Keratin 5 to withstand mechanical, and non-mechanical, stresses. K5/K14 keratin pairs are able to undergo extensive bundling due to the non-helical tail of K15 acting as a weak cross-linker at the intermediate filament surface. This bundling increases the elasticity, and therefore the mechanical resilience, of the intermediate filaments. K5/K14 intermediate filaments are anchored to the desmosomes of basal cells via desmoplakin and plakophilin-1, connecting the cells to their neighbours. At the hemidesmosome, plectin and BPAG1 associate with transmembrane proteins α6β4 integrin, a type of cell adhesion molecule, and BP180/collagen XVII, linking K5/K14 filaments in the basal cells to the basal lamina. Epidermolysis
Myosin cells, the long coiled-coil tails of the individual myosin molecules join together, forming the thick filaments of the sarcomere. The force-producing head domains stick out from the side of the thick filament, ready to walk along the adjacent actin-based thin filaments in response to the proper chemical signals. Myosin III is a poorly understood member of the myosin family. It has been studied "in vivo" in the eyes of "Drosophila", where it is thought to play a role in phototransduction. A human homologue gene for myosin III, MYO3A, has been uncovered through the Human Genome Project and is expressed in