Sc. Meyer et al., ROLE OF ACTIN-BINDING PROTEIN IN INSERTION OF ADHESION RECEPTORS INTOTHE MEMBRANE, The Journal of biological chemistry, 273(5), 1998, pp. 3013-3020
The goal of this study was to determine whether actin-binding protein
(ABP) regulates membrane composition, ABP-deficient and ABP-containing
cells were transfected with the cDNAs coding for glycoprotein (GP) Ib
-IX, a platelet receptor that interacts with ABP, Most of the GP Ib-IX
remained inside the ABP-deficient cells, When ABP was present, functi
onal GP Ib-IX was inserted into the membrane, GP Ib-IX lacking the dom
ain that interacts with ABP also showed increased membrane insertion i
n ABP-expressing cells. Furthermore, a fragment of ABP that lacks the
dimerization and GP Ib-IX-binding sites restored the spreading of the
cells and increased the amount of GP Ib-IX in the membrane, Finally, e
xpression of ABP also increased endogenous beta(1) integrin in the mem
brane, These results indicate that 1) ABP maintains the properties of
the cell such that adhesion receptors can be efficiently expressed in
the membrane; 2) increased receptor expression is accompanied by incre
ased ability of the cell to spread; and 3) ABP exerts its effect by a
mechanism that does not appear to involve direct cross-linking of acti
n filaments or direct interaction with receptors.