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One of the most apparent differences between normal cells and their malignantly transformed counterparts and between immature and fully differentiated cells is the shape of the cells (1). Cell morphology is controlled largely by the structure of the cytoskeleton, a system of three distinct types of filamentous polymers that assemble into networks and bundles of various kinds to link the cell interior physically with the plasma membrane and endow the cell with viscoelastic properties. The transformation of cytoplasm from a liquid to a solid was observed by early microscopists to be tightly associated with the cells' ability to move, and this sol-to-gel transition is now known to be caused by changes in the state of polymerization and organization of the protein actin, one of the three types of filaments comprising the cytoskeleton (2). When something goes wrong in the complex system of control proteins and messengers that signals for changes in the actin system, as can happen with genetic mutations or by the insertion of viral genes coding for maliciously altered control proteins, cells may migrate and divide inappropriately, because the signals for division or motility cannot be stopped. One such control factor is the protooncogene protein Abl. In addition to its implication in human leukemias, the tyrosine kinase Abl also is an important regulator of the actin system involved in neuronal cell function and early neuronal development (3, 4). Abl is part of the signaling pathways that control the actin cytoskeleton and associates with large actin-containing cellular structures, because it has two actin binding sites at its C-terminal domain (6). Abl's ability to control cell function requires its actin binding function, presumably because such targeting to the cytoskeleton directs its kinase activity to appropriate targets (6). Most cells, including neurons, also express other proteins similar to Abl …

Creating a niche in the cytoskeleton: Actin reorganization by a protein kinase