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Actin restricts FcepsilonRI diffusion and facilitates antigen-induced receptor immobilization.

Abstract：

:The actin cytoskeleton has been implicated in restricting diffusion of plasma membrane components. Here, simultaneous observations of quantum dot-labelled FcepsilonRI 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 FcepsilonRI often maintain extended close proximity without detectable correlated motion, suggesting that they are co-confined within membrane domains. FcepsilonRI 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.

journal_name

Nat Cell Biol

journal_title

Nature cell biology

authors

Andrews NL,Lidke KA,Pfeiffer JR,Burns AR,Wilson BS,Oliver JM,Lidke DS

doi

10.1038/ncb1755

subject

Has Abstract

pub_date

2008-08-01 00:00:00

pages

955-63

issue

8

eissn

1465-7392

issn

1476-4679

pii

ncb1755

journal_volume

10

pub_type

杂志文章

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