Abstract
Several cell membrane proteins bind to cortical F-actin and are driven by actomyosin flows to form transient nanoclusters and functional mesoscale assemblies. Examples include integrins, E-cadherins, T-cell receptors, Ras proteins, glycoproteins such as CD44 etc. Faced with such membrane protein diversity—their mode of interaction with cortical actin, actin-binding affinity, and relative cell surface expression—it is pertinent to ask how local control of cluster composition might be achieved. Using an in-vitro reconstitution of a thin, dynamic actomyosin layer on a planar lipid membrane and a theory based on active clustering induced by cortical flows, we show that the interplay between actomyosin remodelling and differential actin-binding affinity can lead to specific molecular patterning. This provides an attractive mechanism for the local control of plasma membrane composition.
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