In biology, a protein filament is a long chain of protein monomers, such as those found in hair, muscle, or in flagella. Protein filaments form together to make the cytoskeleton of the cell. They are often bundled together to provide support, strength, and rigidity to the cell. When the filaments are packed up together, they are able to form three different cellular parts. The three major classes of protein filaments that make up the cytoskeleton include: actin filaments, microtubules and intermediate filaments.
Cellular types
Microfilaments
Compared to the other parts of the cytoskeletons, the microfilaments contain the thinnest filaments, with a diameter of approximately 7 nm. Microfilaments are part of the cytoskeleton that are composed of protein called actin. Two strands of actin intertwined together form a filamentous structure allowing for the movement of motor proteins. Microfilaments can either occur in the monomeric G-actin or filamentous F-actin. Microfilaments are important when it comes to the overall organization of the plasma membrane. Actin filaments are considered to be both helical and flexible. They are composed of several actin monomers chained together which add to their flexibility. They are found in several places in the body including the microvilli, contractile rings, stress fibers, cellular cortex, etc. In a contractile ring, actin have the ability to help with cellular division while in the cellular cortex they can help with the structural integrity of the cell.
Microfilament Polymerization Microfilament polymerization is divided into three steps. The nucleation step is the first step, and it is the rate limiting and slowest step of the process. Elongation is the next step in this process, and it is the rapid addition of actin monomers at both the plus and minus end of the microfilament. The final step is the steady state. At this state the addition of monomers will equal the subtraction of monomers causing the microfilament to no longer grow. This is known as the critical concentration of actin. There are several toxins that have been known to limit the polymerization of actin. Cytochalasin is a toxin that will bind to the actin polymer, so it can no longer bind to the incoming actin monomers. Actin originally attached in the polymer is still leaving the microfilament causing depolymerization. Phalloidin is a toxin that will bind to actin locking the filament in place. Monomers are neither adding or leaving this polymer which causes the stabilization of the molecule. Latrunculin is similar to cytochalasin, but it is a toxin which will bind to the actin monomers preventing it from adding onto the actin polymer. This will cause the depolymerization of the actin polymer in the cell.
Actin Based Motor Protein- Myosin
There are several different proteins that interact with actin in the body. However, one of the most famous types of motor proteins is myosin. Myosin will bind to these actins causing the movement of actin. This movement of myosin along the microfilament can cause muscle contraction, membrane association, endocytosis, and organelle transport. The actin microfilament is composed of three bands and one disk. The A band is the part of the actin that will bind to the myosin during muscle contraction. The I band is the part of the actin that is not bound to the myosin, but it will still move during muscle contraction. The H zone is the space in between two adjacent actin that will shrink when the muscle begins to contract. The Z disk is the part of the microfilament that characterizes the overall end of each side of the sarcomere, a structural unit of a myofibril.
Proteins Limiting Microfilaments These microfilaments have the potential to be limited by several factors or proteins. Tropomodulin is a protein that will cap the ends of the actin filaments causing the overall stability of the structure. Nebulin is another protein that can bind to the sides of the actin preventing the attachment of myosin to them. This causes stabilization of the actin limiting muscle contraction. Titin is another protein, but it binds to the myosin rather than the actin microfilament. Titin will help stabilize the contraction and myosin-actin structure.
Microtubules
Microtubules are the largest type of filament, with a diameter of 25 nm wide, in the cytoskeleton. A single microtubule consists of 13 linear microfilaments. Unlike microfilaments, microtubules are composed of a protein called tubulin. The tubulin consists of dimers, named either "αβ-tubulin" or "tubulin dimers", which polymerize to form the microtubules. These microtubules are structurally quantified into three main groups: singlets, doublets, and triplets. Singlets are microtubule structures that are known to be found in the cytoplasm. Doublets are structures found in the cilia and flagella. Triplets are found in the basal bodies and centrioles. There are two main populations of these microtubules. There are unstable short-lived microtubules that will assemble and disassemble rapidly. The other population are stable long-lived microtubules. These microtubules will remain polymerized for longer periods of time and can be found in flagella, red blood cells, and nerve cells. Microtubules have the ability to play a significant role in the organization of organelles and vesicles, beating of cilia and flagella, nerve and red blood cell structure, and alignment/ separation of chromosomes during mitosis and meiosis.
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