The barbed ends of actin filaments in striated muscle are moored inside the Z-disc and capped by CapZ this protein blocks actin polymerization and depolymerization in vitro. The mature lengths from the thin filaments are most likely per the enormous “molecular ruler” unesbulin, which spans the size of the skinny filament. Here, we are convinced that CapZ particularly interacts using the C terminus of nebulin (modules 160-164) in blot overlay, solid-phase binding, tryptophan fluorescence, and SPOTs membrane assays. Binding of nebulin modules 160-164 to CapZ has no effect on ale CapZ to cap actin filaments in vitro, in line with our observation that neither of these two C-terminal actin binding parts of CapZ is essential because of its interaction with nebulin. Knockdown of nebulin in chick skeletal myotubes using small interfering RNA produces a decrease in put together CapZ, and, strikingly, a loss of revenue from the uniform alignment from the barbed ends from the actin filaments. These data claim that nebulin restricts the positioning of thin filament barbed ends towards the Z-disc using a direct interaction with CapZ. We advise a singular molecular type of Z-disc architecture by which nebulin interacts with CapZ from the thin filament of the adjacent sarcomere, thus supplying a structural outcomes of sarcomeres.