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Troponin T (blue) anchors the complex on tropomyosin. Troponin is found in both skeletal muscle and cardiac muscle, but the specific versions of troponin differ between types of muscle. The main difference is that the TnC subunit of troponin in skeletal muscle has four calcium ion-binding sites, whereas in cardiac muscle there are only three.
Troponin C is a protein which is part of the troponin complex. It contains four calcium-binding EF hands , although different isoforms may have fewer than four functional calcium-binding subdomains. It is a component of thin filaments , along with actin and tropomyosin .
Troponin C, also known as TN-C or TnC, is a protein that resides in the troponin complex on actin thin filaments of striated muscle (cardiac, fast-twitch skeletal, or slow-twitch skeletal) and is responsible for binding calcium to activate muscle contraction.
Troponin (Tn), is a key protein complex in the regulation of striated muscle contraction, composed of three subunits. The TnI subunit inhibits actomyosin ATPase , the TnT subunit binds tropomyosin and TnC, while the TnC subunit binds calcium and overcomes the inhibitory action of the troponin complex on actin thin filaments .
The calcium binds to the calcium release channels (RYRs) in the SR, opening them; this phenomenon is called "calcium-induced calcium release", or CICR. However the RYRs are opened, either through mechanical-gating or CICR, Ca 2+ is released from the SR and is able to bind to troponin C on the actin filaments.
Caldesmon binds to actin, tropomyosin, calmodulin, and myosin, of which its interactions with actin are most important. The binding of caldesmon is strongly influenced by tropomyosin. Caldesmon is an inhibitor of actinomyosin ATPase and motility, and both actin binding and caldesmon inhibition are greatly enhanced in the presence of tropomyosin.
This gene encodes an intracellular calcium-binding protein belonging to the troponin C superfamily. Members of this protein family have six EF-hand domains which bind calcium. This protein plays a role in diverse cellular functions, including message targeting and intracellular calcium buffering. [6]
Calcium-binding proteins can be either intracellular and extracellular. Those that are intracellular can contain or lack a structural EF-hand domain. Extracellular calcium-binding proteins are classified into six groups. [2] Since Ca (2+) is an important second messenger, it can act as an activator or inhibitor in gene transcription.