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Motor proteins

Dynein

Adapted from Wikipedia ยท Discoverer experience

An animation showing how a protein called dynein moves along a tiny structure in our cells called a microtubule.

Dyneins are a special group of proteins in our cells that act like tiny machines. These machines, called motor proteins, move along thin strands inside cells known as microfilaments. They use a chemical called ATP for energy, turning it into movement that helps the cell do its work.

Cytoplasmic dynein on a microtubule

Dyneins have many important jobs in a cell. They carry important materials from one place to another, help cells divide, and make the hair-like structures on cells called cilia and flagella move. This movement is crucial for many processes in our bodies, like moving fluids through tiny tubes or helping cells split during growth.

Unlike most other motor proteins, dyneins move toward one specific end of the microfilaments, which scientists call the minus-end. This direction is important for many cell functions and is different from another type of motor protein called kinesin, which moves in the opposite direction. Thanks to dynein, our cells can keep working smoothly and efficiently.

Classification

Dyneins are divided into two main groups: cytoplasmic dyneins and axonemal dyneins, also called ciliary or flagellar dyneins. Cytoplasmic dyneins have several types of chains, including heavy chains like DYNC1H1 and DYNC2H1, and various intermediate and light chains. Axonemal dyneins also include several heavy chains such as DNAH2 and DNAH3, along with intermediate, light intermediate, and light chains. These different types help dyneins perform various important jobs inside cells.

Function

Axonemal dynein helps move tiny hair-like structures called cilia and flagella by sliding microscopic tubes inside cells. These structures are important for movement and sensing in many organisms.

Cytoplasmic dynein, found in most animal cells, helps move important parts inside the cell, like organelles and packages of materials called vesicles. It also plays a role in cell division by helping position the structures that separate chromosomes. Dynein works along microscopic tracks inside cells, allowing it to carry materials from one place to another without losing its grip.

Structure

Human cytoplasmic dynein 2 domains. Shown is the order of regions of interest for human cytoplasmic dynein 2 motor domains as they occur from the linker to C-terminal. This is oriented to demonstrate the general bound position of dynein on a microtubule. The mirror effect allows the view to observe the dynein from both sides of the complex.

Each dynein molecule is a complex made of many smaller parts called polypeptides. There are two main types: cytoplasmic dynein and axonemal dynein. Both have similar parts but also some unique ones.

Cytoplasmic dynein helps move things inside cells. It has heavy chains that generate movement, intermediate chains that attach to cargo, and light chains. Axonemal dynein is found in structures like cilia and flagella, helping them move by sliding microtubules past each other. This movement allows cells to propel themselves or move particles.

History

The protein that makes cilia and flagella move was first found and named dynein in 1963. Twenty years later, another type of dynein inside cells was discovered and identified.

Chromosome segregation during meiosis

During the first division of meiosis, homologous chromosomes move to opposite ends of the cell. This process is important for creating cells with the right number of chromosomes. In most cases, structures called chiasmata help this process, but in some yeast, a protein called dynein can do the job even without them. Specific parts of the dynein protein, like Dhc1 and Dlc1, are needed for this movement to happen correctly.

Images

A colorful cartoon showing the shape of a tiny protein called dynein light chain 1, which helps cells move.
Scientific illustration showing the structure of a protein called Roadblock from mouse cells.

This article is a child-friendly adaptation of the Wikipedia article on Dynein, available under CC BY-SA 4.0.

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