Contractile Proteins: Actin, Myosin
Start with the big picture
Actin monomers (G-actin) assemble into polar F-actin filaments that form the backbone of the thin filament. In striated muscle, tropomyosin and troponin regulate access to myosin-binding sites in response to calcium. Myosin II forms thick filaments; its heads bind actin and hydrolyze ATP. In the cross-bridge cycle, ATP binding detaches myosin, ATP hydrolysis cocks the head, and subsequent phosphate and ADP release lead to strong binding and the power stroke. ATP availability is therefore central to cycling, while smooth muscle can regulate myosin through light-chain phosphorylation rather than troponin. The lesson also considers myosin isoforms and examples of agents that affect actin or myosin function.
What you'll learn
- Describe G-actin polymerization and the polarity of F-actin.
- Explain how actin filaments are organized and regulated in striated muscle.
- Identify the major structural features of myosin II and thick filaments.
- Outline the cross-bridge cycle and relate ATP binding to myosin–actin interactions.
- Distinguish smooth muscle light-chain regulation from troponin-based regulation.
Continue your study
Work through the complete notes and reinforce the topic with the study tools available in the full lesson.