Name: myosin types in muscle and cell transport
Uploaded: 2023-04-30T09:31:54.000Z
Duration: 1 min 15 s
Channel: JoVE

K12 Standards

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NC K-12 Science Standard Course of Study

9-12

Biology

from-molecules-to-organisms-structures-and-processes

From Molecules to Organisms- Structures and Processes

LS.Bio.1.3

overview-of-myosin-structure-and-function

Overview of Myosin Structure and Function

Myosin is a superfamily of actin-based motor proteins, with prominent members myosin I and II.
Myosin I is a short monomeric protein with a globular head attached to the actin filaments and a short tail that binds vesicles and organelles for cargo transport.
Myosin II, found in the sarcomere of muscle cells, is a highly asymmetric dimer, consisting of six polypeptide subunits&#8212;two identical heavy chains and one pair each of essential and regulatory light chains.
The heavy chains have an N-terminal globular head domain with a nucleotide-binding site for ATPase activity, and an actin-binding site, for attaching to the actin filament.
Adjacent to the actin-binding domain is a flexible neck attached to the light chains that extend to a long alpha-helical C-terminal tail forming a coiled-coil structure.
The essential light chains maintain the stability of the coiled-coil tail of the heavy chains, while the regulating light chains help in the movement of the globular heads during cross-bridge formation with actin filaments during muscle contraction.

overview of myosin structure and function

Myosins are a family of molecular motor proteins, first identified in the skeletal muscles, where they are responsible for muscle contraction. Along with their role in muscle contraction, these proteins also play a role in the intracellular transport of molecules and vesicles. There are twenty-four classes of myosins based on their domain sequence and organization. Of the twenty-four, six classes (Myosin I, Myosin II, Myosin V, Myosin VI, Myosin VII, and Myosin X)&#160; have been well characterized. The other roles of these molecular motor proteins include forming contractile rings during cytokinesis, organelle transport across polar actin filaments, aiding cell polarization, and signal transduction.
Myosin I is a monomeric protein with a globular head and a short tail. Unlike other myosin proteins, the tail domain can bind with a lipid membrane. The globular head with the actin-binding domain attaches to the F-actin. This myosin protein allows the intracellular transport of molecules and vesicles. Along with actin filaments, they are also present in intestinal cells as a component of the small cellular projections in microvilli.
Myosin II is the most widely studied member of this class of proteins, and its role in high-speed motility for muscle contraction has been well established. The general structure of myosin II is a dimer composed of two helically arranged polypeptide chains, each having a globular head, a narrow neck, and an alpha-helical tail. Each globular head has an actin-binding and ATP-binding domain where ATP hydrolysis occurs. The neck portion comprises a shorter light chain domain that acts as a lever for the neck movement, and the tail region has a long heavy chain domain that extends into the tail. The two tail polypeptide chains form a coiled-coil structure.

Myosins are a family of molecular motor proteins, first identified in the skeletal muscles, where they are responsible for muscle contraction. Along with ...

Education

JoVE Core

Cell Biology

Unit 1

The Cytoskeleton I: Actin and Microfilaments

the-cytoskeleton-i-actin-and-microfilaments

KEY TERMS AND CONCEPTS

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 during cytokinesis, organelle transport across polar actin filaments, cell polarization, and signal transduction.

Myosin I is a monomeric protein, which means it is made of one unit. It has a globular head and a short tail. Its tail can bind to a lipid membrane, and its head binds to F-actin through an actin-binding domain. This myosin helps transport molecules and vesicles inside the cell, and it is also found in intestinal cells as part of microvilli.

Myosin II is the most widely studied myosin class and is known for high-speed motility in muscle contraction. Its structure is a dimer made of two helically arranged polypeptide chains. Each chain has a globular head, a narrow neck, and an alpha-helical tail. The head contains actin-binding and ATP-binding domains, where ATP hydrolysis occurs. The neck has a shorter light chain domain that acts as a lever, and the tail contains a long heavy chain domain. The two tails form a coiled-coil structure.

Myosin Types in Muscle and Cell Transport

myosin-types-in-muscle-and-cell-transport

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...

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...

the role of actin and myosin in non-muscle cells

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

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...

key terms and concepts

Explore myosin classes, from muscle contraction to vesicle transport. Learn how Myosin I and Myosin II differ in structure and function.

Myosin Types in Muscle and Cell Transport | 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.

Pennsylvania State Academic Standards

Life Science

Structure and Function

3.1.9-12.A

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Ohio’s Learning Standards and Model Curriculum

Cells

Cell structure and function

Virginia  Standards of Learning

HIgh School

BIO.3

BIO.3.a

Arizona Science Standards

High School

HS+B.L1

HS+B.L1U1.4

Alabama Course of Study Science

From Molecules to Organisms: Structures and Processes

9-12.B.1.1

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Myosin Types in Muscle and Cell Transport

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