Myosin Va
Mostrando 1-12 de 18 artigos, teses e dissertações.
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1. Myosin Va is developmentally regulated and expressed in the human cerebellum from birth to old age
Myosin Va functions as a processive, actin-based motor molecule highly enriched in the nervous system, which transports and/or tethers organelles, vesicles, and mRNA and protein translation machinery. Mutation of myosin Va leads to Griscelli disease that is associated with severe neurological deficits and a short life span. Despite playing a critical role in
Braz J Med Biol Res. Publicado em: 2013-02
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2. Expressão de um fragmento da Miosina Va inibe o crescimento de tumores de melanoma induzidos em modelo animal / Expression of a proapoptotic myosin Va fragment inhibits melanoma tumor growth in animal model
A miosina Va é uma proteína motora envolvida no transporte e posicionamento de vesículas, organelas e mRNA. Além disso, postulou-se que a miosina-Va atua no seqüestro do fator pró-apoptótico, Bmf, no citoesqueleto de actina. Pesquisas realizadas em nosso laboratório demonstraram que um fragmento da miosina Va (MVaf), que corresponde ao sítio ligante
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 27/01/2012
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3. Papel da Miosina Va na neuritogênese de neurônios TrkA-positivos do glânglio da raiz dorsal. / The role of Myosin Va in the neuritogenesis of dorsal root ganglia TrkA-positive neurons.
Os gânglios da raiz dorsal (GRD) armazenam neurônios TrkA-positivos. A percepção e transmissão de estímulos por estes neurônios dependem de uma neuritogênese adequada. Miosina (MioVa) é expressa no tecido nervoso e está presente em neuritos, corpo celular e cone de crescimento. Caracterizamos o padrão de expressão de MioVa na neuritogênese de c�
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 14/10/2011
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4. Differential patterns of myosin Va expression during the ontogenesis of the rat hippocampus
Myosin Va is an actin-based, processive molecular motor protein highly enriched in the nervous tissue of vertebrates. It has been associated with processes of cellular motility, which include organelle transport and neurite outgrowth. The in vivo expression of myosin Va protein in the developing nervous system of mammals has not yet been reported. We describ
Brazilian Journal of Medical and Biological Research. Publicado em: 2010-09
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5. Myosin V and iNOS expression is enhanced in J774 murine macrophages treated with IFN-gamma
Actin-based motor protein requirements and nitric oxide (NO) production are important features of macrophage activity during phagocytosis or microbicidal processes. Different classes of myosins contribute directly or indirectly to phagocytosis by providing mechanical force for phagosome closure or organelle movement. Recent data have shown the presence of my
Brazilian Journal of Medical and Biological Research. Publicado em: 2001-02
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6. Rab27a Is an Essential Component of Melanosome Receptor for Myosin Va
Melanocytes that lack the GTPase Rab27a (ashen) are disabled in myosin Va-dependent melanosome capture because the association of the myosin with the melanosome surface depends on the presence of this resident melanosomal membrane protein. One interpretation of these observations is that Rab27a functions wholly or in part as the melanosome receptor for myosi
The American Society for Cell Biology.
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7. Myosin-Va Binds to and Mechanochemically Couples Microtubules to Actin Filaments
Myosin-Va was identified as a microtubule binding protein by cosedimentation analysis in the presence of microtubules. Native myosin-Va purified from chick brain, as well as the expressed globular tail domain of this myosin, but not head domain bound to microtubule-associated protein-free microtubules. Binding of myosin-Va to microtubules was saturable and o
The American Society for Cell Biology.
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8. Myosin Va Bound to Phagosomes Binds to F-Actin and Delays Microtubule-dependent Motility
We established a light microscopy-based assay that reconstitutes the binding of phagosomes purified from mouse macrophages to preassembled F-actin in vitro. Both endogenous myosin Va from mouse macrophages and exogenous myosin Va from chicken brain stimulated the phagosome–F-actin interaction. Myosin Va association with phagosomes correlated with thei
The American Society for Cell Biology.
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9. The Actin-Binding Domain of Slac2-a/Melanophilin Is Required for Melanosome Distribution in Melanocytes
Melanosomes containing melanin pigments are transported from the cell body of melanocytes to the tips of their dendrites by a combination of microtubule- and actin-dependent machinery. Three proteins, Rab27A, myosin Va, and Slac2-a/melanophilin (a linker protein between Rab27A and myosin Va), are known to be essential for proper actin-based melanosome transp
American Society for Microbiology.
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10. Myosin-Va restrains the trafficking of Na+/K+-ATPase-containing vesicles in alveolar epithelial cells
Stimulation of Na+/K+-ATPase activity in alveolar epithelial cells by cAMP involves its recruitment from intracellular compartments to the plasma membrane. Here, we studied the role of the actin molecular motor myosin-V in this process. We provide evidence that, in alveolar epithelial cells, cAMP promotes Na+/K+-ATPase recruitment to the plasma membrane
Company of Biologists.
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11. Random Walk of Processive, Quantum Dot-Labeled Myosin Va Molecules within the Actin Cortex of COS-7 Cells
Myosin Va (myoVa) is an actin-based intracellular cargo transporter. In vitro experiments have established that a single myoVa moves processively along actin tracks, but less is known about how this motor operates within cells. Here we track the movement of a quantum dot (Qdot)-labeled myoVa HMM in COS-7 cells using total internal reflectance fluorescence m
The Biophysical Society.
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12. Myosin-Va-interacting protein, RILPL2, controls cell shape and neuronal morphogenesis via Rac signaling
Neuronal morphology plays an essential role in neuronal function. The establishment and maintenance of neuronal morphology is intimately linked to the actin cytoskeleton; however, the molecular mechanisms that regulate changes in neuronal morphology are poorly understood. Here we identify a novel myosin-Va (MyoVa)-interacting protein, RILPL2, which regul
Company of Biologists.