메뉴 건너뛰기




Volumn 12, Issue 1, 2000, Pages 42-51

Functions of unconventional myosins

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; DYNEIN ADENOSINE TRIPHOSPHATASE; MYOSIN;

EID: 0033969154     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(99)00055-1     Document Type: Review
Times cited : (104)

References (108)
  • 2
    • 0032559349 scopus 로고    scopus 로고
    • Unconventional myosins in cell movement, membrane traffic, and signal transduction
    • Mermall V., Post P.L., Mooseker M.S. Unconventional myosins in cell movement, membrane traffic, and signal transduction. Science. 279:1998;527-533.
    • (1998) Science , vol.279 , pp. 527-533
    • Mermall, V.1    Post, P.L.2    Mooseker, M.S.3
  • 3
  • 4
    • 0028902506 scopus 로고
    • The role of myo2, a yeast class V myosin, in vesicular transport
    • Govindan B., Bowser R., Novick P. The role of myo2, a yeast class V myosin, in vesicular transport. J Cell Biol. 128:1995;1055-1068.
    • (1995) J Cell Biol , vol.128 , pp. 1055-1068
    • Govindan, B.1    Bowser, R.2    Novick, P.3
  • 6
    • 0032576569 scopus 로고    scopus 로고
    • Tropomyosin-containing actin cables direct the myo2p-dependent polarized delivery of secretory vesicles in budding yeast
    • 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
    • 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.
    • (1998) J Cell Biol , vol.143 , pp. 1931-1945
    • Pruyne, D.W.1    Schott, D.H.2    Bretscher, A.3
  • 7
    • 0032426664 scopus 로고    scopus 로고
    • The terminal tail region of a yeast myosin-V mediates its attachment to vacuole membranes and sites of polarized growth
    • 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
    • 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.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 14799-14804
    • Catlett, N.L.1    Weisman, L.S.2
  • 8
    • 0032915418 scopus 로고    scopus 로고
    • The tail of a yeast class V myosin, myo2p, functions as a localization domain
    • 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
    • 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.
    • (1999) Mol Biol Cell , vol.10 , pp. 1001-1017
    • Reck-Peterson, S.L.1    Novick, P.J.2    Mooseker, M.S.3
  • 9
    • 0031822156 scopus 로고    scopus 로고
    • Mlc1p is a light chain for the unconventional myosin myo2p in Saccharomyces cerevisiae
    • Stevens R.C., Davis T.N. Mlc1p is a light chain for the unconventional myosin myo2p in Saccharomyces cerevisiae. J Cell Biol. 142:1998;711-722.
    • (1998) J Cell Biol , vol.142 , pp. 711-722
    • Stevens, R.C.1    Davis, T.N.2
  • 10
    • 0030978526 scopus 로고    scopus 로고
    • High rates of actin filament turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A
    • Ayscough K.R., Stryker J., Pokala N., Sanders M., Crews P., Drubin D.G. High rates of actin filament turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A. J Cell Biol. 2:1997;399-416.
    • (1997) J Cell Biol , vol.2 , pp. 399-416
    • Ayscough, K.R.1    Stryker, J.2    Pokala, N.3    Sanders, M.4    Crews, P.5    Drubin, D.G.6
  • 11
    • 0032538297 scopus 로고    scopus 로고
    • Motors driving mRNA localization: New insights from in vivo imaging
    • Arn E.A., Macdonald P.M. Motors driving mRNA localization: new insights from in vivo imaging. Cell. 95:1998;151-154.
    • (1998) Cell , vol.95 , pp. 151-154
    • Arn, E.A.1    Macdonald, P.M.2
  • 12
    • 0032185810 scopus 로고    scopus 로고
    • Localization of ASH1 mRNA particles in living yeast
    • 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
    • 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.
    • (1998) Mol Cell , vol.2 , pp. 437-445
    • Bertrand, E.1    Chartrand, P.2    Schaefer, M.3    Shenoy, S.M.4    Singer, R.H.5    Long, R.M.6
  • 13
    • 0344780902 scopus 로고    scopus 로고
    • Association of the class V myosin Myo4p with a localised messenger RNA in budding yeast depends on She proteins
    • Mönchow S., Sauter C., Jansen R-P. Association of the class V myosin Myo4p with a localised messenger RNA in budding yeast depends on She proteins. J Cell Sci. 112:1999;1511-1518.
    • (1999) J Cell Sci , vol.112 , pp. 1511-1518
    • Mönchow, S.1    Sauter, C.2    Jansen, R.-P.3
  • 14
    • 0028942256 scopus 로고
    • Actin- And microtubule-dependent organelle motors: Interrelationships between the two motility systems
    • Langford G.M. Actin- and microtubule-dependent organelle motors: interrelationships between the two motility systems. Curr Opin Cell Biol. 7:1995;82-88.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 82-88
    • Langford, G.M.1
  • 15
    • 0033280225 scopus 로고    scopus 로고
    • Cooperation between microtubule- And actin-based motor proteins
    • in press
    • Brown S.S. Cooperation between microtubule- and actin-based motor proteins. Annu Rev Cell Dev Biol. 1999;. in press.
    • (1999) Annu Rev Cell Dev Biol
    • Brown, S.S.1
  • 16
    • 0032559708 scopus 로고    scopus 로고
    • Cruising along microtubule highways: How membranes move through the secretory pathway
    • Bloom G.S., Goldstein S.B. Cruising along microtubule highways: how membranes move through the secretory pathway. J Cell Biol. 140:1998;1277-1280.
    • (1998) J Cell Biol , vol.140 , pp. 1277-1280
    • Bloom, G.S.1    Goldstein, S.B.2
  • 17
    • 0032554788 scopus 로고    scopus 로고
    • Intracellular motility: How can we all work together?
    • Kelleher J.F., Titus M.A. Intracellular motility: how can we all work together? Curr Biol. 8:1998;304-397.
    • (1998) Curr Biol , vol.8 , pp. 304-397
    • Kelleher, J.F.1    Titus, M.A.2
  • 18
    • 0032576622 scopus 로고    scopus 로고
    • Visualization of melanosome dynamics within wild-type and dilute melanocytes suggests a paradigm for myosin V function in vivo
    • 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
    • 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.
    • (1998) J Cell Biol , vol.143 , pp. 1899-1918
    • Wu, X.1    Bowers, B.2    Rao, K.3    Wei, Q.4    Hammer, J.A.5
  • 19
    • 0028079158 scopus 로고
    • Regulation of organelle transport: Lessons from color change in fish
    • Haimo L.T., Thaler C.D. Regulation of organelle transport: lessons from color change in fish. Bioessays. 16:1994;727-733.
    • (1994) Bioessays , vol.16 , pp. 727-733
    • Haimo, L.T.1    Thaler, C.D.2
  • 20
    • 0032576766 scopus 로고    scopus 로고
    • Functional coordination of microtubule-based and actin-based motility in melanophores
    • 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
    • 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.
    • (1998) Curr Biol , vol.8 , pp. 165-168
    • Rodionov, V.I.1    Hope, A.J.2    Svitkina, T.M.3    Borisy, G.G.4
  • 21
    • 0032576778 scopus 로고    scopus 로고
    • Myosin cooperates with microtubule motors during organelle transport in melanophores
    • 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
    • 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.
    • (1998) Curr Biol , vol.8 , pp. 161-164
    • Rogers, S.L.1    Gelfand, V.I.2
  • 22
    • 0033588979 scopus 로고    scopus 로고
    • Regulation of melanosome movement in the cell cycle by reversible association with myosin-V
    • 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
    • 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.
    • (1999) J Cell Biol , vol.146 , pp. 1265-1276
    • Rogers, S.L.1    Karcher, R.L.2    Roland, J.T.3    Minin, A.A.4    Steffen, W.5    Gelfand, V.I.6
  • 23
    • 0026534466 scopus 로고
    • Actin-dependent organelle movement in squid axoplasm
    • Kuznetsov S.A., Langford G.M., Weiss D.G. Actin-dependent organelle movement in squid axoplasm. Nature. 356:1992;722-725.
    • (1992) Nature , vol.356 , pp. 722-725
    • Kuznetsov, S.A.1    Langford, G.M.2    Weiss, D.G.3
  • 24
    • 0031784059 scopus 로고    scopus 로고
    • Transport of ER vesicles on actin filaments in neurons by myosin V
    • 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
    • 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.
    • (1998) J Cell Sci , vol.111 , pp. 3221-3234
    • Tabb, J.S.1    Molyneaux, B.J.2    Cohen, D.L.3    Kuznetsov, S.A.4    Langford, G.M.5
  • 26
    • 0031819385 scopus 로고    scopus 로고
    • Vesicle-associated brain myosin-V can be activated to catalyze actin-based transport
    • Evans L.L., Lee A.J., Bridgman P.C., Mooseker M.S. Vesicle-associated brain myosin-V can be activated to catalyze actin-based transport. J Cell Sci. 111:1998;2055-2066.
    • (1998) J Cell Sci , vol.111 , pp. 2055-2066
    • Evans, L.L.1    Lee, A.J.2    Bridgman, P.C.3    Mooseker, M.S.4
  • 27
    • 0032872611 scopus 로고    scopus 로고
    • Myosin Va movements in normal and dilute-lethal axons provide support for a dual filament motor complex
    • 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
    • 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.
    • (1999) J Cell Biol , vol.146 , pp. 1045-1060
    • Bridgman, P.C.1
  • 29
    • 0033527043 scopus 로고    scopus 로고
    • Myosin-V is a processive actin-based motor
    • 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
    • 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.
    • (1999) Nature , vol.400 , pp. 590-593
    • Mehta, A.D.1    Rock, R.S.2    Rief, M.3    Spudich, J.A.4    Mooseker, M.S.5    Cheney, R.E.6
  • 30
    • 0033535556 scopus 로고    scopus 로고
    • The motor protein myosin-I produces its working stroke in two steps
    • 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
    • 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.
    • (1999) Nature , vol.398 , pp. 530-533
    • Veigel, C.1    Coluccio, L.M.2    Jontes, J.D.3    Sparrow, J.C.4    Milligan, R.A.5    Molloy, J.E.6
  • 31
    • 0033618274 scopus 로고    scopus 로고
    • Transient kinetic analysis of the 130 kDa myosin I (MYR-1 gene product) from rat liver
    • Coluccio L.M., Geeves M.A. Transient kinetic analysis of the 130 kDa myosin I (MYR-1 gene product) from rat liver. J Biol Chem. 274:1999;21575-21580.
    • (1999) J Biol Chem , vol.274 , pp. 21575-21580
    • Coluccio, L.M.1    Geeves, M.A.2
  • 32
    • 0033619258 scopus 로고    scopus 로고
    • Myosin VI is an actin-based motor that moves backwards
    • 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
    • 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.
    • (1999) Nature , vol.401 , pp. 505-508
    • Wells, A.L.1    Lin, A.W.2    Chen, L.Q.3    Saler, D.4    Cain, S.M.5    Hasson, T.6    Carraghers, B.O.7    Milligan, R.A.8    Sweeney, H.L.9
  • 33
    • 0028359778 scopus 로고
    • Transport of cytoplasmic particles by an unconventional myosin in living Drosophila embryos
    • Mermall V., McNally J.G., Miller K.G. Transport of cytoplasmic particles by an unconventional myosin in living Drosophila embryos. Nature. 369:1994;560-562.
    • (1994) Nature , vol.369 , pp. 560-562
    • Mermall, V.1    McNally, J.G.2    Miller, K.G.3
  • 34
    • 0032517817 scopus 로고    scopus 로고
    • The localization of myosin VI at the Golgi complex and leading edge of fibroblasts and its phosphorylation and recruitment into membrane ruffles of A431 cells after growth factor stimulation
    • Buss F., Kendrick-Jones J., Lionne C., Knight A.E., Côté G.P., Luzio J.P. The localization of myosin VI at the Golgi complex and leading edge of fibroblasts and its phosphorylation and recruitment into membrane ruffles of A431 cells after growth factor stimulation. J Cell Biol. 143:1998;1535-1545.
    • (1998) J Cell Biol , vol.143 , pp. 1535-1545
    • Buss, F.1    Kendrick-Jones, J.2    Lionne, C.3    Knight, A.E.4    Côté, G.P.5    Luzio, J.P.6
  • 35
    • 0027993176 scopus 로고
    • Porcine myosin VI: Characterization of a new mammalian unconventional myosin
    • Hasson T., Mooseker M.S. Porcine myosin VI: characterization of a new mammalian unconventional myosin. J Cell Biol. 127:1994;425-440.
    • (1994) J Cell Biol , vol.127 , pp. 425-440
    • Hasson, T.1    Mooseker, M.S.2
  • 36
    • 0030924142 scopus 로고    scopus 로고
    • Reversal in the direction of movement of a molecular motor
    • Henningsen U., Schliwa M. Reversal in the direction of movement of a molecular motor. Nature. 389:1997;93-96.
    • (1997) Nature , vol.389 , pp. 93-96
    • Henningsen, U.1    Schliwa, M.2
  • 37
    • 0033590558 scopus 로고    scopus 로고
    • Direct interaction of microtubule- And actin-based transport motors
    • 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
    • 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.
    • (1999) Nature , vol.397 , pp. 267-270
    • Huang, J.-D.1    Brady, S.T.2    Richards, B.W.3    Stenoien, D.4    Resau, J.H.5    Copeland, N.G.6    Jenkins, N.A.7
  • 38
    • 0026539415 scopus 로고
    • Suppression of a myosin defect by a kinesin-related gene
    • Lillie S.H., Brown S.S. Suppression of a myosin defect by a kinesin-related gene. Nature. 356:1992;358-361.
    • (1992) Nature , vol.356 , pp. 358-361
    • Lillie, S.H.1    Brown, S.S.2
  • 39
    • 0032559545 scopus 로고    scopus 로고
    • Smy1p, a kinesin-related protein that does not require microtubules
    • The ability of the kinesin related protein smy1p to partially suppress the phenotype of a myo2p TS mutant is shown to not require microtubules or smy1p motor function. These and other data indicate that smy1p does not act as a microtubule motor to localize or rescue defective myo2p but rather in some novel way, such as stabilizing/enhancing myo2p function through a direct physical interaction
    • Lillie S.H., Brown S.S. Smy1p, a kinesin-related protein that does not require microtubules. J Cell Biol. 4:1998;873-883. The ability of the kinesin related protein smy1p to partially suppress the phenotype of a myo2p TS mutant is shown to not require microtubules or smy1p motor function. These and other data indicate that smy1p does not act as a microtubule motor to localize or rescue defective myo2p but rather in some novel way, such as stabilizing/enhancing myo2p function through a direct physical interaction.
    • (1998) J Cell Biol , vol.4 , pp. 873-883
    • Lillie, S.H.1    Brown, S.S.2
  • 40
    • 0030861056 scopus 로고    scopus 로고
    • Dimerization of the highly conserved light chain shared by dynein and myosin, V
    • Benashski S.E., Harrison A., Patel-King R.S., King S.M. Dimerization of the highly conserved light chain shared by dynein and myosin, V. J Biol Chem. 272:1997;20929-20935.
    • (1997) J Biol Chem , vol.272 , pp. 20929-20935
    • Benashski, S.E.1    Harrison, A.2    Patel-King, R.S.3    King, S.M.4
  • 41
    • 0032559641 scopus 로고    scopus 로고
    • A class VI unconventional myosin is associated with a homologue of a microtubule-binding protein, cytoplasmic linker protein-170, in neurons and at the posterior pole of Drosophila embryos
    • Drosophila myosin VI is shown to interact physically with a Drosophila homolog of CLIP-170, DCLIP-190, and to colocalize with DCLIP-190. These results reveal another potential mechanism for linking and coordinating actin- and microtubule-dependent organelle movements
    • Lantz V.A., Miller K.G. A class VI unconventional myosin is associated with a homologue of a microtubule-binding protein, cytoplasmic linker protein-170, in neurons and at the posterior pole of Drosophila embryos. J Cell Biol. 140:1998;897-910. Drosophila myosin VI is shown to interact physically with a Drosophila homolog of CLIP-170, DCLIP-190, and to colocalize with DCLIP-190. These results reveal another potential mechanism for linking and coordinating actin- and microtubule-dependent organelle movements.
    • (1998) J Cell Biol , vol.140 , pp. 897-910
    • Lantz, V.A.1    Miller, K.G.2
  • 42
    • 0033582659 scopus 로고    scopus 로고
    • CLIP-170 highlights growing microtubule ends in vivo
    • Perez F., Diamantopoulos G.S., Stalder R., Kreis T.E. CLIP-170 highlights growing microtubule ends in vivo. Cell. 96:1999;517-527.
    • (1999) Cell , vol.96 , pp. 517-527
    • Perez, F.1    Diamantopoulos, G.S.2    Stalder, R.3    Kreis, T.E.4
  • 43
    • 0033051741 scopus 로고    scopus 로고
    • Colocalization of cytoplasmic dynein with dynactin and CLIP-170 at microtubule distal ends
    • Vaughan K.T., Tynan S.H., Faulkner N.E., Echeverri C.J., Vallee R.B. Colocalization of cytoplasmic dynein with dynactin and CLIP-170 at microtubule distal ends. J Cell Sci. 112:1999;1437-1447.
    • (1999) J Cell Sci , vol.112 , pp. 1437-1447
    • Vaughan, K.T.1    Tynan, S.H.2    Faulkner, N.E.3    Echeverri, C.J.4    Vallee, R.B.5
  • 44
    • 0026793891 scopus 로고
    • CLIP-170 links endocytic vesicles to microtubules
    • Pierre P., Scheel J., Rickard J.E., Kreis T.E. CLIP-170 links endocytic vesicles to microtubules. Cell. 70:1992;887-900.
    • (1992) Cell , vol.70 , pp. 887-900
    • Pierre, P.1    Scheel, J.2    Rickard, J.E.3    Kreis, T.E.4
  • 47
    • 0033563024 scopus 로고    scopus 로고
    • Motor and cargo interactions
    • Sheetz M.P. Motor and cargo interactions. Eur J Biochem. 262:1999;19-25.
    • (1999) Eur J Biochem , vol.262 , pp. 19-25
    • Sheetz, M.P.1
  • 48
    • 0030964893 scopus 로고    scopus 로고
    • Myosin V associates with melanosomes in mouse melanocytes: Evidence that myosin V is an organelle motor
    • Wu X., Bowers B., Wei Q., Kocher B., Hammer J.A. Jr. Myosin V associates with melanosomes in mouse melanocytes: evidence that myosin V is an organelle motor. J Cell Sci. 110:1997;847-859.
    • (1997) J Cell Sci , vol.110 , pp. 847-859
    • Wu, X.1    Bowers, B.2    Wei, Q.3    Kocher, B.4    Hammer, J.A.5
  • 49
    • 0030822624 scopus 로고    scopus 로고
    • Subcellular localization of myosin-V in the B16 melanoma cells, a wild-type cell line for the dilute gene
    • Nascimento A.A.C., Amaral R.G., Bizario J.C.S., Larson R.E., Espreafico E.M. Subcellular localization of myosin-V in the B16 melanoma cells, a wild-type cell line for the dilute gene. Mol Biol Cell. 8:1997;1971-1988.
    • (1997) Mol Biol Cell , vol.8 , pp. 1971-1988
    • Nascimento, A.A.C.1    Amaral, R.G.2    Bizario, J.C.S.3    Larson, R.E.4    Espreafico, E.M.5
  • 50
    • 0031737659 scopus 로고    scopus 로고
    • Myosin V colocalizes with melanosomes and subcortical actin bundles not associated with stress fibers in human epidermal melanocytes
    • Lambert J., Onderwater J., Haeghen Y.V., Vancoillie G., Koerten H.K., Mommaas A.M., Naeyaert J.M. Myosin V colocalizes with melanosomes and subcortical actin bundles not associated with stress fibers in human epidermal melanocytes. J Invest Dermatol. 111:1998;835-840.
    • (1998) J Invest Dermatol , vol.111 , pp. 835-840
    • Lambert, J.1    Onderwater, J.2    Haeghen, Y.V.3    Vancoillie, G.4    Koerten, H.K.5    Mommaas, A.M.6    Naeyaert, J.M.7
  • 51
    • 0028352176 scopus 로고
    • Immunofluorescence localization of the unconventional myosin, Myo2p, and the putative kinesin-related protein, Smy1p, to the same regions of polarized growth in Saccharomyces cerevisiae
    • Lillie S.H., Brown S.S. Immunofluorescence localization of the unconventional myosin, Myo2p, and the putative kinesin-related protein, Smy1p, to the same regions of polarized growth in Saccharomyces cerevisiae. J Cell Biol. 125:1994;825-842.
    • (1994) J Cell Biol , vol.125 , pp. 825-842
    • Lillie, S.H.1    Brown, S.S.2
  • 54
    • 0031748734 scopus 로고    scopus 로고
    • Myosin Va associates with microtubule-rich domains in both interphase and dividing cells
    • Wu X., Kocher B., Wei Q., Hammer J.A. Myosin Va associates with microtubule-rich domains in both interphase and dividing cells. Cell Motil Cytoskeleton. 40:1998;286-303.
    • (1998) Cell Motil Cytoskeleton , vol.40 , pp. 286-303
    • Wu, X.1    Kocher, B.2    Wei, Q.3    Hammer, J.A.4
  • 55
    • 0032985891 scopus 로고    scopus 로고
    • Brain myosin-V, a calmodulin-carrying myosin, binds to calmodulin-dependent protein kinase II and activates its kinase activity
    • Costa M.C.R., Mani F., Santoro W., Espreafico E.M., Larson R.E. Brain myosin-V, a calmodulin-carrying myosin, binds to calmodulin-dependent protein kinase II and activates its kinase activity. J Biol Chem. 274:1999;15811-15819.
    • (1999) J Biol Chem , vol.274 , pp. 15811-15819
    • Costa, M.C.R.1    Mani, F.2    Santoro, W.3    Espreafico, E.M.4    Larson, R.E.5
  • 56
    • 0033538519 scopus 로고    scopus 로고
    • Cloning and characterization of a novel RING finger protein that interacts with class V myosins
    • El-Husseini A.E-d., Vincent S.R. Cloning and characterization of a novel RING finger protein that interacts with class V myosins. J Biol Chem. 274:1999;19771-19777.
    • (1999) J Biol Chem , vol.274 , pp. 19771-19777
    • El-Husseini, A.E.-D.1    Vincent, S.R.2
  • 57
    • 0030470182 scopus 로고    scopus 로고
    • Actin and myosin function in directed vacuole movement during cell division in Saccharomyces cerevisiae
    • Hill K.L., Catlett N.L., Weisman L.S. Actin and myosin function in directed vacuole movement during cell division in Saccharomyces cerevisiae. J Cell Biol. 135:1996;1535-1549.
    • (1996) J Cell Biol , vol.135 , pp. 1535-1549
    • Hill, K.L.1    Catlett, N.L.2    Weisman, L.S.3
  • 58
    • 0029954709 scopus 로고    scopus 로고
    • Cell cycle regulation of dynein association with membranes modulates microtubule-based organelle transport
    • Niclas J., Allan V.J., Vale R.D. Cell cycle regulation of dynein association with membranes modulates microtubule-based organelle transport. J Cell Biol. 133:1996;585-593.
    • (1996) J Cell Biol , vol.133 , pp. 585-593
    • Niclas, J.1    Allan, V.J.2    Vale, R.D.3
  • 59
    • 0029006373 scopus 로고
    • TEDS rule: A molecular rationale for differential regulation of myosins by phosphorylation of the heavy chain head
    • Bement W.M., Mooseker M.S. TEDS rule: a molecular rationale for differential regulation of myosins by phosphorylation of the heavy chain head. Cell Motil Cytoskeleton. 31:1995;87-92.
    • (1995) Cell Motil Cytoskeleton , vol.31 , pp. 87-92
    • Bement, W.M.1    Mooseker, M.S.2
  • 60
    • 0030054719 scopus 로고    scopus 로고
    • Regulation of class I and class II myosins by heavy chain phosphorylation
    • Brzeska H., Korn E.D. Regulation of class I and class II myosins by heavy chain phosphorylation. J Biol Chem. 271:1996;16983-16986.
    • (1996) J Biol Chem , vol.271 , pp. 16983-16986
    • Brzeska, H.1    Korn, E.D.2
  • 61
    • 0032442353 scopus 로고    scopus 로고
    • Analysis of the regulatory phosphorylation site in Acanthamoeba myosin IC by using site-directed mutagenesis
    • Wang Z-Y., Wang F., Sellers J.R., Korn E.D., Hammer J.A. Jr. Analysis of the regulatory phosphorylation site in Acanthamoeba myosin IC by using site-directed mutagenesis. Proc Natl Acad Sci USA. 95:1998;15200-15205.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 15200-15205
    • Wang, Z.-Y.1    Wang, F.2    Sellers, J.R.3    Korn, E.D.4    Hammer, J.A.5
  • 63
    • 0029991890 scopus 로고    scopus 로고
    • Human myosin-1Xb, an unconventional myosin with a chimerin-like rho/rac GTPase-activating protein domain in its tail
    • Wirth J.A., Jensen K.A., Post P.L., Bement W.M., Mooseker M.S. Human myosin-1Xb, an unconventional myosin with a chimerin-like rho/rac GTPase-activating protein domain in its tail. J Cell Sci. 109:1996;653-661.
    • (1996) J Cell Sci , vol.109 , pp. 653-661
    • Wirth, J.A.1    Jensen, K.A.2    Post, P.L.3    Bement, W.M.4    Mooseker, M.S.5
  • 64
    • 0031977198 scopus 로고    scopus 로고
    • Human myosin-IXb is a mechanochemically active motor and a GAP for rho
    • Post P.L., Bokoch G.M., Mooseker M.S. Human myosin-IXb is a mechanochemically active motor and a GAP for rho. J Cell Sci. 111:1998;941-950.
    • (1998) J Cell Sci , vol.111 , pp. 941-950
    • Post, P.L.1    Bokoch, G.M.2    Mooseker, M.S.3
  • 65
    • 0031042493 scopus 로고    scopus 로고
    • Rho, rac, cdc42 GTPases regulate the organization of the actin cytoskeleton
    • Tapon N., Hall A. Rho, rac, cdc42 GTPases regulate the organization of the actin cytoskeleton. Curr Opin Cell Biol. 9:1997;86-92.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 86-92
    • Tapon, N.1    Hall, A.2
  • 66
    • 0039521743 scopus 로고    scopus 로고
    • The rat myosin myr 5 is a GTPase activating protein for rho in vivo. Essential role of arginine 1695
    • Müller R.T., Honnert U., Reinhard J., Bähler M. The rat myosin myr 5 is a GTPase activating protein for rho in vivo. Essential role of arginine 1695. Mol Biol Cell. 8:1997;2039-2053.
    • (1997) Mol Biol Cell , vol.8 , pp. 2039-2053
    • Müller, R.T.1    Honnert, U.2    Reinhard, J.3    Bähler, M.4
  • 68
    • 0008467934 scopus 로고    scopus 로고
    • Molecular links between rho family GTPases and myosins
    • H. Maruta, & K. Kohama. Austin, Texas: RG Landes Company
    • Hammer J.A. Jr., Côté G.P. Molecular links between rho family GTPases and myosins. Maruta H., Kohama K. G Proteins, Cytoskeleton and Cancer. 1998;37-52 RG Landes Company, Austin, Texas.
    • (1998) G Proteins, Cytoskeleton and Cancer , pp. 37-52
    • Hammer, J.A.1    Côté, G.P.2
  • 69
    • 0032526679 scopus 로고    scopus 로고
    • The Src homology domain 3 (SH3) of a yeast type I myosin, myo5p, binds to verprolin and is required for targeting to sites of actin polarization
    • In vivo structure/function analyses of the type I myosin myo5p indicate that its SH3 domain is required for localization of myo5p patches to sites of polarized growth, and for myo5p to exert its full effects on the integrity of the actin cytoskeleton. The proline-rich protein verprolin (Vrp1p), which plays an important role early in polarity establishment, interacts with myo5p via its SH3 domain, and myo5p patches are depolarized in VRPI deletion strains. Therefore, although myo5p patch assembly does not require Vrp1p-myo5p interaction, localization of these patches to sites of polarized growth does. The authors suggest that Vrp1p serves as a scaffold to bind and concentrate myo5p patches in the bud
    • Anderson B.L., Boldogh I., Evangelista M., Boone C., Greene L.A., Pon L.A. The Src homology domain 3 (SH3) of a yeast type I myosin, myo5p, binds to verprolin and is required for targeting to sites of actin polarization. J Cell Biol. 141:1998;1357-1370. In vivo structure/function analyses of the type I myosin myo5p indicate that its SH3 domain is required for localization of myo5p patches to sites of polarized growth, and for myo5p to exert its full effects on the integrity of the actin cytoskeleton. The proline-rich protein verprolin (Vrp1p), which plays an important role early in polarity establishment, interacts with myo5p via its SH3 domain, and myo5p patches are depolarized in VRPI deletion strains. Therefore, although myo5p patch assembly does not require Vrp1p-myo5p interaction, localization of these patches to sites of polarized growth does. The authors suggest that Vrp1p serves as a scaffold to bind and concentrate myo5p patches in the bud.
    • (1998) J Cell Biol , vol.141 , pp. 1357-1370
    • Anderson, B.L.1    Boldogh, I.2    Evangelista, M.3    Boone, C.4    Greene, L.A.5    Pon, L.A.6
  • 70
    • 0031416482 scopus 로고    scopus 로고
    • Actin-binding verprolin is a polarity development protein required for the morphogenesis and function of the yeast actin cytoskeleton
    • Vaduva G., Martin N.C., Hopper A.K. Actin-binding verprolin is a polarity development protein required for the morphogenesis and function of the yeast actin cytoskeleton. J Cell Biol. 139:1997;1821-1833.
    • (1997) J Cell Biol , vol.139 , pp. 1821-1833
    • Vaduva, G.1    Martin, N.C.2    Hopper, A.K.3
  • 71
    • 0032572759 scopus 로고    scopus 로고
    • The WASP homologue Las17p functions with the WIP homologue end5p/verprolin and is essential for endocytosis in yeast
    • Naqvi S.N., Zahn R., Mitchell D.A., Stevenson B.J., Munn A.L. The WASP homologue Las17p functions with the WIP homologue end5p/verprolin and is essential for endocytosis in yeast. Curr Biol. 8:1998;959-962.
    • (1998) Curr Biol , vol.8 , pp. 959-962
    • Naqvi, S.N.1    Zahn, R.2    Mitchell, D.A.3    Stevenson, B.J.4    Munn, A.L.5
  • 72
    • 0033528995 scopus 로고    scopus 로고
    • Activation of the yeast Arp2/3 complex by Bee1p, a WASP-family protein
    • Winter D., Lechler T., Li R. Activation of the yeast Arp2/3 complex by Bee1p, a WASP-family protein. Curr Biol. 9:1999;501-504.
    • (1999) Curr Biol , vol.9 , pp. 501-504
    • Winter, D.1    Lechler, T.2    Li, R.3
  • 73
    • 0032585538 scopus 로고    scopus 로고
    • Scar1 and the related Wiskott Aldrich syndrome protein WASP regulate the actin cytoskeleton through the Arp2/3 complex
    • Machesky L.M., Insall R.H. Scar1 and the related Wiskott Aldrich syndrome protein WASP regulate the actin cytoskeleton through the Arp2/3 complex. Curr Biol. 8:1998;1347-1356.
    • (1998) Curr Biol , vol.8 , pp. 1347-1356
    • Machesky, L.M.1    Insall, R.H.2
  • 74
    • 0033606788 scopus 로고    scopus 로고
    • Signaling to actin dynamics
    • Machesky L.M., Insall R.H. Signaling to actin dynamics. J Cell Biol. 146:1999;267-272.
    • (1999) J Cell Biol , vol.146 , pp. 267-272
    • Machesky, L.M.1    Insall, R.H.2
  • 75
    • 0031933790 scopus 로고    scopus 로고
    • The myosin I SH3 domain and TEDS rule phosphorylation site are required for in vivo function
    • Novak D.K., Titus M.A. The myosin I SH3 domain and TEDS rule phosphorylation site are required for in vivo function. Mol Biol Cell. 9:1998;75-88.
    • (1998) Mol Biol Cell , vol.9 , pp. 75-88
    • Novak, D.K.1    Titus, M.A.2
  • 76
    • 0028930161 scopus 로고
    • A novel mammalian myosin I from rat with an SH3 domain localizes to ConA-inducible, F-actin-rich structures at cell-cell contacts
    • Stöffler H-E., Ruppert C., Reinhard J., Bähler M. A novel mammalian myosin I from rat with an SH3 domain localizes to ConA-inducible, F-actin-rich structures at cell-cell contacts. J Cell Biol. 129:1995;819-830.
    • (1995) J Cell Biol , vol.129 , pp. 819-830
    • Stöffler, H.-E.1    Ruppert, C.2    Reinhard, J.3    Bähler, M.4
  • 77
    • 0032459354 scopus 로고    scopus 로고
    • Human brush border myosin-I and myosin-Ic expression in human intestine and Caco-2BBe Cells
    • Skowron J.F., Bement W.M., Mooseker M.S. Human brush border myosin-I and myosin-Ic expression in human intestine and Caco-2BBe Cells. Cell Motil Cytoskeleton. 41:1998;308-324.
    • (1998) Cell Motil Cytoskeleton , vol.41 , pp. 308-324
    • Skowron, J.F.1    Bement, W.M.2    Mooseker, M.S.3
  • 78
    • 0031446340 scopus 로고    scopus 로고
    • WIP, a protein associated with Wiskott-Aldrich syndrome protein, induces actin polymerization and redistribution in lymphoid cells
    • Ramesh N., Anton I.M., Hartwig J.H., Geha R.S. WIP, a protein associated with Wiskott-Aldrich syndrome protein, induces actin polymerization and redistribution in lymphoid cells. Proc Natl Acad Sci USA. 94:1997;14671-14676.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 14671-14676
    • Ramesh, N.1    Anton, I.M.2    Hartwig, J.H.3    Geha, R.S.4
  • 79
    • 0030846814 scopus 로고    scopus 로고
    • Unconventional myosins, the basis for deafness in mouse and man
    • Hasson T. Unconventional myosins, the basis for deafness in mouse and man. Amer J Hum Genet. 61:1997;801-805.
    • (1997) Amer J Hum Genet , vol.61 , pp. 801-805
    • Hasson, T.1
  • 83
    • 0031594148 scopus 로고    scopus 로고
    • Immunolocalization of myosin Iβ in the hair cell's hair bundle
    • Metcalf A.B. Immunolocalization of myosin Iβ in the hair cell's hair bundle. Cell Motil Cytoskeleton. 39:1998;159-165.
    • (1998) Cell Motil Cytoskeleton , vol.39 , pp. 159-165
    • Metcalf, A.B.1
  • 84
    • 0032194948 scopus 로고    scopus 로고
    • Localization of myosin-1β near both ends of tip links in frog saccular hair cells
    • Using quantitative immunoelectron microscopy, the authors show in this careful study that myosin Iβ is concentrated at both the side plaques and tip plaques, supporting its role as the adaptation motor
    • Garcia J.A., Yee A.G., Gillespie P.G., Corey D.P. Localization of myosin-1β near both ends of tip links in frog saccular hair cells. J Neurosci. 18:1998;8637-8647. Using quantitative immunoelectron microscopy, the authors show in this careful study that myosin Iβ is concentrated at both the side plaques and tip plaques, supporting its role as the adaptation motor.
    • (1998) J Neurosci , vol.18 , pp. 8637-8647
    • Garcia, J.A.1    Yee, A.G.2    Gillespie, P.G.3    Corey, D.P.4
  • 86
    • 17644442703 scopus 로고    scopus 로고
    • Correction of deafness in shaker-2 mice by an unconventional myosin in a BAC transgene
    • The auditory hair cells from shaker-2 mice are shown to exhibit very short stereocilia and an abnormal actin-containing basal projection. These structural defects, as well as the vestibular defects and deafness exhibited by shaker-2 mice, are corrected by a BAC (bacterial artificial chromosome) transgene encoding myosin XV. The myosin VX gene in shaker-2 mice is shown to encode an amino acid substitution at a highly conserved site in the motor domain
    • Probst F.J., Fridell R.A., Raphael Y., Saunders T.L., Wang A., Liang Y., Morell R.J., Touchman J.W., Lyons R.H., Nobenn-Trauth K.et al. Correction of deafness in shaker-2 mice by an unconventional myosin in a BAC transgene. Science. 280:1998;1444-1447. The auditory hair cells from shaker-2 mice are shown to exhibit very short stereocilia and an abnormal actin-containing basal projection. These structural defects, as well as the vestibular defects and deafness exhibited by shaker-2 mice, are corrected by a BAC (bacterial artificial chromosome) transgene encoding myosin XV. The myosin VX gene in shaker-2 mice is shown to encode an amino acid substitution at a highly conserved site in the motor domain.
    • (1998) Science , vol.280 , pp. 1444-1447
    • Probst, F.J.1    Fridell, R.A.2    Raphael, Y.3    Saunders, T.L.4    Wang, A.5    Liang, Y.6    Morell, R.J.7    Touchman, J.W.8    Lyons, R.H.9    Nobenn-Trauth, K.10
  • 89
    • 0032085412 scopus 로고    scopus 로고
    • Mutant myosin VII causes defective melanosome distribution in the RPE of shaker-1 mice
    • Liu X., Ondek B., Williams D.S. Mutant myosin VII causes defective melanosome distribution in the RPE of shaker-1 mice. Nat Genet. 19:1998;117-118.
    • (1998) Nat Genet , vol.19 , pp. 117-118
    • Liu, X.1    Ondek, B.2    Williams, D.S.3
  • 90
    • 0033178341 scopus 로고    scopus 로고
    • Myosin VIIa participates in opsin transport through the photoreceptor cilium
    • Immunoelectron microscopy and microscopic autoradiography of photoreceptor cells from the myosin VIIa mutant mouse shaker-1 suggest that this unconventional myosin functions in the connecting cilium and participates in the transport of opsin through this structure. Abnormal opsin transport might contribute to blindness in humans with mutations in the gene encoding myosin VIIa (Usher's syndrome)
    • Liu X., Udovichenko I.P., Brown S.D.M., Steel K.P., Williams D.S. Myosin VIIa participates in opsin transport through the photoreceptor cilium. J Neurosci. 19:1999;6267-6274. Immunoelectron microscopy and microscopic autoradiography of photoreceptor cells from the myosin VIIa mutant mouse shaker-1 suggest that this unconventional myosin functions in the connecting cilium and participates in the transport of opsin through this structure. Abnormal opsin transport might contribute to blindness in humans with mutations in the gene encoding myosin VIIa (Usher's syndrome).
    • (1999) J Neurosci , vol.19 , pp. 6267-6274
    • Liu, X.1    Udovichenko, I.P.2    Brown, S.D.M.3    Steel, K.P.4    Williams, D.S.5
  • 91
    • 0033280228 scopus 로고    scopus 로고
    • Visual transduction in Drosophila
    • Montell C. Visual transduction in Drosophila. Annu Rev Cell Dev Biol. 15:1999;231-268.
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 231-268
    • Montell, C.1
  • 92
    • 0032400782 scopus 로고    scopus 로고
    • Requirement for the NINAC kinase/myosin for stable termination of the visual cascade
    • Li H-S., Porter J.A., Montell C. Requirement for the NINAC kinase/myosin for stable termination of the visual cascade. J Neurosci. 18:1998;9601-9606.
    • (1998) J Neurosci , vol.18 , pp. 9601-9606
    • Li, H.-S.1    Porter, J.A.2    Montell, C.3
  • 93
    • 0033366539 scopus 로고    scopus 로고
    • Termination of phototransduction requires binding of the NINAC myosin III and the PDZ protein INAD
    • Wes P.D., Xu X-Z.S., Li H.S., Chien F., Doberstein S.K., Montell C. Termination of phototransduction requires binding of the NINAC myosin III and the PDZ protein INAD. Nat Neurosci. 2:1999;447-453.
    • (1999) Nat Neurosci , vol.2 , pp. 447-453
    • Wes, P.D.1    Xu, X.-Z.S.2    Li, H.S.3    Chien, F.4    Doberstein, S.K.5    Montell, C.6
  • 94
    • 0028838302 scopus 로고
    • Dictyostelium myosin I double mutants exhibit conditional defects in pinocytosis
    • Novak K.D., Peterson M.D., Reedy M.C., Titus M.A. Dictyostelium myosin I double mutants exhibit conditional defects in pinocytosis. J Cell Biol. 131:1995;1205-1221.
    • (1995) J Cell Biol , vol.131 , pp. 1205-1221
    • Novak, K.D.1    Peterson, M.D.2    Reedy, M.C.3    Titus, M.A.4
  • 95
    • 0029925627 scopus 로고    scopus 로고
    • Dictyostelium mutants lacking multiple classic myosin I isoforms reveal combinations of shared and distinct functions
    • Jung G., Wu X., Hammer J.A. Jr. Dictyostelium mutants lacking multiple classic myosin I isoforms reveal combinations of shared and distinct functions. J Cell Biol. 133:1996;305-323.
    • (1996) J Cell Biol , vol.133 , pp. 305-323
    • Jung, G.1    Wu, X.2    Hammer, J.A.3
  • 96
    • 0029923034 scopus 로고    scopus 로고
    • Role of type I myosins in receptor-mediated endocytosis in yeast
    • Geli M.I., Riezman H. Role of type I myosins in receptor-mediated endocytosis in yeast. Science. 272:1996;533-535.
    • (1996) Science , vol.272 , pp. 533-535
    • Geli, M.I.1    Riezman, H.2
  • 97
    • 0032472908 scopus 로고    scopus 로고
    • Distinct functions of calmodulin are required for the uptake step of receptor-mediated endocytosis in yeast: The type I myosin Myo5p is one of the calmodulin targets
    • Geli M.I., Wesp A., Riezman H. Distinct functions of calmodulin are required for the uptake step of receptor-mediated endocytosis in yeast: the type I myosin Myo5p is one of the calmodulin targets. EMBO J. 17:1998;635-647.
    • (1998) EMBO J , vol.17 , pp. 635-647
    • Geli, M.I.1    Wesp, A.2    Riezman, H.3
  • 98
    • 0032486269 scopus 로고    scopus 로고
    • Constitutive activation of endocytosis by mutation of myoA, the myosin I gene of Aspergillus nidulans
    • A mutation that should constitutively activate myoA results in an activation of endocytosis. This and other data demonstrate the in vivo significance of the regulatory phosphorylation site (TEDS site) in myosin I and suggest that myoA has two functions, one dependent and one independent of phosphorylation
    • Yamashita R.A., May G.S. Constitutive activation of endocytosis by mutation of myoA, the myosin I gene of Aspergillus nidulans. J Biol Chem. 273:1998;14644-14648. A mutation that should constitutively activate myoA results in an activation of endocytosis. This and other data demonstrate the in vivo significance of the regulatory phosphorylation site (TEDS site) in myosin I and suggest that myoA has two functions, one dependent and one independent of phosphorylation.
    • (1998) J Biol Chem , vol.273 , pp. 14644-14648
    • Yamashita, R.A.1    May, G.S.2
  • 99
    • 0032897519 scopus 로고    scopus 로고
    • Association of myosin I alpha with endosomes and lysosomes in mammalian cells
    • Subcellular fractionation experiments, immunoelectron microscopy, and transfection of dominant-negative constructs support a role for myosin Iα in a late endocytic step involving membrane traffic between endosomes and lysosomes
    • Raposo G., Cordonnier M-N., Tenza D., Menichi B., Dürrbach A., Louvard D., Coudrier E. Association of myosin I alpha with endosomes and lysosomes in mammalian cells. Mol Biol Cell. 10:1999;1477-1494. Subcellular fractionation experiments, immunoelectron microscopy, and transfection of dominant-negative constructs support a role for myosin Iα in a late endocytic step involving membrane traffic between endosomes and lysosomes.
    • (1999) Mol Biol Cell , vol.10 , pp. 1477-1494
    • Raposo, G.1    Cordonnier, M.-N.2    Tenza, D.3    Menichi, B.4    Dürrbach, A.5    Louvard, D.6    Coudrier, E.7
  • 101
    • 0028930161 scopus 로고
    • A novel mammalian myosin I from rat with an SH3 domain localizes to ConA-inducible, F-actin-rich structures at cell-cell contacts
    • Stöffler H-E., Ruppert C., Reinhard J., Bähler M. A novel mammalian myosin I from rat with an SH3 domain localizes to ConA-inducible, F-actin-rich structures at cell-cell contacts. J Cell Biol. 129:1995;819-830.
    • (1995) J Cell Biol , vol.129 , pp. 819-830
    • Stöffler, H.-E.1    Ruppert, C.2    Reinhard, J.3    Bähler, M.4
  • 102
    • 0032486408 scopus 로고    scopus 로고
    • 2+ binding to its light chain calmodulin
    • 2+ binding to its light chain calmodulin. J Biol Chem. 273:1998;14605-14611.
    • (1998) J Biol Chem , vol.273 , pp. 14605-14611
    • Stöffler, H.E.1    Bähler, M.2
  • 103
    • 0242517286 scopus 로고    scopus 로고
    • Targeting of the myosin-I myr 3 to intercellular adherens type junctions induced by dominant active Cdc42 in HeLa cells
    • The targeting of the rat myosin I myr3 to actin-rich adherens type intercellular junctions is shown to require a short region of the tail excluding the SH3 domain, and a functional motor domain. This system should prove very useful for testing a variety of structure/function questions regarding myr3
    • Stöffler H-E., Honnert U., Bauer C.A., Höfer D., Schwarz H., Müller R.T., Drenckhahn D., Bähler M. Targeting of the myosin-I myr 3 to intercellular adherens type junctions induced by dominant active Cdc42 in HeLa cells. J Cell Sci. 111:1998;2779-2788. The targeting of the rat myosin I myr3 to actin-rich adherens type intercellular junctions is shown to require a short region of the tail excluding the SH3 domain, and a functional motor domain. This system should prove very useful for testing a variety of structure/function questions regarding myr3.
    • (1998) J Cell Sci , vol.111 , pp. 2779-2788
    • Stöffler, H.-E.1    Honnert, U.2    Bauer, C.A.3    Höfer, D.4    Schwarz, H.5    Müller, R.T.6    Drenckhahn, D.7    Bähler, M.8
  • 106
    • 0032800685 scopus 로고    scopus 로고
    • Myosin I contributes to the generation of resting cortical tension
    • The authors used a micropipette aspiration technique to quantitate resting cortical tension in wild-type cells and cells lacking or overexpressing various myosin I isoforms. The results indicate that class I myosins contribute significantly to the generation of tension within the actin cortex, and that this contribution is required for efficient cell migration and macropinocytosis
    • Dia J., Ting-Beal H.P., Hochmuth R.M., Sheetz M.P., Titus M.A. Myosin I contributes to the generation of resting cortical tension. Biophys J. 77:1999;1168-1176. The authors used a micropipette aspiration technique to quantitate resting cortical tension in wild-type cells and cells lacking or overexpressing various myosin I isoforms. The results indicate that class I myosins contribute significantly to the generation of tension within the actin cortex, and that this contribution is required for efficient cell migration and macropinocytosis.
    • (1999) Biophys J , vol.77 , pp. 1168-1176
    • Dia, J.1    Ting-Beal, H.P.2    Hochmuth, R.M.3    Sheetz, M.P.4    Titus, M.A.5
  • 108
    • 0033603239 scopus 로고    scopus 로고
    • Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain tctex-1
    • Tai A.W., Chuang J-Z., Bode C., Wolfrum U., Sung C-H. Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain tctex-1. Cell. 97:1999;877-887.
    • (1999) Cell , vol.97 , pp. 877-887
    • Tai, A.W.1    Chuang, J.-Z.2    Bode, C.3    Wolfrum, U.4    Sung, C.-H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.