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FLASH GENE
Symbol MYO10 contributors: mct - updated : 10-03-2015
HGNC name myosin X
HGNC id 7593
Location 5p15.1      Physical location : 16.662.016 - 16.936.385
Synonym symbol(s) KIAA0799, FLJ10639, FLJ21066, FLJ22268
DNA
TYPE functioning gene
STRUCTURE 274.37 kb     41 Exon(s)
10 Kb 5' upstream gene genomic sequence study
MAPPING cloned Y linked   status confirmed
RNA
TRANSCRIPTS type messenger
identificationnb exonstypebpproduct
ProteinkDaAAspecific expressionYearPubmed
41 - 11436 240 2058 - 2006 16371656
- - - 165 1401 in cortical neurons, only been identified in the nervous system 2012 22661706
  • lacks a functional motor domain and is known as headless MYO10
  • enrichment in regions of proliferating and migrating cells, including the embryonic ventricular zone and the postnatal rostral migratory stream
  • unable to function as a molecular motor, but is otherwise identical to full-length MYO10 and, containing three pleckstrin homology (PH) domains, a myosin-tail homology 4 (MyTH4) domain, and a band-4.1/ezrin/radixin/moesin (FERM) domain
  • can function as a negative regulator of MYO10 and that the two isoforms of MYO10 have opposing roles in axon outgrowth
  • EXPRESSION
    Type ubiquitous
       expressed in (based on citations)
    organ(s)
    SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
    Cardiovascularvessel   highly Homo sapiens
    Nervousbrainforebraincerebral cortex   Homo sapiens
     brainhindbraincerebellum highly Homo sapiens
    Reproductivefemale systemuteruscervix highly
    Respiratoryrespiratory tractlarynx  predominantly
    Skin/Tegumentskin   highly
    tissue
    SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
    Connective   moderately
    cells
    SystemCellPubmedSpeciesStageRna symbol
    Blood/Hematopoieticprogenitor cell Homo sapiensFetal
    Nervousneuron Homo sapiens
    NervousPurkinje cell Homo sapiens
    cell lineage
    cell lines
    fluid/secretion
    at STAGE
    physiological period fetal
    Text moderately in umbilical cord
    PROTEIN
    PHYSICAL PROPERTIES
    STRUCTURE
    motifs/domains
  • an N terminal motor domain containing ATP and actin-binding sites
  • a Myosin head-like
  • three IQ calmodulin or calmodulin-like light chain binding domains (the third IQ domain [IQ3] is critical for calmodulin-like protein binding)
  • two pleckstrin homology (PH) domains, the second (Myo10-PH2) specifically binds to PtdIns(3,4,5)P&
  • 8323;, and the disruption of this binding led to impairment of filopodia
  • an myosin-tail homology 4 (MyTH4) domain, that is folded into a helical VHS-like structure and is associated with the FERM domain
  • tail region containing a unique array of domains reported to bind to molecules with prominent roles in neuronal function
  • a band-4.1/ezrin/radixin/moesin (FERM) domain
  • 50-AA fragment C-terminal to the SAH forms a stable, antiparallel coiled-coil dimer
  • predicted coiled-coil region (aa 813–962) immediately C-terminal to its IQ motifs with the first 35-AAs (aa 813–847) of this predicted coiled coil that form a monomeric SAH, and the coiled-coil domain C-terminal forms a stable, anti-CC dimer
  • secondary structure a single alpha-helical domain (SAH) that can extend the lever arm, although it is possible that the antiparallel coiled coil also plays a role in extending the lever arm )
    HOMOLOGY
    interspecies homolog to rattus Myo10 (94.8 pc)
    homolog to murine Myo10 (94.2 pc)
    Homologene
    FAMILY
  • myosin family
  • member of a novel class of unconventional myosins characterized by a tail domain containing multiple pleckstrin homology domains
  • CATEGORY motor/contractile
    SUBCELLULAR LOCALIZATION     intracellular
    intracellular,cytoplasm,organelle,lysosome
    intracellular,cytoplasm,cytoskeleton,microtubule,mitotic spindle
    intracellular,cytoplasm,cytoskeleton,microfilament
    text
  • localized to the tips of filopodia, and undergoes intrafilopodial motility
  • also present in cell bodies, neurites, growth cones
  • localizes to mitotic spindle poles and is essential for proper spindle anchoring, normal spindle length, spindle pole integrity, and progression through metaphase
  • localizes to the tips of filopodia and has critical functions in filopodia
  • basic FUNCTION
  • playing a role in regions of dynamic actin
  • functioning in filopodia formation
  • having a role in neuronal actin dynamics
  • playing a role in regulating netrin-1 function
  • is involved in processes ranging from filopodial formation and extension to spindle orientation during cell division
  • important for assembly of meiotic spindles, and having also a role as well as F-actin, in mitotic spindles
  • requirement in spindle pole integrity is F-actin independent, whereas F-actin and MYO10 actually play antagonistic roles in maintenance of spindle length
  • required for pole integrity and normal spindle length by localizing to poles and exerting pulling forces on actin filaments within the spindle
  • plays a role in osteoclast attachment and podosome positioning by direct linkage of actin to the microtubule network
  • transports vascular endothelium-cadherin along filopodia to allow the formation of early endothelial cell-cell contacts
  • role that it plays in filopodial induction suggests that it may function as a bundled actin filament-selective motor
  • molecular motor that is adapted to select bundled actin filaments over single actin filaments for processive motility
  • important unconventional myosin that is critical for cargo transportation to filopodia tips and is also utilized in spindle assembly by interacting with microtubules
  • functions in polarized epithelial cells in junction formation, regulation of paracellular permeability, and epithelial morphogenesis
  • unconventional myosin that localizes to and induces filopodia, structures that are critical for growing axons
  • is likely to have critical functions in neuronal development
  • required for protrusion of growth cones and branches, whereas headless MYO10 opposes the activity of MYO10
  • important role for movement in filopodia
  • unexpected dimerization mechanism discovered in MYO10 may also be relevant to other coiled-coil–containing myosins
  • involved in the regulation of filopodia formation in non-neuronal cells
  • induces formation of dendritic filopodia and modulates filopodia dynamics by trafficking the actin-binding protein vasodilator-stimulated phosphoprotein (VASP) to the tips of filopodia
  • is an actin-based molecular motor that participates in essential intracellular processes such as filopodia formation/extension, phagocytosis, cell migration, and mitotic spindle maintenance
  • load-dependent processivity of myosin-10 as a filopodial transport motor
  • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling signal transduction
    a component
  • calmodulin-like protein (CLP) is a specific light chain of unconventional myosin-10 (Myo10) and enhances Myo10-dependent filopodial extension
  • antiparallel dimerization mechanism in myosin X (MYO10), suggesting that this structural arrangement allows more efficient processive walking in the parallel actin bundles of filopodia )
  • INTERACTION
    DNA
    RNA
    small molecule
  • ATP
  • protein
  • actin
  • interacting with UNC5A (MYO10 interacts with the netrin receptor deleted in colorectal cancer (DCC) and neogenin)
  • phenylalanine-795 in the third IQ domain (IQ3) of MYO10 is critical for CALML3 binding
  • increased CALML3 expression and CALML3-mediated MYO10 function are important for skin differentiation and wound reepithelialization
  • PtdIns(3,4,5)P&
  • 8323; binding to the MYO10-PH2 domain is involved in MYO10 trafficking and regulation of filopodia dynamics
  • DCC promotes movement of MYO10 along basal actin filaments and enhances MYO10-mediated basal filopodium elongation
  • novel function for ADD1 in mitotic spindle assembly through its interaction with MYO10
  • cell & other
    REGULATION
    Other differentially regulated by DCC and neogenin
    ASSOCIATED DISORDERS
    corresponding disease(s)
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    constitutional     --over  
    led to increased formation of podosome belts along with larger sealing zones and enhanced bone resorptive capacity
    Susceptibility
    Variant & Polymorphism
    Candidate gene
    Marker
    Therapy target
    ANIMAL & CELL MODELS