Myosins: A Superfamily of Molecular Motors

Myosins: A Superfamily of Molecular Motors
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The activated neurotrophin and receptor complex can promote neuron growth through regulating gene expression, only when the complex has been transported to neuron soma from the terminal of axon or presynapse Figure 5. It appeared that neurotrophin and its receptor are firstly endocytosed into cells and then transported to the cell nucleus periphery by interacting with cytoplasmic dynein in some unknown manner, which allows extracellular signals to be sent to the cell nucleus [ 58 ].

NGF binding to TrkA extracellular domain leads to a conformation change in its cytoplasmic domain and autophosphorylation its tyrosine residues, which enhance TrkA kinase activity [ 59 ]. BDNF has been demonstrated to regulate dendritic arborization and outgrowth during neuronal development [ 63 ]. The signaling endosomes then associate with dynein motor to undergo axonal retrograde transport to cell body to induce nuclear signal pathway [ 66 ].

Neurotransmission is the most important function of neuron system, a process of systematic communication between two neuronal cells. During the transmission, the neurotransmitters in the presynapse are released into the synaptic cleft and bind to the specific receptors on the postsynapse membrane. In presynapse, the synaptic vesicles containing neurotransmitters need to undergo a long axonal anterograde transport to reach the presynapse [ 68 ].

Additionally, myosin V has also been shown to associate with synaptic vesicles. In hippocampal neurons, myosin Va associates with the postsynaptic density PSD through directly interacting with guanylate kinase domain-associated protein GKAP , which binds to PSD [ 72 , 73 ]. In postsynapse Figure 5 , the receptors need to be transported to and from the postsynaptic membrane [ 76 ]. Myosin VI has been reported to interact with alpha-aminohydroxymethylisoxazolepropionic acid receptor AMPAR , a glutamate receptor, through binding directly to synapse-associated protein 97 SAP97 [ 77 ].

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It implies that the motors can recognize the cargo through specific interactions with adaptor proteins. Also, the different kinds of motors may act in a coherent manner during the cargo transportation process [ 79 , 80 ]. During this process, muskelin acts as the interconnector between actin-based retrograde trafficking and microtubule-based retrograde trafficking of GABAR. Some cytoskeleton motors, including myosin Ic, myosin III and myosin IX, play other roles as mechanoforce sensor, tether and signaling regulator.

Myosin Ic directly binds to cell membranes through the C-terminal pleckstrin homology PH motif, which allows it to crosslink the membranes and actin filaments and transduce the mechanical force from tail-binding membranes to head-binding filaments in inner ear stereocilia [ 83 ].

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A recent structural study showed that myosin Ic undergoes CaM-mediated conformational transformation upon mechanical force transduction [ 84 ]. Myosin III was also found to stimulate the elongation of stereocilia in hair cells through tethering and activating Espin1 at the tips of stereocilia, the plus ends of actin filaments [ 85 ].

Gene mutations in encoding these proteins can lead to hear loss disease [ 86 , 87 ]. In general, these diverse role manifests an integrated and complex function of myosin in cellular processes. We have summarized and discussed the roles of cytoskeleton motors during neuronal development and transmission function.

However, the structural basis for intracellular trafficking and regulations are not yet fully understood. Study on cytoskeleton motors' trafficking in neuron can help us to understand the cause of a variety of brain and nervous disorders. Although much progress has been made in past decades, structural study of neuronal-intracellular trafficking is still an attractive topic, especially in light of recent advance in macromolecule complex structure solvation technology, such as single particle cryo-EM [ 92 ].

To gain further mechanistic insights, we envisage that the following three aspects of intracellular trafficking pertaining to cytoskeleton motors deserve special attentions:. R FDCT project reference no. JCYJ to Z. Odronitz F, Kollmar M. Drawing the tree of eukaryotic life based on the analysis of 2, manually annotated myosins from species. Genome Biol. New insights into myosin evolution and classification. Axonal myosins. J Neurocytol.

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Functions of unconventional myosins. Curr Opin Cell Biol. Unconventional myosins in cell movement, membrane traffic, and signal transduction. Sweeney HL, Houdusse A. Structural and functional insights into the myosin motor mechanism. Annu Rev Biophys. Neck length and processivity of myosin V.

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J Biol Chem. Single-molecule tracking of myosins with genetically engineered amplifier domains. Nat Struct Biol. Krendel M, Mooseker MS. Myosins: tails and heads of functional diversity.

Cell Motil Cytoskeleton. Identification of an organelle receptor for myosin-Va. Nat Cell Biol. All kinesin superfamily protein, KIF, genes in mouse and human. A standardized kinesin nomenclature. J Cell Biol.

Goldstein LS, Yang Z. Microtubule-based transport systems in neurons: the roles of kinesins and dyneins. Annu Rev Neurosci.

Myosins: A Superfamily of Molecular Motors (Proteins and Cell Regulation)

Hirokawa N, Takemura R. Molecular motors and mechanisms of directional transport in neurons. Nat Rev Neurosci. A new kinesin tree. J Cell Sci. Hirokawa N.

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Invited conference report. Nat Commun 3 , Coluccio, J. Article Google Scholar Goldstein LS, Yang Z. Cancer Metastasis Rev.

Kinesin and dynein superfamily proteins and the mechanism of organelle transport. Vale RD.

Journal content

The molecular motor toolbox for intracellular transport. Genome Res. Molecular dissection of the roles of nucleotide binding and hydrolysis in dynein's AAA domains in Saccharomyces cerevisiae. Regulatory ATPase sites of cytoplasmic dynein affect processivity and force generation. Cytoplasmic dynein binds dynactin through a direct interaction between the intermediate chains and p Glued.

Egalitarian binds dynein light chain to establish oocyte polarity and maintain oocyte fate. Phosphorylation regulates targeting of cytoplasmic dynein to kinetochores during mitosis.

Cytoskeletal motors

A type VII myosin encoded by the mouse deafness gene shaker A core cochlear phenotype in USH1 mouse mutants implicates fibrous links of the hair bundle in its cohesion, orientation and differential growth. Interactions in the network of Usher syndrome type 1 proteins. Hum Mol Genet. Structure and function of the phosphothreonine-specific FHA domain. Sci Signal. Regulators of the cytoplasmic dynein motor. Nat Rev Mol Cell Biol.

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The p Glued component of the dynactin complex binds to both microtubules and the actin-related protein centractin Arp Dynein is required for polarized dendritic transport and uniform microtubule orientation in axons. The structure of the dynactin complex and its interaction with dynein. J Med Genet.

Lipid products of PI 3 Ks maintain persistent cell polarity and directed motility in neutrophils. PIP3 is involved in neuronal polarization and axon formation. J Neurochem. Mol Cell Biol. Shootin1: A protein involved in the organization of an asymmetric signal for neuronal polarization. Shootin1 acts in concert with KIF20B to promote polarization of migrating neurons. J Neurosci. Ohno S. Intercellular junctions and cellular polarity: the PAR-aPKC complex, a conserved core cassette playing fundamental roles in cell polarity.

Ron Vale (UCSF, HHMI) 3: Molecular Motor Proteins: Regulation of Mammalian Dynein

Reichardt LF. Neurotrophin-regulated signalling pathways. Bibel M, Barde YA. Neurotrophins: key regulators of cell fate and cell shape in the vertebrate nervous system. Genes Dev. Gene transfer and molecular cloning of the rat nerve growth factor receptor. Neurotrophin signaling: many exciting surprises!