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Dynein
Dyneins are a family of cytoskeletal motor proteins that move along microtubules in cells. They convert the chemical energy stored in ATP to mechanical work. Dynein transports various cellular cargos, provides forces and displacements important in mitosis, and drives the beat of eukaryotic cilia and flagella. All of these functions rely on dynein's ability to move towards the minus-end of the microtubules, known as retrograde transport; thus, they are called "minus-end directed motors". In contrast, most kinesin motor proteins move toward the microtubules' plus-end, in what is called anterograde transport. Classification Dyneins can be divided into two groups: cytoplasmic dyneins and axonemal dyneins, which are also called ciliary or flagellar dyneins. * cytoplasmic ** heavy chain: DYNC1H1, DYNC2H1 ** intermediate chain: DYNC1I1, DYNC1I2 ** light intermediate chain: DYNC1LI1, DYNC1LI2, DYNC2LI1 ** light chain: DYNLL1, DYNLL2, DYNLRB1, DYNLRB2, DYNLT1, DYNLT3 * axo ...
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Axonemal Dynein
Dyneins are a family of cytoskeletal motor proteins that move along microtubules in cells. They convert the chemical energy stored in ATP to mechanical work. Dynein transports various cellular cargos, provides forces and displacements important in mitosis, and drives the beat of eukaryotic cilia and flagella. All of these functions rely on dynein's ability to move towards the minus-end of the microtubules, known as retrograde transport; thus, they are called "minus-end directed motors". In contrast, most kinesin motor proteins move toward the microtubules' plus-end, in what is called anterograde transport. Classification Dyneins can be divided into two groups: cytoplasmic dyneins and axonemal dyneins, which are also called ciliary or flagellar dyneins. * cytoplasmic ** heavy chain: DYNC1H1, DYNC2H1 ** intermediate chain: DYNC1I1, DYNC1I2 ** light intermediate chain: DYNC1LI1, DYNC1LI2, DYNC2LI1 ** light chain: DYNLL1, DYNLL2, DYNLRB1, DYNLRB2, DYNLT1, DYNL ...
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DYNLL1
Dynein light chain 1, cytoplasmic is a protein that in humans is encoded by the ''DYNLL1'' gene. Function Cytoplasmic dyneins are large enzyme complexes with a molecular mass of about 1,200 kD. They contain two force-producing heads formed primarily from dynein heavy chains, and stalks linking the heads to a basal domain, which contains a varying number of accessory intermediate chains. The complex is involved in intracellular transport and motility. The protein described in this record is a light chain and exists as part of this complex but also physically interacts with and inhibits the activity of neuronal nitric oxide synthase. Binding of this protein destabilizes the neuronal nitric oxide synthase dimer, a conformation necessary for activity, and it may regulate numerous biologic processes through its effects on nitric oxide synthase activity. Alternate transcriptional splice variants have been characterized. Interactions DYNLL1 has been shown to interact with: * BCL2L ...
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Motor Protein
Motor proteins are a class of molecular motors that can move along the cytoplasm of cells. They convert chemical energy into mechanical work by the hydrolysis of ATP. Flagellar rotation, however, is powered by a proton pump. Cellular functions Motor proteins are the driving force behind most active transport of proteins and vesicles in the cytoplasm. Kinesins and cytoplasmic dyneins play essential roles in intracellular transport such as axonal transport and in the formation of the spindle apparatus and the separation of the chromosomes during mitosis and meiosis. Axonemal dynein, found in cilia and flagella, is crucial to cell motility, for example in spermatozoa, and fluid transport, for example in trachea. The muscle protein myosin "motors" the contraction of muscle fibers in animals. Diseases associated with motor protein defects The importance of motor proteins in cells becomes evident when they fail to fulfill their function. For example, kinesin deficiencie ...
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Microtubule
Microtubules are polymers of tubulin that form part of the cytoskeleton and provide structure and shape to eukaryotic cells. Microtubules can be as long as 50 micrometres, as wide as 23 to 27  nm and have an inner diameter between 11 and 15 nm. They are formed by the polymerization of a dimer of two globular proteins, alpha and beta tubulin into protofilaments that can then associate laterally to form a hollow tube, the microtubule. The most common form of a microtubule consists of 13 protofilaments in the tubular arrangement. Microtubules play an important role in a number of cellular processes. They are involved in maintaining the structure of the cell and, together with microfilaments and intermediate filaments, they form the cytoskeleton. They also make up the internal structure of cilia and flagella. They provide platforms for intracellular transport and are involved in a variety of cellular processes, including the movement of secretory vesicles, ...
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DYNLT3
Dynein, light chain, Tctex-type 3, also known as DYNLT3, is a protein which in humans is encoded by the ''DYNLT3'' gene. Function DYNLT3 is a member of the dynein motor protein family. DYNLT3 binds to BUB3, a spindle checkpoint protein is present on kinetochores at prometaphase. DYNLT3 can also function as a transcription regulator of Bcl-2 gene through binding to SATB1 SATB1 (special AT-rich sequence-binding protein-1) is a protein which in humans is encoded by the ''SATB1'' gene. Function SATB1, the global chromatin organizer and transcription factor, has emerged as a key factor integrating higher-order chro ... in a dynein-independent manner. Interactions DYNLT3 has been shown to interact with VDAC1. References Further reading

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Kinesin
A kinesin is a protein belonging to a class of motor proteins found in eukaryotic cells. Kinesins move along microtubule (MT) filaments and are powered by the hydrolysis of adenosine triphosphate (ATP) (thus kinesins are ATPases, a type of enzyme). The active movement of kinesins supports several cellular functions including mitosis, meiosis and transport of cellular cargo, such as in axonal transport, and intraflagellar transport. Most kinesins walk towards the plus end of a microtubule, which, in most cells, entails transporting cargo such as protein and membrane components from the center of the cell towards the periphery. This form of transport is known as anterograde transport. In contrast, dyneins are motor proteins that move toward the minus end of a microtubule in retrograde transport. Discovery Kinesins were discovered in 1985, based on their motility in cytoplasm extruded from the giant axon of the squid. They turned out as MT-based anterograde intracellular trans ...
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DYNLL2
Dynein light chain 2, cytoplasmic is a protein that in humans is encoded by the ''DYNLL2'' gene. Interactions DYNLL2 has been shown to Protein-protein interaction, interact with DLG4, C12orf40, DLGAP1, MYO5A and BMF (gene), BMF. References Further reading * * * * * * * * External links

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DYNLRB1
Dynein light chain roadblock-type 1 is a protein that in humans is encoded by the ''DYNLRB1'' gene. This gene is a member of the roadblock dynein light chain family and encodes a cytoplasmic protein that is capable of binding intermediate chain proteins. Upregulation In the biological context of organisms' production of gene products, downregulation is the process by which a cell decreases the quantity of a cellular component, such as RNA or protein, in response to an external stimulus. The complementary proc ... of this gene has been associated with hepatocellular carcinomas, suggesting that this gene may be involved in tumor progression. References Further reading * * * * * * * * * * * * * * * External links

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DNAH5
Dynein axonemal heavy chain 5 is a protein that in humans is encoded by the ''DNAH5'' gene. ''DNAH5'' is a protein-coding gene.1 It provides the instructions for synthesizing a protein that belongs to a microtubule-associated protein complex made of heavy, light and intermediate chains.2 ''DNAH5'' is responsible for making the heavy chain 5, found within the outer dynein arms of cilia.1 It will function as a force generating protein by using ATP, producing the power stroke for cilia.3 During early development, the cilia found on the primitive node will beat in a directional pattern, sending signaling molecules to the left, this process will begin to establish the internal left-right asymmetry.3 Mutations in ''DNAH5'' are linked to primary ciliary dyskinesia, an autosomal recessive disorder.4 This X-linked disorder is characterized by recurrent respiratory infections, infertility, and abnormal organ placement.1 Non-functional DNAH5 proteins have been identified in individuals with ...
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DNAH1
Dynein axonemal heavy chain 1 is a protein that in humans is encoded by the DNAH1 gene In biology, the word gene (from , ; "... Wilhelm Johannsen coined the word gene to describe the Mendelian units of heredity..." meaning ''generation'' or ''birth'' or ''gender'') can have several different meanings. The Mendelian gene is a b .... Function This gene encodes an inner dynein arm heavy chain that provides structural support between the radial spokes and the outer doublet of the sperm tail. Naturally occurring mutations in this gene are associated with primary ciliary dyskinesia and multiple morphological anomalies of the flagella that result in asthenozoospermia and male infertility. Mice with a homozygous knockout of the orthologous gene are viable but have reduced sperm motility and are infertile. rovided by RefSeq, Feb 2017 References Further reading

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DYNLT1
Dynein light chain Tctex-type 1 is a protein that in humans is encoded by the DYNLT1 gene. Cytoplasmic dynein is the major motor protein complex responsible for minus-end, microtubule-based motile processes. Each dynein complex consists of 2 heavy chains that have ATPase and motor activities, plus a group of accessory polypeptides Peptides (, ) are short chains of amino acids linked by peptide bonds. Long chains of amino acids are called proteins. Chains of fewer than twenty amino acids are called oligopeptides, and include dipeptides, tripeptides, and tetrapeptides. A p .... TCTEX1 is a dynein light chain involved in cargo binding (Chuang et al., 2005). upplied by OMIMref name="entrez" /> References Further reading

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Cilia
The cilium, plural cilia (), is a membrane-bound organelle found on most types of eukaryotic cell, and certain microorganisms known as ciliates. Cilia are absent in bacteria and archaea. The cilium has the shape of a slender threadlike projection that extends from the surface of the much larger cell body. Eukaryotic flagella found on sperm cells and many protozoans have a similar structure to motile cilia that enables swimming through liquids; they are longer than cilia and have a different undulating motion. There are two major classes of cilia: ''motile'' and ''non-motile'' cilia, each with a subtype, giving four types in all. A cell will typically have one primary cilium or many motile cilia. The structure of the cilium core called the axoneme determines the cilium class. Most motile cilia have a central pair of single microtubules surrounded by nine pairs of double microtubules called a 9+2 axoneme. Most non-motile cilia have a 9+0 axoneme that lacks the central pai ...
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