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Using a temperature-sensitive tropomyosin mutant to drive rapid and specific disassembly and reassembly of actin cables, the authors present strong evidence that these cables direct the myo2p-dependent transport of secretory vesicles to the bud tip, and show that actin cables respond to polarity cues independently of the overall distribution of cortical actin patches
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Pruyne D.W., Schott D.H., Bretscher A. Tropomyosin-containing actin cables direct the myo2p-dependent polarized delivery of secretory vesicles in budding yeast. J Cell Biol. 143:1998;1931-1945. Using a temperature-sensitive tropomyosin mutant to drive rapid and specific disassembly and reassembly of actin cables, the authors present strong evidence that these cables direct the myo2p-dependent transport of secretory vesicles to the bud tip, and show that actin cables respond to polarity cues independently of the overall distribution of cortical actin patches.
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Catlett N.L., Weisman L.S. The terminal tail region of a yeast myosin-V mediates its attachment to vacuole membranes and sites of polarized growth. Proc Natl Acad Sci USA. 95:1998;14799-14804. This paper provides evidence for the existence of a myo2p receptor on the vacuole membrane and at the bud tip. It indicates that the globular tail domain of myo2p contains the binding site for this 'receptor' and, in a surprising result, shows that myo2p can carry out its essential function in polarized secretion without accumulating to a significant extent at the bud tip.
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Overexpression of the myo2p tail domain is shown to result in a dominant-negative phenotype that is very similar to that of the MYO2 TS mutation myo2-66. The tail localizes to the bud tip, displacing endogenous myo2p in the process, but does not displace endogenous myo2p from a 100,000 × g pellet
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Reck-Peterson S.L., Novick P.J., Mooseker M.S. The tail of a yeast class V myosin, myo2p, functions as a localization domain. Mol Biol Cell. 10:1999;1001-1017. Overexpression of the myo2p tail domain is shown to result in a dominant-negative phenotype that is very similar to that of the MYO2 TS mutation myo2-66. The tail localizes to the bud tip, displacing endogenous myo2p in the process, but does not displace endogenous myo2p from a 100,000 × g pellet.
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Reck-Peterson, S.L.1
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Bertrand E., Chartrand P., Schaefer M., Shenoy S.M., Singer R.H., Long R.M. Localization of ASH1 mRNA particles in living yeast. Mol Cell. 2:1998;437-445. The authors have visualized the transport from mother to bud of a particle containing ASHI mRNA, and She1p and She3p (two of five gene products required for the localization of ASHI mRNA at the bud tip). Evidence is presented that She1p, which corresponds to the type V myosin myo4p, powers this transport. Some aspects of particle dynamics shed light on the polarity of actin filaments within the actin cables upon which this movement is thought to occur.
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The centrifugal transport and peripheral accumulation of melanosomes in mammalian melanocytes is shown to be driven by a cooperative process that involves fast, long-range, bidirectional, microtubule-dependent movements coupled with actomyosin-Va-dependent capture in the actin-rich periphery. Evidence is also presented for the existence of slow, local, myosin-Va-dependent melanosome movements in vivo
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Wu X., Bowers B., Rao K., Wei Q., Hammer J.A. Jr. Visualization of melanosome dynamics within wild-type and dilute melanocytes suggests a paradigm for myosin V function in vivo. J Cell Biol. 143:1998;1899-1918. The centrifugal transport and peripheral accumulation of melanosomes in mammalian melanocytes is shown to be driven by a cooperative process that involves fast, long-range, bidirectional, microtubule-dependent movements coupled with actomyosin-Va-dependent capture in the actin-rich periphery. Evidence is also presented for the existence of slow, local, myosin-Va-dependent melanosome movements in vivo.
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0032576766
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Local, actomyosin-dependent pigment granule movements occurring between the radial array of microtubules are shown to cooperate with long-range, anterograde, microtubule-dependent movements to drive the uniform cytoplasmic distribution of granules characteristic of the dispersed state in fish melanophores
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Rodionov V.I., Hope A.J., Svitkina T.M., Borisy G.G. Functional coordination of microtubule-based and actin-based motility in melanophores. Curr Biol. 8:1998;165-168. Local, actomyosin-dependent pigment granule movements occurring between the radial array of microtubules are shown to cooperate with long-range, anterograde, microtubule-dependent movements to drive the uniform cytoplasmic distribution of granules characteristic of the dispersed state in fish melanophores.
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0032576778
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This paper shows that pigment granules isolated from frog melanophores move in vitro on actin filaments as well as microtubules. The authors indirectly implicate myosin V as the responsible motor and provide evidence that the actin cytoskeleton plays a role in determining pigment granule distribution
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Rogers S.L., Gelfand V.I. Myosin cooperates with microtubule motors during organelle transport in melanophores. Curr Biol. 8:1998;161-164. This paper shows that pigment granules isolated from frog melanophores move in vitro on actin filaments as well as microtubules. The authors indirectly implicate myosin V as the responsible motor and provide evidence that the actin cytoskeleton plays a role in determining pigment granule distribution.
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Gelfand, V.I.2
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The authors provide strong evidence that myosin V is the motor responsible for pigment granule movement on actin. Evidence is presented that myosin-V-dependent granule movements are controlled by a cell cycle dependent association of the myosin with the granule, and that this association is probably regulated by phosphorylation of myosin V during mitosis
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Rogers S.L., Karcher R.L., Roland J.T., Minin A.A., Steffen W., Gelfand V.I. Regulation of melanosome movement in the cell cycle by reversible association with myosin-V. J Cell Biol. 146:1999;1265-1276. The authors provide strong evidence that myosin V is the motor responsible for pigment granule movement on actin. Evidence is presented that myosin-V-dependent granule movements are controlled by a cell cycle dependent association of the myosin with the granule, and that this association is probably regulated by phosphorylation of myosin V during mitosis.
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Rogers, S.L.1
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Transport of ER vesicles on actin filaments in neurons by myosin V
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In vitro studies described here show that tubulovesicular ER membranes isolated from extruded axoplasm of squid giant axon move on actin in vitro and, using function-blocking antibodies, that myosin V is the responsible motor. This and other data support the dual filament model of organelle transport
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Tabb J.S., Molyneaux B.J., Cohen D.L., Kuznetsov S.A., Langford G.M. Transport of ER vesicles on actin filaments in neurons by myosin V. J Cell Sci. 111:1998;3221-3234. In vitro studies described here show that tubulovesicular ER membranes isolated from extruded axoplasm of squid giant axon move on actin in vitro and, using function-blocking antibodies, that myosin V is the responsible motor. This and other data support the dual filament model of organelle transport.
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Endoplasmic reticulum is missing in dendritic spines of Purkinje cells of the ataxic mutant rat
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Visualization of myosin-Va-associated organelle movements in neuronal axons, and analysis of organelle distributions in dilute-lethal neurons, support the idea that myosin Va is often a passive passenger on organelles undergoing long-range microtubule-dependent movement. It probably functions primarily in distal, microtubule-free zones (e.g. presynaptic terminals) to distribute organelles via short range movements
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Bridgman P.C. Myosin Va movements in normal and dilute-lethal axons provide support for a dual filament motor complex. J Cell Biol. 146:1999;1045-1060. Visualization of myosin-Va-associated organelle movements in neuronal axons, and analysis of organelle distributions in dilute-lethal neurons, support the idea that myosin Va is often a passive passenger on organelles undergoing long-range microtubule-dependent movement. It probably functions primarily in distal, microtubule-free zones (e.g. presynaptic terminals) to distribute organelles via short range movements.
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Myosin V is shown to move in a processive manner and to take large steps approximating to the 36 nm psuedo-repeat of F-actin. These results represent the first demonstration that processivity exists in the myosin superfamily and provide strong support for the idea that myosin V functions as an organelle motor in vivo
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Mehta A.D., Rock R.S., Rief M., Spudich J.A., Mooseker M.S., Cheney R.E. Myosin-V is a processive actin-based motor. Nature. 400:1999;590-593. Myosin V is shown to move in a processive manner and to take large steps approximating to the 36 nm psuedo-repeat of F-actin. These results represent the first demonstration that processivity exists in the myosin superfamily and provide strong support for the idea that myosin V functions as an organelle motor in vivo.
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Rat liver myosin I and chick intestinal brush border myosin I are shown to take two steps per power stroke, one of ˜6 nm that is produced within 10 msec of actomyosin binding, and a second of ˜5.5 nm that occurs after a variable time delay. These two steps may be coupled to the release of inorganic phosphate, followed by the release of ADP
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Veigel C., Coluccio L.M., Jontes J.D., Sparrow J.C., Milligan R.A., Molloy J.E. The motor protein myosin-I produces its working stroke in two steps. Nature. 398:1999;530-533. Rat liver myosin I and chick intestinal brush border myosin I are shown to take two steps per power stroke, one of ˜6 nm that is produced within 10 msec of actomyosin binding, and a second of ˜5.5 nm that occurs after a variable time delay. These two steps may be coupled to the release of inorganic phosphate, followed by the release of ADP.
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In a truly astonishing study, the authors show that a class VI myosin moves towards the pointed end of the actin filament. Cryo-election microscopy provides a basis for understanding how reverse direction movement is accomplished by myosin VI. Sequence analyses suggest that of the 15 classes of myosin identified to date, only class VI myosins will move backwards on actin
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Wells A.L., Lin A.W., Chen L.Q., Saler D., Cain S.M., Hasson T., Carraghers B.O., Milligan R.A., Sweeney H.L. Myosin VI is an actin-based motor that moves backwards. Nature. 401:1999;505-508. In a truly astonishing study, the authors show that a class VI myosin moves towards the pointed end of the actin filament. Cryo-election microscopy provides a basis for understanding how reverse direction movement is accomplished by myosin VI. Sequence analyses suggest that of the 15 classes of myosin identified to date, only class VI myosins will move backwards on actin.
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Wells, A.L.1
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Myosin V and conventional kinesin are shown to interact directly through an association between the globular tail domain of myosin V and a small stretch of sequence in kinesin just above the light chain binding site. The results support the idea that the coordination of actin-based and microtubule-based organelle motility may operate via physical communication between different motors present in a complex on the organelle surface
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Huang J-D., Brady S.T., Richards B.W., Stenoien D., Resau J.H., Copeland N.G., Jenkins N.A. Direct interaction of microtubule- and actin-based transport motors. Nature. 397:1999;267-270. Myosin V and conventional kinesin are shown to interact directly through an association between the globular tail domain of myosin V and a small stretch of sequence in kinesin just above the light chain binding site. The results support the idea that the coordination of actin-based and microtubule-based organelle motility may operate via physical communication between different motors present in a complex on the organelle surface.
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