MYO10

Last updated
MYO10
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases MYO10 , myosin X, MyoX
External IDs OMIM: 601481 MGI: 107716 HomoloGene: 36328 GeneCards: MYO10
Orthologs
SpeciesHumanMouse
Entrez

4651

17909

Ensembl

ENSG00000145555

ENSMUSG00000022272

UniProt

Q9HD67

F8VQB6

RefSeq (mRNA)

NM_012334

NM_019472
NM_001353141
NM_001353142

RefSeq (protein)

NP_036466

NP_062345
NP_001340070
NP_001340071

Location (UCSC) Chr 5: 16.66 – 16.94 Mb Chr 15: 25.62 – 25.81 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Myosin X, also known as MYO10, is a protein that in humans is encoded by the MYO10 gene. [5] [6] [7] [8]

Contents

Myo10 is an actin-based motor protein that can localize to the tips of the finger-like cellular protrusions known as filopodia. [9] [10] Myo10 is broadly expressed in mammalian tissues, although at relatively low levels. [8] Studies with knockout mice demonstrate that Myo10 has important functions in embryonic processes such as neural tube closure and eye development. [11] [12] [13] Myo10 also has important functions in cancer invasion and growth. [14] [15] [9] [12] [16] [17]

Myo10 should not be confused with Myh10, which encodes the heavy chain of the class II myosin known as non-muscle myosin 2b.

Structure and function

Bar diagram illustrating the domain structures of full-length and headless Myo10 from human. IQ indicates the 3 IQ motifs, each of which binds to a calmodulin or calmodulin-like light chain. The IQ motifs are followed by an alpha-helical region consisting of an N-terminal segment that forms a single stable alpha helix (SAH) and a C-terminal segment that can dimerize by forming an antiparallel coiled coil (CC). See text for additional discussion and references. The approximate positions along the amino acid sequence of the major domains are based on. (Diagram courtesy of Joshua K. Zachariah and Richard E. Cheney) Bar Diagram of Full-length and Headless MyoX.png
Bar diagram illustrating the domain structures of full-length and headless Myo10 from human. IQ indicates the 3 IQ motifs, each of which binds to a calmodulin or calmodulin-like light chain. The IQ motifs are followed by an alpha-helical region consisting of an N-terminal segment that forms a single stable alpha helix (SAH) and a C-terminal segment that can dimerize by forming an antiparallel coiled coil (CC). See text for additional discussion and references. The approximate positions along the amino acid sequence of the major domains are based on. (Diagram courtesy of Joshua K. Zachariah and Richard E. Cheney)

The human MYO10 gene spans ~274 kb and is located on chromosome 5 band 5p15.1 (GRCh Ensembl release 89). It produces a full-length RNA transcript with 41 exons encoding a MYO10 heavy chain whose deduced sequence has 2058 amino acids and a predicted molecular weight of ~237 kDa. Like many motor proteins, the full-length Myo10 protein can be considered to consist of a head, neck, and tail. [8] [21] The N-terminal head or myosin motor domain can bind to an actin filament, hydrolyze ATP, and produce force. [22] [23] The neck or light chain binding domain consists of 3 IQ motifs, with each IQ motif providing a binding site for one molecule of calmodulin, a ~16.5 kDa calcium-binding protein. [22] Unlike most calmodulin binding sites, which only bind to calmodulin in the presence of calcium, the IQ motifs in Myo10 can bind to calmodulin in the absence of calcium. The Myo10 IQ motifs have also been reported to bind CALML3, a calmodulin-like protein expressed in epithelial cells, so CALML3 may serve as a Myo10 light chain in place of calmodulin in some situations. [24] The Myo10 tail begins with an alpha-helical region whose proximal portion forms a single, stable alpha helix (SAH domain) that lengthens the lever arm formed by the neck domain. [25] [26] The distal portion of the alpha helical region can self-associate with a Kd of ~0.6 uM to form an antiparallel coiled coil, allowing two Myo10 heavy chains to form an antiparallel dimer, a unique structure among known myosins. [26] [27]

The Myo10 tail includes several regions in addition to the SAH and coiled coil. These include a region with 3 PEST sequences—sequences enriched in the amino acids Proline (P), Glutamine (E), Serine (S), and T (Threonine) that are often associated with cleavage by proteases such as calpain . [8] The Myo10 tail is unique among known myosins in containing 3 PH domains (Pleckstrin Homology domain), a domain often involved in binding to membranes. The sequence of Myo10's first PH domain is somewhat unusual in that it is split by the presence of a surface loop that contains the second PH domain. [8] [19] The second PH domain binds to the important signaling lipid phosphatidylinositol (3,4,5)-trisphosphate [PI(3,4,5)P3] and in some situations has been reported to bind to phosphatidylinositol (4,5)-bisphosphate [PI(4,5)P2]. [28] [19] [29] Myo10's 3 PH domains are thought to work together to recruit it to the plasma membrane. The Myo10 tail ends in a supramodule consisting of a MyTH4 domain (Myosin Tail Homology 4) and a FERM  domain (band 4.1, Ezrin, Radixin, Moesin). [18] [20] Myo10's MyTH4 domain can bind to microtubules with a reported affinity of ~0.24 uM and gives full-length Myo10 the important ability to link an actin filament bound by its head to a microtubule bound by its tail. [30] [18] [31] The Myo10 FERM domain can bind to the cytoplasmic domains of several β-integrins, a major class of cell adhesion receptor, and to the cytoplasmic domains of the netrin receptors Deleted in Colorectal Cancer (DCC) and neogenin (Neo1). [32] [33] Although full-length Myo10 protein appears to be expressed at relatively low levels, it can be detected in most mammalian tissues including brain, testes, kidney, lung, stomach, and pancreas. [8]

The native full-length Myo10 heavy chain can exist as a monomer with 3 calmodulin/calmodulin-like light chains or as an antiparallel dimer with 6 calmodulin/calmodulin-like light chains. An antiparallel Myo10 dimer with all 6 light chains would thus have 8 subunits and a native MW of ~574 kDa. Importantly, the tail in a Myo10 monomer can fold back onto the head to inhibit the head's motor activity. [29] Increases in plasma membrane PI(3,4,5)P3  levels are hypothesized to recruit Myo10 monomers to the plasma membrane via their PH domains, activating their motor activity and increasing their local concentration, leading to the formation of active antiparallel dimers that are capable moving along actin filaments. Myo10, like all known myosins other than Myo6, moves towards the barbed end of the actin filament. [34] Myo10 is capable of hydrolyzing ~10-20 ATP/s per head and has been reported to generate movement at rates of ~300-1500 nm/s. [23] [27] Single-molecule studies show that native Myo10 dimers can take steps of up to ~55 nm, which are among the largest steps reported for a motor protein. [27] Myo10's large step size is due in part to the long lever arm formed by its neck domain and stable alpha helix, and in part due to the remarkably large swing of ~120° the Myo10 lever arm undergoes during its power stroke. [27] There is much interest in the mechanisms that target Myo10 to filopodial actin bundles, and in Myo10's ability to step from one actin filament in a bundle to another. [35] [27] [36] In addition to the full-length Myo10 described above, the use of alternative transcription start sites located in intron 19-20 of the full-length transcript results in the production of "headless" Myo10 transcripts that lack most of the myosin head domain, but include the rest of the Myo10 heavy chain. [37] [38] [39] The major headless transcripts in human are predicted to include exons 20-41 of full-length MYO10 and initiation of translation at M644 would result in a 1415 amino acid headless protein with a predicted MW of ~163 kDa that would be identical to amino acids 644-2058 of full-length MYO10. [37] Because headless Myo10 lacks most of the head domain, it lacks motor activity, but it retains all of Myo10's other domains and is thus expected to retain the ability to bind to light chains of the calmodulin superfamily, to membranes containing PI(3,4,5)P3 or PI(4,5)P3, to microtubules, and to proteins that bind the Myo10 tail such as DCC, neogenin, and β-integrins. Headless Myo10 has been hypothesized to act as a scaffolding protein for its various binding partners and/or as a "natural" dominant negative that can inhibit the actions of full-length Myo10. [37] [38]

Evolutionary relationships

Myo10 is a member of an evolutionarily ancient group of myosins whose tails contain MyTH4-FERM domains and that have been shown to have important functions in cellular protrusions based on actin bundles such as filopodia, microvilli, and inner ear stereocilia. [40] [41] The slime mold Dictyostelium expresses a MyTH4-FERM myosin known as myosin-7 that is involved in filopodia formation and has 2 MyTH4-FERM supramodules but no PH domains. [40] Myo10 appears to have originated from an ancestral myosin-7-like protein approximately a billion years ago by several changes including loss of 1 MyTH4-FERM supramodule and addition of 3 PH domains. A Myo10 gene is present in organisms ranging from filozoans and choanoflagellates (the protozoan groups most closely related to multicellular animals) to humans. [40] Myo10 was lost in the invertebrate lineages leading to organisms such as fruit flies and nematodes, although these lineages do express other MyTH4-FERM myosins such as myosin-7. Humans express 3 MyTH4-FERM myosins in addition to Myo10: MYO7A, the gene that is mutated in Usher syndrome 1b deaf-blindness; MYO7B, a component of an adhesion complex at the tips of microvilli; and MYO15A, a myosin that localizes to the tips of inner ear stereocilia and that is mutated in DFNB3 deafness. [41] The head domains of the other MyTH4-FERM myosins expressed in human exhibit at most 45% overall amino acid sequence identity with Myo10 and their tail domains each contain 2 MyTH4-FERM domains instead of the 3 PH domains and 1 MyTH4-FERM domain in Myo10. [8] [41]

Cellular function

A CAD cell (a neuronal cell line) expressing GFP-Myo10 (green) was stained for actin filaments (red) to visualize the slender cellular protrusions known as filopodia. Overexpressing Myo10 induces large numbers of filopodia and is responsible for the unusually large number of filopodia on this cell. (Image courtesy of Aurea D. Sousa and Richard E. Cheney) Fluorescence image of a cell showing localization of Myo10 at the tips of filopodia.png
A CAD cell (a neuronal cell line) expressing GFP-Myo10 (green) was stained for actin filaments (red) to visualize the slender cellular protrusions known as filopodia. Overexpressing Myo10 induces large numbers of filopodia and is responsible for the unusually large number of filopodia on this cell. (Image courtesy of Aurea D. Sousa and Richard E. Cheney)

Myo10 can localize to the tips of filopodia, a property most other myosins lack. When Myo10 was tagged with Green Fluorescent Protein (GFP) and expressed in cells, small puncta of GFP-Myo10 were observed moving forward within filopodia towards the tip at rates of ~100 nm/s. [42] Imaging with single-molecule sensitivity revealed similar movements of individual Myo10 dimers at rates of ~600-1400 nm/s. [43] [44] [45] GFP-Myo10 also moves rearward in filopodia at retrograde flow rates of ~15 nm/s. These observations led to the hypothesis that Myo10 molecules use their motor activity to move themselves rapidly forward along filopodial actin filaments and can bind to filopodial actin filaments to be carried slowly rearward by retrograde actin flow. [42] This "intrafilopodial motility" of Myo10 has led to suggestions that Myo10 functions as a motor protein for transporting cargos within filopodia. Myo10 also has important functions in the formation and/or stabilization of filopodia, with Myo10 overexpression increasing the number and length of filopodia, while knockdown or knockout of Myo10 decreases filopodia. [42] [46] [47] Myo10 also has important functions in cell division, particularly in mitotic spindle orientation. [30] [48] [49] [50] Myo10 is also required to cluster the excess centrosomes that are a hallmark of cancer cells, [49] a process of great interest because cancer cells need to cluster their centrosomes to successfully divide.

Role in disease

Growing evidence demonstrates that Myo10 has important roles in cancer. [9] In addition to its role in clustering the excess centrosomes of cancer cells, [49] Myo10 is a key component of invadopodia, filopodia-related protrusions that cancer cells use to invade their surroundings. [51] Several microRNAs that suppress cancer cell invasion have also been reported to act in part by targeting the Myo10 mRNA. [52] [53] Knockout or knockdown of Myo10 is reported to suppress cancer cell invasion or spread in experimental models of breast cancer, [14] [15] lung cancer, [17] and glioma, [16] where knockout of Myo10 also increased the effectiveness of an otherwise ineffective chemotherapy agent. These results, plus research showing that knockout of Myo10 increased survival time by 260% in a mouse model of melanoma, [12] make Myo10 a potential anti-cancer target.

Related Research Articles

<span class="mw-page-title-main">Microfilament</span> Filament in the cytoplasm of eukaryotic cells

Microfilaments, also called actin filaments, are protein filaments in the cytoplasm of eukaryotic cells that form part of the cytoskeleton. They are primarily composed of polymers of actin, but are modified by and interact with numerous other proteins in the cell. Microfilaments are usually about 7 nm in diameter and made up of two strands of actin. Microfilament functions include cytokinesis, amoeboid movement, cell motility, changes in cell shape, endocytosis and exocytosis, cell contractility, and mechanical stability. Microfilaments are flexible and relatively strong, resisting buckling by multi-piconewton compressive forces and filament fracture by nanonewton tensile forces. In inducing cell motility, one end of the actin filament elongates while the other end contracts, presumably by myosin II molecular motors. Additionally, they function as part of actomyosin-driven contractile molecular motors, wherein the thin filaments serve as tensile platforms for myosin's ATP-dependent pulling action in muscle contraction and pseudopod advancement. Microfilaments have a tough, flexible framework which helps the cell in movement.

<span class="mw-page-title-main">Actin</span> Family of proteins

Actin is a family of globular multi-functional proteins that form microfilaments in the cytoskeleton, and the thin filaments in muscle fibrils. It is found in essentially all eukaryotic cells, where it may be present at a concentration of over 100 μM; its mass is roughly 42 kDa, with a diameter of 4 to 7 nm.

<span class="mw-page-title-main">Myosin</span> Superfamily of motor proteins

Myosins are a superfamily of motor proteins best known for their roles in muscle contraction and in a wide range of other motility processes in eukaryotes. They are ATP-dependent and responsible for actin-based motility.

<span class="mw-page-title-main">Tropomyosin</span> Protein

Tropomyosin is a two-stranded alpha-helical, coiled coil protein found in many animal and fungal cells. In animals, it is an important component of the muscular system which works in conjunction with troponin to regulate muscle contraction. It is present in smooth and striated muscle tissues, which can be found in various organs and body systems, including the heart, blood vessels, respiratory system, and digestive system. In fungi, tropomyosin is found in cell walls and helps maintain the structural integrity of cells.

<span class="mw-page-title-main">MYH7</span> Protein-coding gene in the species Homo sapiens

MYH7 is a gene encoding a myosin heavy chain beta (MHC-β) isoform expressed primarily in the heart, but also in skeletal muscles. This isoform is distinct from the fast isoform of cardiac myosin heavy chain, MYH6, referred to as MHC-α. MHC-β is the major protein comprising the thick filament that forms the sarcomeres in cardiac muscle and plays a major role in cardiac muscle contraction.

<span class="mw-page-title-main">Motor protein</span> Class of molecular proteins

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.

<span class="mw-page-title-main">Growth cone</span> Large actin extension of a developing neurite seeking its synaptic target

A growth cone is a large actin-supported extension of a developing or regenerating neurite seeking its synaptic target. It is the growth cone that drives axon growth. Their existence was originally proposed by Spanish histologist Santiago Ramón y Cajal based upon stationary images he observed under the microscope. He first described the growth cone based on fixed cells as "a concentration of protoplasm of conical form, endowed with amoeboid movements". Growth cones are situated on the tips of neurites, either dendrites or axons, of the nerve cell. The sensory, motor, integrative, and adaptive functions of growing axons and dendrites are all contained within this specialized structure.

<span class="mw-page-title-main">Nebulin</span> Protein-coding gene in the species Homo sapiens

Nebulin is an actin-binding protein which is localized to the thin filament of the sarcomeres in skeletal muscle. Nebulin in humans is coded for by the gene NEB. It is a very large protein and binds as many as 200 actin monomers. Because its length is proportional to thin filament length, it is believed that nebulin acts as a thin filament "ruler" and regulates thin filament length during sarcomere assembly and acts as the coats the actin filament. Other functions of nebulin, such as a role in cell signaling, remain uncertain.

<span class="mw-page-title-main">Filopodia</span> Actin projections on the leading edge of lamellipodia of migrating cells

Filopodia are slender cytoplasmic projections that extend beyond the leading edge of lamellipodia in migrating cells. Within the lamellipodium, actin ribs are known as microspikes, and when they extend beyond the lamellipodia, they're known as filopodia. They contain microfilaments cross-linked into bundles by actin-bundling proteins, such as fascin and fimbrin. Filopodia form focal adhesions with the substratum, linking them to the cell surface. Many types of migrating cells display filopodia, which are thought to be involved in both sensation of chemotropic cues, and resulting changes in directed locomotion.

<span class="mw-page-title-main">Myosin light-chain kinase</span> Class of kinase enzymes

Myosin light-chain kinase also known as MYLK or MLCK is a serine/threonine-specific protein kinase that phosphorylates a specific myosin light chain, namely, the regulatory light chain of myosin II.

<span class="mw-page-title-main">CDC42</span> Protein-coding gene in the species Homo sapiens

Cell division control protein 42 homolog is a protein that in humans is encoded by the CDC42 gene. Cdc42 is involved in regulation of the cell cycle. It was originally identified in S. cerevisiae (yeast) as a mediator of cell division, and is now known to influence a variety of signaling events and cellular processes in a variety of organisms from yeast to mammals.

<span class="mw-page-title-main">Unconventional myosin-Va</span> Protein-coding gene in the species Homo sapiens

Unconventional myosin-Va is a motor protein in charge of the intracellular transport of vesicles, organelles and protein complexes along the actin filaments. In humans it is coded for by the MYO5A gene.

<span class="mw-page-title-main">Unconventional myosin-VI</span>

Unconventional myosin-VI, is a protein that in humans is coded for by MYO6. Unconventional myosin-VI is a myosin molecular motor involved in intracellular vesicle and organelle transport.

<span class="mw-page-title-main">MYH9</span> Mammalian protein found in Homo sapiens

Myosin-9 also known as myosin, heavy chain 9, non-muscle or non-muscle myosin heavy chain IIa (NMMHC-IIA) is a protein which in humans is encoded by the MYH9 gene.

<span class="mw-page-title-main">Dynactin</span>

Dynactin is a 23 subunit protein complex that acts as a co-factor for the microtubule motor cytoplasmic dynein-1. It is built around a short filament of actin related protein-1 (Arp1).

<span class="mw-page-title-main">ANLN</span> Mammalian protein found in Homo sapiens

Anillin is a conserved protein implicated in cytoskeletal dynamics during cellularization and cytokinesis. The ANLN gene in humans and the scraps gene in Drosophila encode Anillin. In 1989, anillin was first isolated in embryos of Drosophila melanogaster. It was identified as an F-actin binding protein. Six years later, the anillin gene was cloned from cDNA originating from a Drosophila ovary. Staining with anti-anillin antibody showed the anillin localizes to the nucleus during interphase and to the contractile ring during cytokinesis. These observations agree with further research that found anillin in high concentrations near the cleavage furrow coinciding with RhoA, a key regulator of contractile ring formation.

<span class="mw-page-title-main">Unconventional myosin-Ia</span> Protein-coding gene in the species Homo sapiens

Unconventional myosin-Ia is a protein that in humans is encoded by the MYO1A gene.

<span class="mw-page-title-main">Rho-associated protein kinase</span>

Rho-associated protein kinase (ROCK) is a kinase belonging to the AGC family of serine-threonine specific protein kinases. It is involved mainly in regulating the shape and movement of cells by acting on the cytoskeleton.

<span class="mw-page-title-main">Myosin head</span> Part of myofilaments

The myosin head is the part of the thick myofilament made up of myosin that acts in muscle contraction, by sliding over thin myofilaments of actin. Myosin is the major component of the thick filaments and most myosin molecules are composed of a head, neck, and tail domain; the myosin head binds to thin filamentous actin, and uses ATP hydrolysis to generate force and "walk" along the thin filament. Myosin exists as a hexamer of two heavy chains, two alkali light chains, and two regulatory light chains. The heavy chain can be subdivided into the globular head at the N-terminal and the coiled-coil rod-like tail at the C-terminal, although some forms have a globular region in their C-terminal.

Force Spectrum Microscopy (FSM) is an application of active microrheology developed to measure aggregate random forces in the cytoplasm. Large, inert flow tracers are injected into live cells and become lodged inside the cytoskeletal mesh, wherein it is oscillated by repercussions from active motor proteins. The magnitude of these random forces can be inferred from the frequency of oscillation of tracer particles. Tracking the fluctuations of tracer particles using optical microscopy can isolate the contribution of active random forces to intracellular molecular transport from that of Brownian motion.

References

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  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000022272 - Ensembl, May 2017
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  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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