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1
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0033619258
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Myosin VI is an actin-based motor that moves backwards
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Wells A.L., Lin A.W., Chen L.Q., Safer D., Cain S.M., Hasson T., Carragher B.O., Milligan R.A., and Sweeney H.L. Myosin VI is an actin-based motor that moves backwards. Nature 401 (1999) 505-508
-
(1999)
Nature
, vol.401
, pp. 505-508
-
-
Wells, A.L.1
Lin, A.W.2
Chen, L.Q.3
Safer, D.4
Cain, S.M.5
Hasson, T.6
Carragher, B.O.7
Milligan, R.A.8
Sweeney, H.L.9
-
2
-
-
0026475396
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An unconventional myosin heavy chain gene from Drosophila melanogaster
-
Kellerman K.A., and Miller K.G. An unconventional myosin heavy chain gene from Drosophila melanogaster. J Cell Biol 119 (1992) 823-834
-
(1992)
J Cell Biol
, vol.119
, pp. 823-834
-
-
Kellerman, K.A.1
Miller, K.G.2
-
3
-
-
2942592305
-
Myosin VI: a structural role in actin organization important for protein and organelle localization and trafficking
-
Frank D.J., Noguchi T., and Miller K.G. Myosin VI: a structural role in actin organization important for protein and organelle localization and trafficking. Curr Opin Cell Biol 16 (2004) 189-194
-
(2004)
Curr Opin Cell Biol
, vol.16
, pp. 189-194
-
-
Frank, D.J.1
Noguchi, T.2
Miller, K.G.3
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4
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33744767752
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Myosin VI stabilizes an actin network during Drosophila spermatid individualization
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This paper demonstrates that myosin VI plays an anchoring, and probably a cross-linking, role in the organization of the investment cone during spermatogenesis in Drosophila.
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Noguchi T., Lenartowska M., and Miller K.G. Myosin VI stabilizes an actin network during Drosophila spermatid individualization. Mol Biol Cell 17 (2006) 2559-2571. This paper demonstrates that myosin VI plays an anchoring, and probably a cross-linking, role in the organization of the investment cone during spermatogenesis in Drosophila.
-
(2006)
Mol Biol Cell
, vol.17
, pp. 2559-2571
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-
Noguchi, T.1
Lenartowska, M.2
Miller, K.G.3
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5
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0034735917
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Myosin VI is required for asymmetric segregation of cellular components during C. elegans spermatogenesis
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Kelleher J.F., Mandell M.A., Moulder G., Hill K.L., L'Hernault S.W., Barstead R., and Titus M.A. Myosin VI is required for asymmetric segregation of cellular components during C. elegans spermatogenesis. Curr Biol 10 (2000) 1489-1496
-
(2000)
Curr Biol
, vol.10
, pp. 1489-1496
-
-
Kelleher, J.F.1
Mandell, M.A.2
Moulder, G.3
Hill, K.L.4
L'Hernault, S.W.5
Barstead, R.6
Titus, M.A.7
-
6
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0028803112
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The mouse Snell's waltzer deafness gene encodes an unconventional required for structural integrity of inner ear hair cells
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Avraham K.B., Hasson T., Steel K.P., Kingsley D.M., Russell L.B., Mooseker M.S., Copeland N.G., and Jenkins N.A. The mouse Snell's waltzer deafness gene encodes an unconventional required for structural integrity of inner ear hair cells. Nat Genet 11 (1995) 369-375
-
(1995)
Nat Genet
, vol.11
, pp. 369-375
-
-
Avraham, K.B.1
Hasson, T.2
Steel, K.P.3
Kingsley, D.M.4
Russell, L.B.5
Mooseker, M.S.6
Copeland, N.G.7
Jenkins, N.A.8
-
7
-
-
0027993176
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Porcine myosin VI: characterization of a new mammalian unconventional myosin
-
Hasson T., and 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
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9
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0035898659
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Myosin VI isoform localized to clathrin-coated vesicles with a role in clathrin-mediated endocytosis
-
Buss F., Arden S.D., Lindsay M., Luzio J.P., and Kendrick-Jones J. Myosin VI isoform localized to clathrin-coated vesicles with a role in clathrin-mediated endocytosis. EMBO J 20 (2001) 3676-3684
-
(2001)
EMBO J
, vol.20
, pp. 3676-3684
-
-
Buss, F.1
Arden, S.D.2
Lindsay, M.3
Luzio, J.P.4
Kendrick-Jones, J.5
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10
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0041327729
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Myosin VI: two distinct roles in endocytosis
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Hasson T. Myosin VI: two distinct roles in endocytosis. J Cell Sci 116 (2003) 3453-3461
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(2003)
J Cell Sci
, vol.116
, pp. 3453-3461
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Hasson, T.1
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11
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2342512884
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Uncoated endocytic vesicles require the unconventional myosin, Myo6, for rapid transport through actin barriers
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This is an important quantitative study of the role myosin VI plays in the movement of uncoated vesicles through a dense actin network.
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Aschenbrenner L., Naccache S.N., and Hasson T. Uncoated endocytic vesicles require the unconventional myosin, Myo6, for rapid transport through actin barriers. Mol Biol Cell 15 (2004) 2253-2263. This is an important quantitative study of the role myosin VI plays in the movement of uncoated vesicles through a dense actin network.
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(2004)
Mol Biol Cell
, vol.15
, pp. 2253-2263
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Aschenbrenner, L.1
Naccache, S.N.2
Hasson, T.3
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12
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0037415731
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Loss of myosin VI reduces secretion and the size of the Golgi in fibroblasts from Snell's waltzer mice
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Warner C.L., Stewart A., Luzio J.P., Steel K.P., Libby R.T., Kendrick-Jones J., and Buss F. Loss of myosin VI reduces secretion and the size of the Golgi in fibroblasts from Snell's waltzer mice. EMBO J 22 (2003) 569-579
-
(2003)
EMBO J
, vol.22
, pp. 569-579
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Warner, C.L.1
Stewart, A.2
Luzio, J.P.3
Steel, K.P.4
Libby, R.T.5
Kendrick-Jones, J.6
Buss, F.7
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13
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0033569707
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Role of myosin VI in the differentiation of cochlear hair cells
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Self T., Sobe T., Copeland N.G., Jenkins N.A., Avraham K.B., and Steel K.P. Role of myosin VI in the differentiation of cochlear hair cells. Dev Biol 214 (1999) 331-341
-
(1999)
Dev Biol
, vol.214
, pp. 331-341
-
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Self, T.1
Sobe, T.2
Copeland, N.G.3
Jenkins, N.A.4
Avraham, K.B.5
Steel, K.P.6
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14
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0034887805
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MYO6, the human homologue of the gene responsible for deafness in Snell's waltzer mice, is mutated in autosomal dominant nonsyndromic hearing loss
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Melchionda S., Ahituv N., Bisceglia L., Sobe T., Glaser F., Rabionet R., Arbones M.L., Notarangelo A., Di Iorio E., Carella M., et al. MYO6, the human homologue of the gene responsible for deafness in Snell's waltzer mice, is mutated in autosomal dominant nonsyndromic hearing loss. Am J Hum Genet 69 (2001) 635-640
-
(2001)
Am J Hum Genet
, vol.69
, pp. 635-640
-
-
Melchionda, S.1
Ahituv, N.2
Bisceglia, L.3
Sobe, T.4
Glaser, F.5
Rabionet, R.6
Arbones, M.L.7
Notarangelo, A.8
Di Iorio, E.9
Carella, M.10
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15
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0037730096
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Mutations of MYO6 are associated with recessive deafness, DFNB37
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Ahmed Z.M., Morell R.J., Riazuddin S., Gropman A., Shaukat S., Ahmad M.M., Mohiddin S.A., Fananapazir L., Caruso R.C., Husnain T., et al. Mutations of MYO6 are associated with recessive deafness, DFNB37. Am J Hum Genet 72 (2003) 1315-1322
-
(2003)
Am J Hum Genet
, vol.72
, pp. 1315-1322
-
-
Ahmed, Z.M.1
Morell, R.J.2
Riazuddin, S.3
Gropman, A.4
Shaukat, S.5
Ahmad, M.M.6
Mohiddin, S.A.7
Fananapazir, L.8
Caruso, R.C.9
Husnain, T.10
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16
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0036052866
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Myosin VI is required for E-cadherin-mediated border cell migration
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Geisbrecht E.R., and Montell D.J. Myosin VI is required for E-cadherin-mediated border cell migration. Nat Cell Biol 4 (2002) 616-620
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(2002)
Nat Cell Biol
, vol.4
, pp. 616-620
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Geisbrecht, E.R.1
Montell, D.J.2
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17
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5344267416
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Myosin VI plays a role in cell-cell adhesion during epithelial morphogenesis
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Millo H., Leaper K., Lazou V., and Bownes M. Myosin VI plays a role in cell-cell adhesion during epithelial morphogenesis. Mech Dev 121 (2004) 1335-1351
-
(2004)
Mech Dev
, vol.121
, pp. 1335-1351
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Millo, H.1
Leaper, K.2
Lazou, V.3
Bownes, M.4
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18
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2542623703
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Lessons from border cell migration in the Drosophila ovary: A role for myosin VI in dissemination of human ovarian cancer
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Yoshida H., Cheng W., Hung J., Montell D., Geisbrecht E., Rosen D., Liu J., and Naora H. Lessons from border cell migration in the Drosophila ovary: A role for myosin VI in dissemination of human ovarian cancer. Proc Natl Acad Sci USA 101 (2004) 8144-8149
-
(2004)
Proc Natl Acad Sci USA
, vol.101
, pp. 8144-8149
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Yoshida, H.1
Cheng, W.2
Hung, J.3
Montell, D.4
Geisbrecht, E.5
Rosen, D.6
Liu, J.7
Naora, H.8
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19
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33644752095
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Myosin VI is a mediator of the p53-dependent cell survival pathway
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Jung E.J., Liu G., Zhou W., and Chen X. Myosin VI is a mediator of the p53-dependent cell survival pathway. Mol Cell Biol 26 (2006) 2175-2186
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(2006)
Mol Cell Biol
, vol.26
, pp. 2175-2186
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Jung, E.J.1
Liu, G.2
Zhou, W.3
Chen, X.4
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20
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33747871719
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Nuclear myosin VI enhances RNA polymerase II-dependent transcription
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While this was not the first paper to demonstrate that myosin VI is in the nucleus, it is an important demonstration of it having a functional role in the nucleus. Perhaps this is yet another anchoring role, providing physical support for the process of transcription.
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Vreugde S., Ferrai C., Miluzio A., Hauben E., Marchisio P.C., Crippa M.P., Bussi M., and Biffo S. Nuclear myosin VI enhances RNA polymerase II-dependent transcription. Mol Cell 23 (2006) 749-755. While this was not the first paper to demonstrate that myosin VI is in the nucleus, it is an important demonstration of it having a functional role in the nucleus. Perhaps this is yet another anchoring role, providing physical support for the process of transcription.
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(2006)
Mol Cell
, vol.23
, pp. 749-755
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Vreugde, S.1
Ferrai, C.2
Miluzio, A.3
Hauben, E.4
Marchisio, P.C.5
Crippa, M.P.6
Bussi, M.7
Biffo, S.8
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21
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18544367185
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Optineurin links myosin VI to the Golgi complex and is involved in Golgi organization and exocytosis
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This study demonstrates that myosin VI localization to the Golgi can be mediated by the adapter protein, optineurin. The binding sites for optineurin and myosin VI are mapped. Since optineurin is a dimer, the work may imply that myosin VI serves its Golgi function as a dimer.
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Sahlender D.A., Roberts R.C., Arden S.D., Spudich G., Taylor M.J., Luzio J.P., Kendrick-Jones J., and Buss F. Optineurin links myosin VI to the Golgi complex and is involved in Golgi organization and exocytosis. J Cell Biol 169 (2005) 285-295. This study demonstrates that myosin VI localization to the Golgi can be mediated by the adapter protein, optineurin. The binding sites for optineurin and myosin VI are mapped. Since optineurin is a dimer, the work may imply that myosin VI serves its Golgi function as a dimer.
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(2005)
J Cell Biol
, vol.169
, pp. 285-295
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Sahlender, D.A.1
Roberts, R.C.2
Arden, S.D.3
Spudich, G.4
Taylor, M.J.5
Luzio, J.P.6
Kendrick-Jones, J.7
Buss, F.8
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22
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13844294267
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A role for myosin VI in postsynaptic structure and glutamate receptor endocytosis
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Osterweil E., Wells D.G., and Mooseker M.S. A role for myosin VI in postsynaptic structure and glutamate receptor endocytosis. J Cell Biol 168 (2005) 329-338
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(2005)
J Cell Biol
, vol.168
, pp. 329-338
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Osterweil, E.1
Wells, D.G.2
Mooseker, M.S.3
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24
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0036242467
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Myosin VI binds to and localizes with Dab2, potentially linking receptor-mediated endocytosis and the actin cytoskeleton
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Morris S.M., Arden S.D., Roberts R.C., Kendrick-Jones J., Cooper J.A., Luzio J.P., and Buss F. Myosin VI binds to and localizes with Dab2, potentially linking receptor-mediated endocytosis and the actin cytoskeleton. Traffic 3 (2002) 331-341
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(2002)
Traffic
, vol.3
, pp. 331-341
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Morris, S.M.1
Arden, S.D.2
Roberts, R.C.3
Kendrick-Jones, J.4
Cooper, J.A.5
Luzio, J.P.6
Buss, F.7
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25
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4744348952
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Regulation of myosin-VI targeting to endocytic compartments
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The long insertion splice-form of the tail is shown to target myosin VI to Dab2 on coated endocytic vesicles, but only in the context of the full-length molecule. In the absence of Dab2, the same splice-form is retargeted to uncoated vesicles.
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Dance A.L., Miller M., Seragaki S., Aryal P., White B., Aschenbrenner L., and Hasson T. Regulation of myosin-VI targeting to endocytic compartments. Traffic 5 (2004) 798-813. The long insertion splice-form of the tail is shown to target myosin VI to Dab2 on coated endocytic vesicles, but only in the context of the full-length molecule. In the absence of Dab2, the same splice-form is retargeted to uncoated vesicles.
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(2004)
Traffic
, vol.5
, pp. 798-813
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Dance, A.L.1
Miller, M.2
Seragaki, S.3
Aryal, P.4
White, B.5
Aschenbrenner, L.6
Hasson, T.7
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26
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20444457946
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The structure of the myosin VI motor reveals the mechanism of directionality reversal
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The structure of the myosin VI motor domain at 2.4Å reveals how a class-specific insert (insert 2) recruits a CaM and repositions the lever arm by 120°. This is the basis for the reversal of directionality in myosin VI.
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Ménétrey J., Bahloul A., Wells A.L., Yengo C.M., Morris C.A., Sweeney H.L., and Houdusse A. The structure of the myosin VI motor reveals the mechanism of directionality reversal. Nature 435 (2005) 779-785. The structure of the myosin VI motor domain at 2.4Å reveals how a class-specific insert (insert 2) recruits a CaM and repositions the lever arm by 120°. This is the basis for the reversal of directionality in myosin VI.
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(2005)
Nature
, vol.435
, pp. 779-785
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Ménétrey, J.1
Bahloul, A.2
Wells, A.L.3
Yengo, C.M.4
Morris, C.A.5
Sweeney, H.L.6
Houdusse, A.7
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27
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1542299042
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The mechanism of myosin VI translocation and its load-induced anchoring
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Using an optical trap, the authors demonstrate that myosin VI remains tightly bound to actin for long periods of time (seconds) in the presence of ATP when subjected to loads greater than that needed to stop its processive movement (the stall force). This provides in vitro evidence of, and the mechanism for, the anchoring role of myosin VI in cells.
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Altman D., Sweeney H.L., and Spudich J.A. The mechanism of myosin VI translocation and its load-induced anchoring. Cell 116 (2004) 737-749. Using an optical trap, the authors demonstrate that myosin VI remains tightly bound to actin for long periods of time (seconds) in the presence of ATP when subjected to loads greater than that needed to stop its processive movement (the stall force). This provides in vitro evidence of, and the mechanism for, the anchoring role of myosin VI in cells.
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(2004)
Cell
, vol.116
, pp. 737-749
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Altman, D.1
Sweeney, H.L.2
Spudich, J.A.3
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28
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11144354046
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The unique insert in myosin VI is a structural calcium-calmodulin binding site
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Bahloul A., Chevreux G., Wells A.L., Martin D., Nolt J., Yang Z., Chen L.Q., Potier N., Van Dorsselaer A., Rosenfeld S., et al. The unique insert in myosin VI is a structural calcium-calmodulin binding site. Proc Natl Acad Sci USA 101 (2004) 4787-4792
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(2004)
Proc Natl Acad Sci USA
, vol.101
, pp. 4787-4792
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Bahloul, A.1
Chevreux, G.2
Wells, A.L.3
Martin, D.4
Nolt, J.5
Yang, Z.6
Chen, L.Q.7
Potier, N.8
Van Dorsselaer, A.9
Rosenfeld, S.10
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29
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0035939958
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The core of the motor domain determines the direction of myosin movement
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Homma K., Yoshimura M., Saito J., Ikebe R., and Ikebe M. The core of the motor domain determines the direction of myosin movement. Nature 412 (2001) 831-834
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(2001)
Nature
, vol.412
, pp. 831-834
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Homma, K.1
Yoshimura, M.2
Saito, J.3
Ikebe, R.4
Ikebe, M.5
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30
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33846530168
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Park H, Li A, Chen L-Q, Houdusse A, Selvin PR, Sweeney HL: The unique insert at the end of the myosin VI motor is the sole determinant of directionality. Proc Natl Acad Sci USA 2007, in press. This work demonstrates that the unique myosin insert that is part of the converter (insert 2) is the sole determinant of directionality reversal. With it removed, myosin VI is plus-end directed. The approach used is to affix myosin V lever arms to the myosin VI converter with and without insert 2. Motility assays are used to determine the directionality of single- and double-headed constructs. Surprisingly, by examining the step size of the single dimeric molecules using a FIONA assay, the study also demonstrates that the large variability of the myosin VI step size is an inherent property of the motor, and is not due to a flexible lever arm extension.
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33846329353
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Bryant Z, Altman D, Spudich JA: The power stroke of myosin VI and determinants of directionality. Proc Natl Acad Sci USA 2007, in press. This work uses an optical trap to measure the size of the stroke and motility assays to determine the directionality of molecules created via sequential truncations of single-headed myosin VI constructs. The longest construct contains the putative lever arm extension, while the shortest removes insert 2. With insert 2 removed, the motor becomes plus-end directed, demonstrating that insert 2 is sufficient to reverse the directionality of the motor. The study also demonstrates that the single-headed myosin VI stroke size is large, even though the lever arm is short, consistent with a near 180° rotation of the converter from the pre-powerstroke to the end of the powerstroke (rigor).
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0035923504
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Myosin VI is a processive motor with a large step size
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Rock R.S., Rice S.E., Wells A.L., Purcell T.J., Spudich J.A., and Sweeney H.L. Myosin VI is a processive motor with a large step size. Proc Natl Acad Sci USA 98 (2001) 13655-13659
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(2001)
Proc Natl Acad Sci USA
, vol.98
, pp. 13655-13659
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Rock, R.S.1
Rice, S.E.2
Wells, A.L.3
Purcell, T.J.4
Spudich, J.A.5
Sweeney, H.L.6
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33
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18444414585
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Class VI myosin moves processively along actin filaments backward with large steps
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Nishikawa S., Homma K., Komori Y., Iwaki M., Wazawa T., Hikikoshi Iwane A., Saito J., Ikebe R., Katayama E., Yanagida T., and Ikebe M. Class VI myosin moves processively along actin filaments backward with large steps. Biochem Biophys Res Commun 290 (2002) 311-317
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(2002)
Biochem Biophys Res Commun
, vol.290
, pp. 311-317
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Nishikawa, S.1
Homma, K.2
Komori, Y.3
Iwaki, M.4
Wazawa, T.5
Hikikoshi Iwane, A.6
Saito, J.7
Ikebe, R.8
Katayama, E.9
Yanagida, T.10
Ikebe, M.11
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34
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0035943690
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Kinetic mechanism and regulation of myosin VI
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De La Cruz E.M., Ostap E.M., and Sweeney H.L. Kinetic mechanism and regulation of myosin VI. J Biol Chem 276 (2001) 32373-32381
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(2001)
J Biol Chem
, vol.276
, pp. 32373-32381
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De La Cruz, E.M.1
Ostap, E.M.2
Sweeney, H.L.3
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35
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Myosin VI steps via a hand-over-hand mechanism with its lever arm undergoing fluctuations when attached to actin
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This was a demonstration, using a single molecule imaging technique known as FIONA, that myosin VI, like myosin V, uses a hand-over-hand mechanism for processive movement. This study further shows that the lever arm position fluctuates during stepping. This may underlie the large variability in the myosin VI step size, which appears to be a property of the motor core.
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Yildiz A., Park H., Safer D., Yang Z., Chen L.Q., Selvin P.R., and Sweeney H.L. Myosin VI steps via a hand-over-hand mechanism with its lever arm undergoing fluctuations when attached to actin. J Biol Chem 279 (2004) 37223-37226. This was a demonstration, using a single molecule imaging technique known as FIONA, that myosin VI, like myosin V, uses a hand-over-hand mechanism for processive movement. This study further shows that the lever arm position fluctuates during stepping. This may underlie the large variability in the myosin VI step size, which appears to be a property of the motor core.
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(2004)
J Biol Chem
, vol.279
, pp. 37223-37226
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Yildiz, A.1
Park, H.2
Safer, D.3
Yang, Z.4
Chen, L.Q.5
Selvin, P.R.6
Sweeney, H.L.7
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37
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Unconstrained steps of myosin VI appear longest among known molecular motors
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Ali M.Y., Homma K., Iwane A.H., Adachi K., Itoh H., Kinosita Jr. K., Yanagida T., and Ikebe M. Unconstrained steps of myosin VI appear longest among known molecular motors. Biophys J 86 (2004) 3804-3810
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(2004)
Biophys J
, vol.86
, pp. 3804-3810
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Ali, M.Y.1
Homma, K.2
Iwane, A.H.3
Adachi, K.4
Itoh, H.5
Kinosita Jr., K.6
Yanagida, T.7
Ikebe, M.8
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38
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13944269581
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A flexible domain is essential for the large step size and processivity of myosin VI
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This study presents both structural (EM) and single molecule functional data demonstrating that what we now term the 'lever arm extension' is in part responsible for the large step size of myosin VI. That it is a flexible element, which was inferred from the variability of the step size, is now in doubt.
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Rock R.S., Ramamurthy B., Dunn A.R., Beccafico S., Rami B.R., Morris C., Spink B.J., Franzini-Armstrong C., Spudich J.A., and Sweeney H.L. A flexible domain is essential for the large step size and processivity of myosin VI. Mol Cell 17 (2005) 603-609. This study presents both structural (EM) and single molecule functional data demonstrating that what we now term the 'lever arm extension' is in part responsible for the large step size of myosin VI. That it is a flexible element, which was inferred from the variability of the step size, is now in doubt.
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(2005)
Mol Cell
, vol.17
, pp. 603-609
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Rock, R.S.1
Ramamurthy, B.2
Dunn, A.R.3
Beccafico, S.4
Rami, B.R.5
Morris, C.6
Spink, B.J.7
Franzini-Armstrong, C.8
Spudich, J.A.9
Sweeney, H.L.10
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39
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Mechanism of nucleotide binding to actomyosin VI: Evidence for allosteric head-head communication
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Robblee J.P., Olivares A.O., and De La Cruz E.M. Mechanism of nucleotide binding to actomyosin VI: Evidence for allosteric head-head communication. J Biol Chem 279 (2004) 38608-38617
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(2004)
J Biol Chem
, vol.279
, pp. 38608-38617
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Robblee, J.P.1
Olivares, A.O.2
De La Cruz, E.M.3
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40
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4544232738
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A model of myosin V processivity
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This is the kinetic study that elucidated the mechanism for coordination ('gating') between the heads of myosin V during processive movement.
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Rosenfeld S.S., and Sweeney H.L. A model of myosin V processivity. J Biol Chem 279 (2004) 40100-40111. This is the kinetic study that elucidated the mechanism for coordination ('gating') between the heads of myosin V during processive movement.
-
(2004)
J Biol Chem
, vol.279
, pp. 40100-40111
-
-
Rosenfeld, S.S.1
Sweeney, H.L.2
-
41
-
-
0037593548
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Calcium functionally uncouples the heads of myosin VI
-
Morris C.A., Wells A.L., Yang Z., Chen L.Q., Baldacchino C.V., and Sweeney H.L. Calcium functionally uncouples the heads of myosin VI. J Biol Chem 278 (2003) 23324-23330
-
(2003)
J Biol Chem
, vol.278
, pp. 23324-23330
-
-
Morris, C.A.1
Wells, A.L.2
Yang, Z.3
Chen, L.Q.4
Baldacchino, C.V.5
Sweeney, H.L.6
-
42
-
-
25444437003
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A force-dependent state controls the coordination of processive myosin V
-
Purcell T.J., Sweeney H.L., and Spudich J.A. A force-dependent state controls the coordination of processive myosin V. Proc Natl Acad Sci USA 102 (2005) 13873-13878
-
(2005)
Proc Natl Acad Sci USA
, vol.102
, pp. 13873-13878
-
-
Purcell, T.J.1
Sweeney, H.L.2
Spudich, J.A.3
-
43
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-
26944449015
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Load-dependent kinetics of myosin V can explain its high processivity
-
Veigel C., Schmitz S., Wang F., and Sellers J.R. Load-dependent kinetics of myosin V can explain its high processivity. Nat Cell Biol 7 (2005) 861-869
-
(2005)
Nat Cell Biol
, vol.7
, pp. 861-869
-
-
Veigel, C.1
Schmitz, S.2
Wang, F.3
Sellers, J.R.4
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44
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Full-length myosin VI dimerizes and moves processively along actin filaments upon monomer clustering
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This work addresses the question of whether or not full-length myosin VI can dimerize and function as a dimer. It demonstrates in vitro that it does when two full-length monomers bind near each other on actin, or are held together by antibody binding. The implication is that cargo binding regulates dimerization in vivo.
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Park H., Ramamurthy B., Travaglia M., Safer D., Chen L.Q., Franzini-Armstrong C., Selvin P.R., and Sweeney H.L. Full-length myosin VI dimerizes and moves processively along actin filaments upon monomer clustering. Mol Cell 21 (2006) 331-336. This work addresses the question of whether or not full-length myosin VI can dimerize and function as a dimer. It demonstrates in vitro that it does when two full-length monomers bind near each other on actin, or are held together by antibody binding. The implication is that cargo binding regulates dimerization in vivo.
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(2006)
Mol Cell
, vol.21
, pp. 331-336
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Park, H.1
Ramamurthy, B.2
Travaglia, M.3
Safer, D.4
Chen, L.Q.5
Franzini-Armstrong, C.6
Selvin, P.R.7
Sweeney, H.L.8
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45
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1842681965
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Myosin V processivity: multiple kinetic pathways for head-to-head coordination
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Baker J.E., Krementsova E.B., Kennedy G.G., Armstrong A., Trybus K.M., and Warshaw D.M. Myosin V processivity: multiple kinetic pathways for head-to-head coordination. Proc Natl Acad Sci USA 101 (2004) 5542-5546
-
(2004)
Proc Natl Acad Sci USA
, vol.101
, pp. 5542-5546
-
-
Baker, J.E.1
Krementsova, E.B.2
Kennedy, G.G.3
Armstrong, A.4
Trybus, K.M.5
Warshaw, D.M.6
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46
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2442609583
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A monomeric myosin VI with a large working stroke
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This was the initial demonstration that full-length myosin VI is isolated from cells as a monomer and does not readily dimerize in vitro. It raises the question of whether myosin VI works as a monomer or dimer in cells, or as both.
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Lister I., Schmitz S., Walker M., Trinick J., Buss F., Veigel C., and Kendrick-Jones J. A monomeric myosin VI with a large working stroke. EMBO J 23 (2004) 1729-1738. This was the initial demonstration that full-length myosin VI is isolated from cells as a monomer and does not readily dimerize in vitro. It raises the question of whether myosin VI works as a monomer or dimer in cells, or as both.
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(2004)
EMBO J
, vol.23
, pp. 1729-1738
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Lister, I.1
Schmitz, S.2
Walker, M.3
Trinick, J.4
Buss, F.5
Veigel, C.6
Kendrick-Jones, J.7
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47
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25844528995
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The predicted coiled-coil domain of myosin 10 forms a novel elongated domain that lengthens the head
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Knight P.J., Thirumurugan K., Xu Y., Wang F., Kalverda A.P., Stafford III W.F., Sellers J.R., and Peckham M. The predicted coiled-coil domain of myosin 10 forms a novel elongated domain that lengthens the head. J Biol Chem 280 (2005) 34702-34708
-
(2005)
J Biol Chem
, vol.280
, pp. 34702-34708
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-
Knight, P.J.1
Thirumurugan, K.2
Xu, Y.3
Wang, F.4
Kalverda, A.P.5
Stafford III, W.F.6
Sellers, J.R.7
Peckham, M.8
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48
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33645801204
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Dimerized Drosophila myosin VIIa: a processive motor
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In this study the authors show that myosin VIIA, which has a putative coiled coil similar to that of myosin VI, is a processive motor when forced to dimerize (by the addition of leucine zipper). The authors also state (without showing data) that, as in the case of myosin VI, monomer clustering on actin can lead to dimerization and processive movement in the absence of a leucine zipper. Thus, myosin VIIa joins myosin VI as a candidate for cellular regulation via cargo-mediated dimerization.
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Yang Y., Kovacs M., Sakamoto T., Zhang F., Kiehart D.P., and Sellers J.R. Dimerized Drosophila myosin VIIa: a processive motor. Proc Natl Acad Sci USA 103 (2006) 5746-5751. In this study the authors show that myosin VIIA, which has a putative coiled coil similar to that of myosin VI, is a processive motor when forced to dimerize (by the addition of leucine zipper). The authors also state (without showing data) that, as in the case of myosin VI, monomer clustering on actin can lead to dimerization and processive movement in the absence of a leucine zipper. Thus, myosin VIIa joins myosin VI as a candidate for cellular regulation via cargo-mediated dimerization.
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(2006)
Proc Natl Acad Sci USA
, vol.103
, pp. 5746-5751
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Yang, Y.1
Kovacs, M.2
Sakamoto, T.3
Zhang, F.4
Kiehart, D.P.5
Sellers, J.R.6
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49
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33746129173
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Three-dimensional structure of the myosin V inhibited state by cryoelectron tomography
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This paper is an elegant use of two-dimensional crystallization and cryoelectron tomography and provides a structure for the inhibited, folded state of myosin V. Unlike myosin VI, myosin V is a constitutive dimer that is thought to unfold and be activated either by cargo binding or by increased calcium concentration in a cell
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Liu J., Taylor D.W., Krementsova E.B., Trybus K.M., and Taylor K.A. Three-dimensional structure of the myosin V inhibited state by cryoelectron tomography. Nature 442 (2006) 208-211. This paper is an elegant use of two-dimensional crystallization and cryoelectron tomography and provides a structure for the inhibited, folded state of myosin V. Unlike myosin VI, myosin V is a constitutive dimer that is thought to unfold and be activated either by cargo binding or by increased calcium concentration in a cell
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(2006)
Nature
, vol.442
, pp. 208-211
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Liu, J.1
Taylor, D.W.2
Krementsova, E.B.3
Trybus, K.M.4
Taylor, K.A.5
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51
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33748993440
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Myosin VI altered at threonine 406 stabilizes actin filaments in vivo
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This is an intriguing demonstration that a mutation mimicking phosphorylation of the myosin VI motor within its actin-binding domain influences its behavior in cells. It is not clear that the mutation truly mimics phosphorylation in the myosin VI context, but the findings warrant further investigation.
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Naccache S.N., and Hasson T. Myosin VI altered at threonine 406 stabilizes actin filaments in vivo. Cell Motil Cytoskeleton 63 (2006) 633-645. This is an intriguing demonstration that a mutation mimicking phosphorylation of the myosin VI motor within its actin-binding domain influences its behavior in cells. It is not clear that the mutation truly mimics phosphorylation in the myosin VI context, but the findings warrant further investigation.
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(2006)
Cell Motil Cytoskeleton
, vol.63
, pp. 633-645
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Naccache, S.N.1
Hasson, T.2
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52
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0032517817
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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
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Buss F., Kendrick-Jones J., Lionne C., Knight A.E., Cote G.P., and Paul Luzio J. 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
Cote, G.P.5
Paul Luzio, J.6
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53
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3343024445
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Myosin VI is required for structural integrity of the apical surface of sensory hair cells in zebrafish
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This paper demonstrates a conserved role among vertebrates for myosin VI in the maintenance of stereocilia. It further reinforces the idea that myosin VI is involved with anchoring interactions with the plasma membrane. The study again raises the possibility of a vesicle-transporting role in the hair cells, in addition to the anchoring role.
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Seiler C., Ben-David O., Sidi S., Hendrich O., Rusch A., Burnside B., Avraham K.B., and Nicolson T. Myosin VI is required for structural integrity of the apical surface of sensory hair cells in zebrafish. Dev Biol 272 (2004) 328-338. This paper demonstrates a conserved role among vertebrates for myosin VI in the maintenance of stereocilia. It further reinforces the idea that myosin VI is involved with anchoring interactions with the plasma membrane. The study again raises the possibility of a vesicle-transporting role in the hair cells, in addition to the anchoring role.
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(2004)
Dev Biol
, vol.272
, pp. 328-338
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Seiler, C.1
Ben-David, O.2
Sidi, S.3
Hendrich, O.4
Rusch, A.5
Burnside, B.6
Avraham, K.B.7
Nicolson, T.8
-
54
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-
0028359778
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Transport of cytoplasmic particles catalyzed by an unconventional myosin in living Drosophila embryos
-
Mermall V., McNally J.G., and Miller K.G. Transport of cytoplasmic particles catalyzed 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
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55
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0032576622
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Visualization of melanosome dynamics within wild-type and dilute melanocytes suggests a paradigm for myosin V function in vivo
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Wu X., Bowers B., Rao K., Wei Q., and Hammer III J.A. 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
-
(1998)
J Cell Biol
, vol.143
, pp. 1899-1918
-
-
Wu, X.1
Bowers, B.2
Rao, K.3
Wei, Q.4
Hammer III, J.A.5
-
56
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0037115631
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A role for myosin VI in actin dynamics at sites of membrane remodeling during Drosophila spermatogenesis
-
Rogat A.D., and Miller K.G. A role for myosin VI in actin dynamics at sites of membrane remodeling during Drosophila spermatogenesis. J Cell Sci 115 (2002) 4855-4865
-
(2002)
J Cell Sci
, vol.115
, pp. 4855-4865
-
-
Rogat, A.D.1
Miller, K.G.2
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