Protein kinase C and the cytoskeleton.

The protein kinase C family of serine-threonine kinases are important signal transducers participating in many different agonist-induced signalling cascades. PKC is activated by increases in diacylglycerol produced in response to agonist-induced hydrolysis of inositol phospholipids. PKC is thought to reside in the cytosol in an inactive conformation and translocate to the plasma membrane upon cell activation where it modifies various cellular functions through phosphorylation of target substrates. Increasing evidence has illustrated that this family of enzymes is capable of translocating to other subcellular sites than the plasma membrane. A key to understanding the functions of the members of this family is identifying their physiological substrates and their relationship with those target substrates. The idea that PKC may be an important regulator of cytoskeletal function has been suggested by numerous studies. Activation of PKC in a variety of different cell types leads to changes in the cell cytoskeleton including lymphocyte surface receptor capping, smooth muscle contraction and actin rearrangement in T cells and neutrophils. Given the ubiquitous expression of PKC and the diversity of cytoskeletons in different cell types it is not surprising that PKC has been shown to be associated with and/or phosphorylate a wide range of cytoskeletal components. This review examines the interaction of PKC with the cytoskeleton and discusses some of the cytoskeletal functions ascribed to PKC to date.