Role of actin-binding protein in insertion of adhesion receptors into the membrane.
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, functional GP Ib-IX was inserted into the membrane. GP Ib-IX lacking the domain that interacts with ABP also showed increased membrane insertion in 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, expression of ABP also increased endogenous beta1 integrin in the membrane. 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 increased 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 actin filaments or direct interaction with receptors.
Meyer
S C
SC
Joseph J. Jacobs Center for Thrombosis and Vascular Biology, Cleveland Clinic Foundation, Cleveland, Ohio 44195, USA.
Sanan
D A
DA
Fox
J E
JE
D002462:Cell Membrane / Q000502:physiology*; D005434:Flow Cytometry; D005786:Gene Expression Regulation; D017261:Glycosylphosphatidylinositols / Q000502:physiology*; D006801:Humans; D019012:Integrin beta1 / Q000378:metabolism; D008840:Microfilament Proteins / Q000502:physiology*; D008858:Microscopy, Phase-Contrast; D014162:Transfection; D014407:Tumor Cells, Cultured
D017261:Glycosylphosphatidylinositols; D019012:Integrin beta1; D008840:Microfilament Proteins