The cytoskeleton is the internal structure of the cell that makes diverse cellular functions possible. These structures are extremely dynamic, undergoing continual remodelling within the cytoplasm and requiring continual change in the protein-protein interactions as part of their function. It is therefore not surprising that cytoskeletal proteins require the attention of protein chaperones at all stages of their life. Initially, chaperonins ensure the nascent chains of actin and tubulin fold correctly as they emerge from the ribosome and in this review, the role of the small heat shock proteins (sHSPs) in further cytoskeletal function will be discussed. Chaperones are most certainly important components in the birth and life of the cytoskeleton. This review will discuss the importance of protein chaperones, and specifically sHSPs, to the maintenance and control of the cytoskeleton. A key viewpoint within the article is the consideration of the cytoskeleton as a whole, removing the convenient, but artificial, boundaries of actin, tubulin and intermediate filaments to discuss sHSP function. Importantly, viewing chaperones and the cytoskeleton as a functional unit suggests exciting new possibilities that should cause us to rethink the commonly perceived role of chaperones as just" quality control" proteins. At the very least sHSPs improve the efficiency of cytoskeletal function and prevent potentially damaging liaisons, but there is greater potential in sHSP-cytoskeleton complex. This review will discuss what is currently known about the interaction of sHSPs with the cytoskeleton and will end with some ideas to inspire future research based on this emerging holistic view of the cell!