Myosin binding protein-C (MyBP-C) is an enigmatic protein of muscle sarcomeres that plays both structural and regulatory roles that are critical to muscle function. MyBP-C was first identified through its tight association with myosin, the force generator of muscle contraction, but it was soon recognized that MyBP-C also binds to actin on thin filaments. MyBP-C interactions with both filament systems are now known to affect contraction and relaxation through multiple complex pathways. For instance, MyBP-C inhibits thick filaments by stabilizing a slowly cycling, quiescent state of myosin (the myosin super-relaxed state, SRX). However, MyBP-C exerts opposite effects, prolonging thin filament activation and delaying relaxation, by binding to the thin filament and shifting tropomyosin to its open position. Furthermore, by simultaneously binding to both thick and thin filaments that move relative to one another, MyBP-C may act as a drag force that slows shortening velocity while also being perfectly positioned to act as mechano-sensor that efficiently relays information from one filament system to another. Here we will present structural and functional data in an integrative model describing how MyBP-C may dynamically alternate between its binding partners in a way that accounts for the ability of MyBP-C to seemingly be everything, everywhere, all at once. This work was supported by R01 HL080367 and HL140925.