Name: how actomyosin bundles shape cell movement
Uploaded: 2023-04-30T09:32:08.000Z
Duration: 1 min 10 s
Channel: JoVE

In non-muscle cells, F-actin and myosin-II form small contractile bundles that are smaller and less organized than muscle fibers.
In epithelial cells, these contractile bundles arrange parallel to the cell membrane as adherence or circumferential belts, connecting adjacent adherens junctions.
Adherence belts help maintain the stability and structural integrity of epithelial cells.
In macrophages,&#160; F-actin and myosin arrange into compact bundles called stress fibers. During phagocytosis, the stress bundles rearrange to engulf and internalize foreign particles and pathogens.
Stress fibers also bind with integrins, which are connected to the extracellular matrix, helping the cells attach to surrounding surfaces.
In dividing cells, septin rings recruit actin and myosin, forming a temporary structure called a contractile ring that helps in cytokinesis.
The ring-like structure forms in the middle of the cell dividing the cytoplasm to form two daughter cells.

the role of actin and myosin in non-muscle cells

The Role of Actin and Myosin in Non-muscle Cells

Actin and myosin or actomyosin filaments also play a significant role in cells other than those involved in muscle contraction (which occurs within the sarcomere of muscle cells). The mechanism of non-muscle cell contractile bundles was first observed in Dictyostelium and Acanthamoeba. In non-muscle cells, two bundles are commonly found: stress fibers and actomyosin adherence belts. These contractile bundles are smaller and less organized than the ones found in muscle cells. They&#160; are held together by accessory proteins such as&#160; fascin, filamin, and fimbrin depending on where they are located. The formation and contractile ability of these actomyosin bundles are regulated by phosphorylation.
In non-muscle cells,&#160; actin and non-muscle myosin II (NMM) filaments combine to form stress fibers. There are about 15 to 20 myosin filaments in each bundle. The mechanism of action of these actinomyosin contractile bundles is similar to those in muscle fibers, where&#160; ATP hydrolysis by the myosin globular head drives the actin contraction. The stress fibers, along with the focal adhesions present at the cell edges, regulate the mechanosensitive machinery in the cells. These bundles are also responsible for regulating cell morphogenesis. In cells, these stress fibers are found near the cell edges, where they help the cell anchor on the substratum.
In epithelial cells, the actomyosin bundles are attached to the adhesion junctions as circumferential or adherence belts close to the plasma membrane. These belts regulate the apical constriction of polarized&#160; epithelial cells. In dividing cells, these actomyosin bundles are recruited by the septin ring at the cell cleavage furrow to form the contractile ring, which is a major step in&#160; cytokinesis.

Actin and myosin or actomyosin filaments also play a significant role in cells other than those involved in muscle contraction (which occurs within the ...

the-role-of-actin-and-myosin-in-non-muscle-cells

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JoVE Core

Cell Biology

Unit 1

The Cytoskeleton I: Actin and Microfilaments

the-cytoskeleton-i-actin-and-microfilaments

KEY TERMS AND CONCEPTS

how actomyosin bundles shape cell movement

Actin and myosin form contractile bundles in non-muscle cells. These actomyosin structures help cells change shape, attach to surfaces, and divide. They were first observed in Dictyostelium and Acanthamoeba.

Two common bundles are stress fibers and actomyosin adherence belts. These bundles are smaller and less organized than the ones found in muscle cells. Accessory proteins such as fascin, filamin, and fimbrin help hold them together, depending on where they are in the cell.

Their formation and ability to contract are regulated by phosphorylation, which is the addition of a phosphate group to a molecule. In stress fibers, actin combines with non-muscle myosin II, or NMM, to build bundles with about 15 to 20 myosin filaments each. The myosin globular head uses ATP hydrolysis to drive contraction, much like in muscle fibers.

Stress fibers sit near the cell edges, where they connect with focal adhesions and help the cell anchor to the substratum. They also support the mechanosensitive machinery in cells and help regulate cell morphogenesis, which is the way a cell takes shape. In epithelial cells, actomyosin bundles form circumferential adherence belts near the plasma membrane and at adhesion junctions.

These belts help control apical constriction in polarized epithelial cells. In dividing cells, actomyosin bundles are recruited by the septin ring at the cleavage furrow to form the contractile ring. This ring is an important step in cytokinesis, when one cell splits into two.

How Actomyosin Bundles Shape Cell Movement

how-actomyosin-bundles-shape-cell-movement

introduction to the cytoskeleton

Cytoskeleton Structure and Cell Movement

The cytoskeleton is a network of protein filaments inside the cell. It gives cells shape, helps organize cell contents, and supports movement. Although the name suggests a fixed skeleton, it is a dynamic structure that can change quickly in response to signals or forces. Three main filament types make up the cytoskeleton: microfilaments, microtubules, and intermediate filaments. Each one has different assembly and disassembly behavior, mechanical strength, polarity, and associated motor...

adaptability of cytoskeletal filaments

Cytoskeletal Filaments in Cell Movement

Cytoskeletal filaments help cells change shape, divide, and move. Their flexibility lets them stay stable for hours during interphase or reorganize quickly during cell division. Strong regulation controls how these filaments assemble, fall apart, and form networks. Microfilaments and microtubules are dynamic, while intermediate filaments are considered more static. Microfilaments are spread throughout the cell body and can shift into different structures. Many proteins in the cell, including...

polarity of the cytoskeleton

How Cytoskeleton Polarity Guides Cell Movement

Cell polarity depends on the organization of the cytoskeleton and the uneven placement of cell parts. Two main factors help create this polarity. Mobile components such as regulatory molecules and subcellular structures can collect more on one side of the cell. Polar cytoskeletal filaments also line up along the cell’s axis of polarity. The interactions between cytoskeletal filaments help build and maintain this polarized shape. Several features also matter. These include the structure of the...

assembly of cytoskeletal filaments

Actin Bundles and Microtubule Cylinders

Cytoskeletal filaments are built from smaller protein subunits, but they can also join with similar filaments to form stronger cell structures. Microfilaments, which are made of actin monomers, depend on actin-binding proteins to form bundles and networks. Microtubules use microtubule-associated proteins, or MAPs, to form sturdy cylindrical structures. The protein partners for rope-like intermediate filament structures are still unknown. Actin bundles can be compact or loosely spaced. Compact...

cytoskeletal linker proteins - plakins

Plakins in Cell Junctions and Disease

Plakins are large cytoskeletal linker proteins that connect microtubules, microfilaments, intermediate filaments, and membrane protein complexes at cell junctions. They help organize the cytoskeleton by crosslinking its parts and by linking them to the cell matrix and cell adhesion complexes. These proteins also do more than provide structure. Plakins can interact with signal transducers, act as scaffolds for signaling complexes, and help control vesicle trafficking. They were first found with...

cytoskeletal accessory proteins

How Accessory Proteins Support the Cytoskeleton

Accessory proteins help the cytoskeleton work as a connected system. The cytoskeleton is a key cell structure with both structural and functional roles. Its filaments do not work well on their own, so accessory proteins assist with filament formation, stability, and function. These proteins also support communication between cytoskeletal filaments. They are found in both prokaryotes and eukaryotes, although bacterial accessory proteins differ a lot from one species to another. The evolutionary...

cytoskeletal proteins in bacteria

Bacterial Cytoskeleton and Cell Shape

Bacterial cytoskeletal proteins help bacteria keep their shape and divide correctly. They also help set cell polarity and move plasmids, which are small DNA circles, into place during cell division. Bacteria were once thought to be simple and randomly organized, but the discovery of cytoskeleton homologs changed that view. The main bacterial cytoskeletal proteins are actin-like and tubulin-like proteins. These proteins are more diverse in bacteria than in eukaryotic cells, and intermediate...

intracellular movement of viruses and bacteria

intracellular-movement-of-viruses-and-bacteria

How Viruses and Bacteria Ride the Cytoskeleton

Intracellular bacteria and viruses use the host cell cytoskeleton to move inside and between cells. These pathogens can travel from the cell surface to the nuclear region and back again. They may also spread across cells through cortical protrusions, which are cell membrane extensions at the edge of the cell. Several infectious agents use this strategy. Bacterial examples include Rickettsia, which can cause Rocky Mountain spotted fever and Mediterranean spotted fever, Chlamydia, which causes a...

studying the cytoskeleton

Visualizing Cytoskeleton Structure and Motion

The cytoskeleton can be studied with microscopy and biochemical methods. Electron microscopy helped reveal its architecture in the 1960s. It gives very high-resolution structural detail, but sample preparation can limit what is seen in biological samples. One electron microscopy method is rotary shadowing, also called metal replica. In this protocol, cytoskeletal filaments are fixed with chemicals such as glutaraldehyde or formaldehyde. The sample is then dehydrated with alcohol to a critical...

introduction to actin

Actin Structure, Isoforms, and Roles

Actin is a major cytoskeletal protein in eukaryotic cells. In muscle cells, it can make up about 10% of the total cellular protein. In non-muscle cells, it is lower and usually makes up around 1 to 5 percent of total cell protein. Actin is also highly conserved, which means it has changed very little over time. Actin in unicellular amoebae and in complex multicellular animals is about 80% similar. Actin genes are also conserved within a species and across different species. For example, actin...

actin polymerization

Actin Filament Growth Stages

Actin filament growth starts when G-actin, or monomeric actin, links together to form F-actin, the filament form. This process builds the actin network in cells through head-to-tail binding between actin subunits. It moves through three stages: nucleation, elongation, and the steady-state phase. Nucleation is the first and hardest step. During this phase, three actin monomers come together to form a stable nucleus. That nucleus then serves as the start of a new actin filament. After...

actin treadmilling

Actin Filament Growth and Loss

Actin filaments grow and shrink at the same time in a process called treadmilling. In this process, G-actin monomers are added at one end of the filament and removed from the other end. The rate of each step depends on the amount of free G-actin in the cytosol, the fluid inside the cell. The plus end, also called the barbed end, usually adds actin faster. The minus end, also called the pointed end, usually loses actin faster. At steady state, the critical concentration is the level of free...

generation of straight or branched actin filaments

generation-of-straight-or-branched-actin-filaments

Actin Filament Branching and Straight Growth

Actin filaments can grow as either straight strands or branched networks. Two nucleating proteins control this shape choice: formins and the Arp2/3 complex. Formins build straight actin filaments, while the Arp2/3 complex builds branched ones. The Arp2/3 complex is made of seven subunits. Two of them, Arp2 and Arp3, are actin-like proteins, and five other subunits help keep them inactive until they are needed. Activation happens with help from other proteins called nucleation-promoting...

actin filament depolymerization

Actin Filament Breakdown at Cell Ends

Actin filaments are built from actin subunits, and they can break down from either end. This process is called depolymerization. It happens faster at the minus-end, also called the pointed end, where the subunits are usually in the ADP-actin form. Several proteins help speed up actin filament breakdown. The actin-depolymerizing factor, or ADF, and cofilin proteins bind to ADP-actin in a one-to-one ratio. When they bind, the filament twists, which creates stress and makes it brittle. That...

formation of higher-order actin filaments

formation-of-higher-order-actin-filaments

Actin Bundles and Cell Shape

Actin bundles and cross-links help shape cells by organizing F-actin into larger networks. G-actin monomers first polymerize into filamentous F-actin, and those filaments then assemble into higher-order structures that support cell function. These structures can help build lamellipodia and filopodia at the leading edge of a migrating cell. They also help form microvilli on the brush border of epithelial cells. Higher-order actin networks can form in two main ways. Straight F-actins may bundle...

overview of myosin structure and function

overview-of-myosin-structure-and-function

Myosin Types in Muscle and Cell Transport

Myosins are molecular motor proteins that help cells move materials and generate force. They were first identified in skeletal muscle, where they drive muscle contraction. They also help move molecules and vesicles inside cells. Myosin proteins are divided into 24 classes based on their domain sequence and organization. Six classes are especially well characterized: Myosin I, Myosin II, Myosin V, Myosin VI, Myosin VII, and Myosin X. These proteins also take part in contractile ring formation...

actin and myosin in muscle contraction

Sarcomere Structure in Skeletal Muscle

Sarcomere structure in skeletal muscle explains how actin and myosin help muscles contract. These contractile proteins are arranged in repeating units called sarcomeres, which are found in skeletal muscle tissue. Their repeated pattern gives skeletal muscle a striped, or striated, look under a microscope. The bands in a myofibril create this striped pattern. Dark A bands and light I bands repeat along the length of the myofibrils. When many myofibrils line up in a muscle cell, the whole cell...

Actin and myosin form contractile bundles in non-muscle cells. These actomyosin structures help cells change shape, attach to surfaces, and divide. They were first observed in Dictyostelium and Acanthamoeba. Two common bundles are stress fibers and actomyosin adherence belts. These bundles are smaller and less organized than the ones found in muscle cells. Accessory proteins such as fascin, filamin, and fimbrin help hold them together, depending on where they are in the cell. Their formation...

key terms and concepts

Learn how actin and myosin build stress fibers and adherence belts in non-muscle cells, helping cells attach, change shape, and complete cytokinesis.

How Actomyosin Bundles Shape Cell Movement | JoVE K12

cell biology

JoVE Core Cell Biology illustrates complex cellular processes in easy-to-understand yet comprehensive animated video lessons. This collection focuses on the essential components and functions of cells, including organelles and membranes, cellular transport, and cell energetics. It is complemented by scientist-in-action videos that demonstrate the application of cell biology in real-world research experiments.

How Actomyosin Bundles Shape Cell Movement

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