Recent studies have suggested that integrin (CR3) participates in the signal transduction pathways of certain GPI-anchored phagocytic receptors including $Fc{gamma}RIIIB$. One consequence of this functional linkage is an inducible association between CR3 and cortical microfilaments that is triggered by $Fc{gamma}RIIIB$ binding to immobilized immune complexes (IC). That this signaling event requires the co-expression of $Fc{gamma}RIIIB$ with CR3 was documented by the use of NIH 3T3 transfectants expressing both CR3 and $Fc{gamma}RIIIB$ (clone 3-23), CR3 alone (clone 3-19), and $Fc{gamma}RIIIB$ alone (clone 3-15). Pretreatment of 3-23 cells with protein kinase inhibitors such as staurosporine and methyl 2,5-dihydroxycinnamate (MDHC) blocked IC-stimulated CR3 microfilament proximity without affecting the extent to which $Fc{gamma}RIIIB$ constrains the lateral membrane mobility of a subset of CR3 on the cell surface (as measured in fluorescence recovery after photobleaching experiments). These data support that CR3 and $Fc{gamma}RIIIB$ molecules are physically and functionally associated and that ligation of FcgRIIIB triggers CR3-dependent signal transduction.