The B cell antigen receptor (BCR) plays two central roles in B cell activation: to internalize antigens for processing and presentation, and to initiate signal transduction cascades that both promote B cells to enter the cell cycle and facilitate antigen processing by accelerating antigen transport. An early event in B cell activation is the association of BCR with the actin cytoskeleton, and an increase in cellular F‐actin. Current evidence indicates that the organization of actin filaments changes in response to BCR‐signaling, making actin filaments good candidates for regulation of BCR‐antigen targeting. Here, we have analyzed the role of actin filaments in BCR‐mediated antigen transport, using actin filament‐disrupting reagents, cytochalasin D and latrunculin B, and an actin filament‐stabilizing reagent, jasplakinolide. Perturbing actin filaments, either by disrupting or stabilizing them, blocked the movement of BCR from the plasma membrane to late endosomes/lysosomes. Cytochalasin D‐treatment dramatically reduced the rate of internalization of BCR, and blocked the movement of the BCR from early endosomes to late endosomes/lysosomes, without affecting BCR‐signaling. Thus, BCR‐trafficking requires functional actin filaments for both internalization and movement to late endosomes/lysosomes, defining critical control points in BCR‐antigen targeting.