 RR022493, S10 RR19287, S10 RR15734, S10 RR14668, S10 RR019287, P20 RR11830, S10 RR16918, RR022493] Funding Source: Medline
- NIAID NIH HHS [R01 AO051575, R01 AI051575] Funding Source: Medline
- NIGMS NIH HHS [P20 GM067597, R01 GM049814-07, R01 GM49814, P20 GM067594, R01 GM049814, P20 GM067594-01, P20 GM 67594] Funding Source: Medline
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The actin cytoskeleton has been implicated in restricting diffusion of plasma membrane components. Here, simultaneous observations of quantum dot-labelled Fc epsilon RI motion and GFP-tagged actin dynamics provide direct evidence that actin filament bundles define micron-sized domains that confine mobile receptors. Dynamic reorganization of actin structures occurs over seconds, making the location and dimensions of actin-defined domains time-dependent. Multiple Fc epsilon RI often maintain extended close proximity without detectable correlated motion, suggesting that they are co-confined within membrane domains. Fc epsilon RI signalling is activated by crosslinking with multivalent antigen. We show that receptors become immobilized within seconds of crosslinking. Disruption of the actin cytoskeleton results in delayed immobilization kinetics and increased diffusion of crosslinked clusters. These results implicate actin in membrane partitioning that not only restricts diffusion of membrane proteins, but also dynamically influences their long-range mobility, sequestration and response to ligand binding.
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