Fluorescence-imaged micropipette aspiration was used to map redistribu
tion of the proteins and lipids in highly extended human red blood cel
l membranes. Whereas the fluid bilayer distributed uniformly (+/-10 pe
rcent), the underlying, solidlike cytoskeleton of spectrin, actin, and
protein 4.1 exhibited a steep gradient in density along the aspirated
projection, which was reversible on release from deformation. Quantit
ation of the cytoskeletal protein density gradients showed that skelet
al elasticity is well represented by a grafted polymer network with a
ratio of surface dilation modulus to shear modulus of approximately 2:
1. Fractionally mobile integral proteins, such as band 3, and highly m
obile receptors, such as CD59 as well as glycophorin C in protein 4.1-
deficient cells, appeared to be squeezed out of areas dense in the und
erlying network and enriched in areas of network dilation. This comple
mentary segregation demonstrates patterning of cell surface components
by cytoskeletal dilation.