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Volumn 124, Issue 22, 2011, Pages 3733-3741

Myosin-X: A MyTH-FERM myosin at the tips of filopodia

Author keywords

Filopodia; Intrafilopodial motility; Myo10; Myosin X; MyTH4 FERM

Indexed keywords

ACTIN; INTEGRIN; MYOSIN; MYOSIN 10; TALIN; TRANSFORMING GROWTH FACTOR BETA; UNCLASSIFIED DRUG;

EID: 84856777960     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.023549     Document Type: Note
Times cited : (119)

References (95)
  • 5
    • 40849097482 scopus 로고    scopus 로고
    • Calmodulin-like protein enhances myosin-10 translation
    • Bennett, R. D. and Strehler, E. E. (2008). Calmodulin-like protein enhances myosin-10 translation. Biochem. Biophys. Res. Commun. 369, 654-659.
    • (2008) Biochem. Biophys. Res. Commun. , vol.369 , pp. 654-659
    • Bennett, R.D.1    Strehler, E.E.2
  • 6
    • 34047250470 scopus 로고    scopus 로고
    • Calmodulin-like protein increases filopodia-dependent cell motility via up-regulation of myosin-10
    • Bennett, R. D., Mauer, A. S. and Strehler, E. E. (2007). Calmodulin-like protein increases filopodia-dependent cell motility via up-regulation of myosin-10. J. Biol. Chem. 282, 3205-3212.
    • (2007) J. Biol. Chem. , vol.282 , pp. 3205-3212
    • Bennett, R.D.1    Mauer, A.S.2    Strehler, E.E.3
  • 7
    • 45549109551 scopus 로고    scopus 로고
    • Interaction with the IQ3 motif of myosin-10 is required for calmodulin-like protein-dependent filopodial extension
    • Bennett, R. D., Caride, A. J., Mauer, A. S. and Strehler, E. E. (2008). Interaction with the IQ3 motif of myosin-10 is required for calmodulin-like protein-dependent filopodial extension. FEBS Lett. 582, 2377-2381.
    • (2008) FEBS Lett , vol.582 , pp. 2377-2381
    • Bennett, R.D.1    Caride, A.J.2    Mauer, A.S.3    Strehler, E.E.4
  • 8
    • 0036122307 scopus 로고    scopus 로고
    • Myosin-X is an unconventional myosin that undergoes intrafilopodial motility
    • Berg, J. S. and Cheney, R. E. (2002). Myosin-X is an unconventional myosin that undergoes intrafilopodial motility. Nat. Cell Biol. 4, 246-250.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 246-250
    • Berg, J.S.1    Cheney, R.E.2
  • 9
    • 0033766768 scopus 로고    scopus 로고
    • Myosin-X, a novel myosin with pleckstrin homology domains, associates with regions of dynamic actin
    • Berg, J. S., Derfler, B. H., Pennisi, C. M., Corey, D. P. and Cheney, R. E. (2000). Myosin-X, a novel myosin with pleckstrin homology domains, associates with regions of dynamic actin. J. Cell Sci. 113, 3439-3451.
    • (2000) J. Cell Sci. , vol.113 , pp. 3439-3451
    • Berg, J.S.1    Derfler, B.H.2    Pennisi, C.M.3    Corey, D.P.4    Cheney, R.E.5
  • 10
    • 33747622327 scopus 로고    scopus 로고
    • Myosin-X is a molecular motor that functions in filopodia formation
    • Bohil, A. B., Robertson, B. W. and Cheney, R. E. (2006). Myosin-X is a molecular motor that functions in filopodia formation. Proc. Natl. Acad. Sci. USA 103, 12411-12416.
    • Proc. Natl. Acad. Sci. USA , vol.103 , pp. 12411-12416
    • Bohil, A.B.1    Robertson, B.W.2    Cheney, R.E.3
  • 11
    • 67649875674 scopus 로고    scopus 로고
    • Unconventional myosin traffic in cells reveals a selective actin cytoskeleton
    • Brawley, C. M. and Rock, R. S. (2009). Unconventional myosin traffic in cells reveals a selective actin cytoskeleton. Proc. Natl. Acad. Sci. USA 106, 9685-9690.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 9685-9690
    • Brawley, C.M.1    Rock, R.S.2
  • 12
    • 77951054905 scopus 로고    scopus 로고
    • An unconventional myosin required for cell polarization and chemotaxis
    • Breshears, L. M., Wessels, D., Soll, D. R. and Titus, M. A. (2010). An unconventional myosin required for cell polarization and chemotaxis. Proc. Natl. Acad. Sci. USA 107, 6918-6923.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 6918-6923
    • Breshears, L.M.1    Wessels, D.2    Soll, D.R.3    Titus, M.A.4
  • 13
    • 77956582527 scopus 로고    scopus 로고
    • Kinetic analysis reveals differences in the binding mechanism of calmodulin and calmodulin-like protein to the IQ motifs of myosin-10
    • Caride, A. J., Bennett, R. D. and Strehler, E. E. (2010). Kinetic analysis reveals differences in the binding mechanism of calmodulin and calmodulin-like protein to the IQ motifs of myosin-10. Biochemistry 49, 8105-8116.
    • (2010) Biochemistry , vol.49 , pp. 8105-8116
    • Caride, A.J.1    Bennett, R.D.2    Strehler, E.E.3
  • 15
    • 0141953237 scopus 로고    scopus 로고
    • Cytoskeletal dynamics and transport in growth cone motility and axon guidance
    • Dent, E. W. and Gertler, F. B. (2003). Cytoskeletal dynamics and transport in growth cone motility and axon guidance. Neuron 40, 209-227.
    • (2003) Neuron , vol.40 , pp. 209-227
    • Dent, E.W.1    Gertler, F.B.2
  • 17
    • 84856786932 scopus 로고    scopus 로고
    • Myosin10
    • (ed. L. M. Coluccio), Dordrecht, The Netherlands: Springer
    • Divito, M. M. and Cheney, R. E. (2008). Myosin10. In Myosins: A Superfamily of Molecular Motors (ed. L. M. Coluccio), pp. 403-419. Dordrecht, The Netherlands: Springer.
    • (2008) Myosins: A Superfamily of Molecular Motors , pp. 403-419
    • Divito, M.M.1    Cheney, R.E.2
  • 18
    • 77957241701 scopus 로고    scopus 로고
    • Dynamics of endothelial cell behavior in sprouting angiogenesis
    • Eilken, H. M. and Adams, R. H. (2010). Dynamics of endothelial cell behavior in sprouting angiogenesis. Curr. Opin. Cell Biol. 22, 617-625.
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 617-625
    • Eilken, H.M.1    Adams, R.H.2
  • 21
    • 79960072801 scopus 로고    scopus 로고
    • Structural basis of cargo recognition by the myosin-X MyTH4-FERM domain
    • Hirano, Y., Hatano, T., Takahashi, A., Toriyama, M., Inagaki, N. and Hakoshima, T. (2011). Structural basis of cargo recognition by the myosin-X MyTH4-FERM domain. EMBO J. 30, 2734-2747.
    • (2011) EMBO J , vol.30 , pp. 2734-2747
    • Hirano, Y.1    Hatano, T.2    Takahashi, A.3    Toriyama, M.4    Inagaki, N.5    Hakoshima, T.6
  • 22
    • 23844449706 scopus 로고    scopus 로고
    • Myosin X is a high duty ratio motor
    • Homma, K. and Ikebe, M. (2005). Myosin X is a high duty ratio motor. J. Biol. Chem. 280, 29381-29391.
    • J. Biol. Chem. , vol.280 , pp. 29381-29391
    • Homma, K.1    Ikebe, M.2
  • 23
    • 0035823492 scopus 로고    scopus 로고
    • Motor function and regulation of myosin X
    • Homma, K., Saito, J., Ikebe, R. and Ikebe, M. (2001). Motor function and regulation of myosin X. J. Biol. Chem. 276, 34348-34354.
    • (2001) J. Biol. Chem. , vol.276 , pp. 34348-34354
    • Homma, K.1    Saito, J.2    Ikebe, R.3    Ikebe, M.4
  • 24
    • 70349322724 scopus 로고    scopus 로고
    • Myosin-X is required for cranial neural crest cell migration in Xenopus laevis
    • Hwang, Y. S., Luo, T., Xu, Y. and Sargent, T. D. (2009). Myosin-X is required for cranial neural crest cell migration in Xenopus laevis. Dev. Dyn. 238, 2522-2529.
    • (2009) Dev. Dyn. , vol.238 , pp. 2522-2529
    • Hwang, Y.S.1    Luo, T.2    Xu, Y.3    Sargent, T.D.4
  • 25
    • 0032530384 scopus 로고    scopus 로고
    • Identification and analysis of PH domain-containing targets of phosphatidylinositol 3-kinase using a novel in vivo assay in yeast
    • Isakoff, S. J., Cardozo, T., Andreev, J., Li, Z., Ferguson, K. M., Abagyan, R., Lemmon, M. A., Aronheim, A. and Skolnik, E. Y. (1998). Identification and analysis of PH domain-containing targets of phosphatidylinositol 3-kinase using a novel in vivo assay in yeast. EMBO J. 17, 5374-5387.
    • (1998) EMBO J , vol.17 , pp. 5374-5387
    • Isakoff, S.J.1    Cardozo, T.2    Andreev, J.3    Li, Z.4    Ferguson, K.M.5    Abagyan, R.6    Lemmon, M.A.7    Aronheim, A.8    Skolnik, E.Y.9
  • 27
    • 78149423038 scopus 로고    scopus 로고
    • Formation of salt bridges mediates internal dimerization of myosin VI medial tail domain
    • Kim, H., Hsin, J., Liu, Y., Selvin, P. R. and Schulten, K. (2010). Formation of salt bridges mediates internal dimerization of myosin VI medial tail domain. Structure 18, 1443-1449.
    • (2010) Structure , vol.18 , pp. 1443-1449
    • Kim, H.1    Hsin, J.2    Liu, Y.3    Selvin, P.R.4    Schulten, K.5
  • 29
    • 0038387454 scopus 로고    scopus 로고
    • Do filopodia enable the growth cone to find its way?
    • Koleske, A. J. (2003). Do filopodia enable the growth cone to find its way? Sci. STKE 2003, pe20.
    • (2003) Sci. STKE , vol.2003 , pp. 20
    • Koleske, A.J.1
  • 30
    • 17644397906 scopus 로고    scopus 로고
    • Mechanism of action of myosin X, a membrane-associated molecular motor
    • Kovacs, M., Wang, F. and Sellers, J. R. (2005). Mechanism of action of myosin X, a membrane-associated molecular motor. J. Biol. Chem. 280, 15071-15083.
    • (2005) J. Biol. Chem. , vol.280 , pp. 15071-15083
    • Kovacs, M.1    Wang, F.2    Sellers, J.R.3
  • 31
    • 50049085789 scopus 로고    scopus 로고
    • Mechanisms to suppress multipolar divisions in cancer cells with extra centrosomes
    • Kwon, M., Godinho, S. A., Chandhok, N. S., Ganem, N. J., Azioune, A., Thery, M. and Pellman, D. (2008). Mechanisms to suppress multipolar divisions in cancer cells with extra centrosomes. Genes Dev. 22, 2189-2203.
    • (2008) Genes Dev , vol.22 , pp. 2189-2203
    • Kwon, M.1    Godinho, S.A.2    Chandhok, N.S.3    Ganem, N.J.4    Azioune, A.5    Thery, M.6    Pellman, D.7
  • 32
    • 22944446447 scopus 로고    scopus 로고
    • Actin- and myosin-driven movement of viruses along filopodia precedes their entry into cells
    • Lehmann, M. J., Sherer, N. M., Marks, C. B., Pypaert, M. and Mothes, W. (2005). Actin- and myosin-driven movement of viruses along filopodia precedes their entry into cells. J. Cell Biol. 170, 317-325.
    • (2005) J. Cell Biol. , vol.170 , pp. 317-325
    • Lehmann, M.J.1    Sherer, N.M.2    Marks, C.B.3    Pypaert, M.4    Mothes, W.5
  • 33
    • 79960291022 scopus 로고    scopus 로고
    • Extension of a threehelix bundle domain of myosin VI and key role of calmodulins
    • Liu, Y., Hsin, J., Kim, H., Selvin, P. R. and Schulten, K. (2011). Extension of a threehelix bundle domain of myosin VI and key role of calmodulins. Biophys. J. 100, 2964-2973.
    • (2011) Biophys. J. , vol.100 , pp. 2964-2973
    • Liu, Y.1    Hsin, J.2    Kim, H.3    Selvin, P.R.4    Schulten, K.5
  • 35
    • 2442595175 scopus 로고    scopus 로고
    • The spatial and temporal dynamics of pleckstrin homology domain binding at the plasma membrane measured by imaging single molecules in live mouse myoblasts
    • Mashanov, G. I., Tacon, D., Peckham, M. and Molloy, J. E. (2004). The spatial and temporal dynamics of pleckstrin homology domain binding at the plasma membrane measured by imaging single molecules in live mouse myoblasts. J. Biol. Chem. 279, 15274-15280.
    • (2004) J. Biol. Chem. , vol.279 , pp. 15274-15280
    • Mashanov, G.I.1    Tacon, D.2    Peckham, M.3    Molloy, J.E.4
  • 36
    • 44349179335 scopus 로고    scopus 로고
    • Filopodia: molecular architecture and cellular functions
    • Mattila, P. K. and Lappalainen, P. (2008). Filopodia: molecular architecture and cellular functions. Nat. Rev. Mol. Cell Biol. 9, 446-454.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 446-454
    • Mattila, P.K.1    Lappalainen, P.2
  • 37
    • 77951211165 scopus 로고    scopus 로고
    • Myosin X regulates sealing zone patterning in osteoclasts through linkage of podosomes and microtubules
    • McMichael, B. K., Cheney, R. E. and Lee, B. S. (2010). Myosin X regulates sealing zone patterning in osteoclasts through linkage of podosomes and microtubules. J. Biol. Chem. 285, 9506-9515.
    • (2010) J. Biol. Chem. , vol.285 , pp. 9506-9515
    • McMichael, B.K.1    Cheney, R.E.2    Lee, B.S.3
  • 38
    • 33644775671 scopus 로고    scopus 로고
    • Myosin II functions in actinbundle turnover in neuronal growth cones
    • Medeiros, N. A., Burnette, D. T. and Forscher, P. (2006). Myosin II functions in actinbundle turnover in neuronal growth cones. Nat. Cell Biol. 8, 215-226.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 215-226
    • Medeiros, N.A.1    Burnette, D.T.2    Forscher, P.3
  • 39
    • 77956215275 scopus 로고    scopus 로고
    • Structured post-IQ domain governs selectivity of myosin X for fascin-actin bundles
    • Nagy, S. and Rock, R. S. (2010). Structured post-IQ domain governs selectivity of myosin X for fascin-actin bundles. J. Biol. Chem. 285, 26608-26617.
    • (2010) J. Biol. Chem. , vol.285 , pp. 26608-26617
    • Nagy, S.1    Rock, R.S.2
  • 41
    • 77950613612 scopus 로고    scopus 로고
    • Myosin motor function: the ins and outs of actin-based membrane protrusions
    • Nambiar, R., McConnell, R. E. and Tyska, M. J. (2010). Myosin motor function: the ins and outs of actin-based membrane protrusions. Cell. Mol. Life Sci. 67, 1239-1254.
    • (2010) Cell. Mol. Life Sci. , vol.67 , pp. 1239-1254
    • Nambiar, R.1    McConnell, R.E.2    Tyska, M.J.3
  • 42
    • 0032100916 scopus 로고    scopus 로고
    • Characterization of microtubule binding domains in the Arabidopsis kinesin-like calmodulin binding protein
    • Narasimhulu, S. B. and Reddy, A. S. (1998). Characterization of microtubule binding domains in the Arabidopsis kinesin-like calmodulin binding protein. Plant Cell 10, 957-965.
    • (1998) Plant Cell , vol.10 , pp. 957-965
    • Narasimhulu, S.B.1    Reddy, A.S.2
  • 43
    • 70349783561 scopus 로고    scopus 로고
    • Myosin-X is critical for migratory ability of Xenopus cranial neural crest cells
    • Nie, S., Kee, Y. and Bronner-Fraser, M. (2009). Myosin-X is critical for migratory ability of Xenopus cranial neural crest cells. Dev. Biol. 335, 132-142.
    • (2009) Dev. Biol. , vol.335 , pp. 132-142
    • Nie, S.1    Kee, Y.2    Bronner-Fraser, M.3
  • 44
    • 37549069575 scopus 로고    scopus 로고
    • Drawing the tree of eukaryotic life based on the analysis of 2, 269 manually annotated myosins from 328 species
    • Odronitz, F. and Kollmar, M. (2007). Drawing the tree of eukaryotic life based on the analysis of 2,269 manually annotated myosins from 328 species. Genome Biol. 8, R196.
    • (2007) Genome Biol , vol.8
    • Odronitz, F.1    Kollmar, M.2
  • 46
    • 42949124488 scopus 로고    scopus 로고
    • Comprehensive identification of PIP3-regulated PH domains from C. elegans to H. sapiens by model prediction and live imaging
    • Park, W. S., Heo, W. D., Whalen, J. H., O'Rourke, N. A., Bryan, H. M., Meyer, T. and Teruel, M. N. (2008). Comprehensive identification of PIP3-regulated PH domains from C. elegans to H. sapiens by model prediction and live imaging. Mol. Cell 30, 381-392.
    • (2008) Mol. Cell , vol.30 , pp. 381-392
    • Park, W.S.1    Heo, W.D.2    Whalen, J.H.3    O'Rourke, N.A.4    Bryan, H.M.5    Meyer, T.6    Teruel, M.N.7
  • 47
    • 70349266063 scopus 로고    scopus 로고
    • When a predicted coiled coil is really a single α-helix, in myosins and other proteins
    • Peckham, M. and Knight, P. J. (2009). When a predicted coiled coil is really a single α-helix, in myosins and other proteins. Soft Matter 5, 2493-2503.
    • (2009) Soft Matter , vol.5 , pp. 2493-2503
    • Peckham, M.1    Knight, P.J.2
  • 48
    • 38049037417 scopus 로고    scopus 로고
    • Sequential roles for myosin-X in BMP6-dependent filopodial extension, migration, and activation of BMP receptors
    • Pi, X., Ren, R., Kelley, R., Zhang, C., Moser, M., Bohil, A. B., Divito, M., Cheney, R. E. and Patterson, C. (2007). Sequential roles for myosin-X in BMP6-dependent filopodial extension, migration, and activation of BMP receptors. J. Cell Biol. 179, 1569-1582.
    • (2007) J. Cell Biol. , vol.179 , pp. 1569-1582
    • Pi, X.1    Ren, R.2    Kelley, R.3    Zhang, C.4    Moser, M.5    Bohil, A.B.6    Divito, M.7    Cheney, R.E.8    Patterson, C.9
  • 49
    • 77957874785 scopus 로고    scopus 로고
    • PtdIns(3,4,5)P is a regulator of myosin-X localization and filopodia formation
    • Plantard, L., Arjonen, A., Lock, J. G., Nurani, G., Ivaska, J. and Stromblad, S. (2010). PtdIns(3,4,5)P is a regulator of myosin-X localization and filopodia formation. J. Cell Sci. 123, 3525-3534.
    • (2010) J. Cell Sci. , vol.123 , pp. 3525-3534
    • Plantard, L.1    Arjonen, A.2    Lock, J.G.3    Nurani, G.4    Ivaska, J.5    Stromblad, S.6
  • 50
    • 0042626585 scopus 로고    scopus 로고
    • Activity-regulated dynamic behavior of early dendritic protrusions: evidence for different types of dendritic filopodia
    • Portera-Cailliau, C., Pan, D. T. and Yuste, R. (2003). Activity-regulated dynamic behavior of early dendritic protrusions: evidence for different types of dendritic filopodia. J. Neurosci. 23, 7129-7142.
    • (2003) J. Neurosci. , vol.23 , pp. 7129-7142
    • Portera-Cailliau, C.1    Pan, D.T.2    Yuste, R.3
  • 51
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner, M. and Rogers, S. W. (1996). PEST sequences and regulation by proteolysis. Trends Biochem. Sci. 21, 267-271.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 52
    • 77957334369 scopus 로고    scopus 로고
    • The stepping pattern of myosin X is adapted for processive motility on bundled actin
    • Ricca, B. L. and Rock, R. S. (2010). The stepping pattern of myosin X is adapted for processive motility on bundled actin. Biophys. J. 99, 1818-1826.
    • (2010) Biophys. J. , vol.99 , pp. 1818-1826
    • Ricca, B.L.1    Rock, R.S.2
  • 53
    • 0035853701 scopus 로고    scopus 로고
    • The tumor-sensitive calmodulin-like protein is a specific light chain of human unconventional myosin X
    • Rogers, M. S. and Strehler, E. E. (2001). The tumor-sensitive calmodulin-like protein is a specific light chain of human unconventional myosin X. J. Biol. Chem. 276, 12182-12189.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12182-12189
    • Rogers, M.S.1    Strehler, E.E.2
  • 54
    • 79955550621 scopus 로고    scopus 로고
    • Cargo binding activates myosin VIIA motor function in cells
    • Sakai, T., Umeki, N., Ikebe, R. and Ikebe, M. (2011). Cargo binding activates myosin VIIA motor function in cells. Proc. Natl. Acad. Sci. USA 108, 7028-7033.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 7028-7033
    • Sakai, T.1    Umeki, N.2    Ikebe, R.3    Ikebe, M.4
  • 56
    • 77951771838 scopus 로고    scopus 로고
    • Actin, microtubules, and vimentin intermediate filaments cooperate for elongation of invadopodia
    • Schoumacher, M., Goldman, R. D., Louvard, D. and Vignjevic, D. M. (2010). Actin, microtubules, and vimentin intermediate filaments cooperate for elongation of invadopodia. J. Cell Biol. 189, 541-556.
    • (2010) J. Cell Biol. , vol.189 , pp. 541-556
    • Schoumacher, M.1    Goldman, R.D.2    Louvard, D.3    Vignjevic, D.M.4
  • 57
    • 49849101970 scopus 로고    scopus 로고
    • Cytonemes and tunneling nanotubules in cell-cell communication and viral pathogenesis
    • Sherer, N. M. and Mothes, W. (2008). Cytonemes and tunneling nanotubules in cell-cell communication and viral pathogenesis. Trends Cell Biol. 18, 414-420.
    • (2008) Trends Cell Biol , vol.18 , pp. 414-420
    • Sherer, N.M.1    Mothes, W.2
  • 59
    • 77957828597 scopus 로고    scopus 로고
    • Melanin transfer in human skin cells is mediated by filopodia-a model for homotypic and heterotypic lysosome-related organelle transfer
    • Singh, S. K., Kurfurst, R., Nizard, C., Schnebert, S., Perrier, E. and Tobin, D. J. (2010). Melanin transfer in human skin cells is mediated by filopodia-a model for homotypic and heterotypic lysosome-related organelle transfer. FASEB J. 24, 3756-3769.
    • (2010) FASEB J , vol.24 , pp. 3756-3769
    • Singh, S.K.1    Kurfurst, R.2    Nizard, C.3    Schnebert, S.4    Perrier, E.5    Tobin, D.J.6
  • 60
    • 38049082269 scopus 로고    scopus 로고
    • Expression of unconventional myosin genes during neuronal development in zebrafish
    • Sittaramane, V. and Chandrasekhar, A. (2008). Expression of unconventional myosin genes during neuronal development in zebrafish. Gene Expr. Patterns 8, 161-170.
    • (2008) Gene Expr. Patterns , vol.8 , pp. 161-170
    • Sittaramane, V.1    Chandrasekhar, A.2
  • 61
    • 51649115555 scopus 로고    scopus 로고
    • Dynamic charge interactions create surprising rigidity in the ER/K alpha-helical protein motif
    • Sivaramakrishnan, S., Spink, B. J., Sim, A. Y., Doniach, S. and Spudich, J. A. (2008). Dynamic charge interactions create surprising rigidity in the ER/K alpha-helical protein motif. Proc. Natl. Acad. Sci. USA 105, 13356-13361.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 13356-13361
    • Sivaramakrishnan, S.1    Spink, B.J.2    Sim, A.Y.3    Doniach, S.4    Spudich, J.A.5
  • 62
    • 0003154314 scopus 로고
    • Molecular cloning of myosins from the bullfrog saccular macula: a candidate for the hair cell adaptation motor
    • Solc, C. K., Derfler, B. H., Duyk, G. M. and Corey, D. P. (1994). Molecular cloning of myosins from the bullfrog saccular macula: a candidate for the hair cell adaptation motor. Auditory Neurosci. 1, 63-75.
    • (1994) Auditory Neurosci , vol.1 , pp. 63-75
    • Solc, C.K.1    Derfler, B.H.2    Duyk, G.M.3    Corey, D.P.4
  • 63
    • 25844435342 scopus 로고    scopus 로고
    • Myosin-X: a molecular motor at the cell's fingertips
    • Sousa, A. D. and Cheney, R. E. (2005). Myosin-X: a molecular motor at the cell's fingertips. Trends Cell Biol. 15, 533-539.
    • (2005) Trends Cell Biol , vol.15 , pp. 533-539
    • Sousa, A.D.1    Cheney, R.E.2
  • 64
    • 31644448163 scopus 로고    scopus 로고
    • Myo10 in brain: developmental regulation, identification of a headless isoform and dynamics in neurons
    • Sousa, A. D., Berg, J. S., Robertson, B. W., Meeker, R. B. and Cheney, R. E. (2006). Myo10 in brain: developmental regulation, identification of a headless isoform and dynamics in neurons. J. Cell Sci. 119, 184-194.
    • (2006) J. Cell Sci. , vol.119 , pp. 184-194
    • Sousa, A.D.1    Berg, J.S.2    Robertson, B.W.3    Meeker, R.B.4    Cheney, R.E.5
  • 65
    • 44849116355 scopus 로고    scopus 로고
    • Long single alpha-helical tail domains bridge the gap between structure and function of myosin VI
    • Spink, B. J., Sivaramakrishnan, S., Lipfert, J., Doniach, S. and Spudich, J. A. (2008). Long single alpha-helical tail domains bridge the gap between structure and function of myosin VI. Nat. Struct. Mol. Biol. 15, 591-597.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 591-597
    • Spink, B.J.1    Sivaramakrishnan, S.2    Lipfert, J.3    Doniach, S.4    Spudich, J.A.5
  • 66
    • 79955925397 scopus 로고    scopus 로고
    • Unique sequences and predicted functions of myosins in Tetrahymena thermophila
    • Sugita, M., Iwataki, Y., Nakano, K. and Numata, O. (2011). Unique sequences and predicted functions of myosins in Tetrahymena thermophila. Gene 480, 10-20.
    • (2011) Gene , vol.480 , pp. 10-20
    • Sugita, M.1    Iwataki, Y.2    Nakano, K.3    Numata, O.4
  • 67
    • 80052429807 scopus 로고    scopus 로고
    • Lever-arm mechanics of processive myosins
    • Sun, Y. and Goldman, Y. E. (2011). Lever-arm mechanics of processive myosins. Biophys. J. 101, 1-11.
    • (2011) Biophys. J. , vol.101 , pp. 1-11
    • Sun, Y.1    Goldman, Y.E.2
  • 70
    • 2442718690 scopus 로고    scopus 로고
    • Myosin X transports Mena/VASP to the tip of filopodia
    • Tokuo, H. and Ikebe, M. (2004). Myosin X transports Mena/VASP to the tip of filopodia. Biochem. Biophys. Res. Commun. 319, 214-220.
    • (2004) Biochem. Biophys. Res. Commun. , vol.319 , pp. 214-220
    • Tokuo, H.1    Ikebe, M.2
  • 71
    • 35548932103 scopus 로고    scopus 로고
    • The motor activity of myosin-X promotes actin fiber convergence at the cell periphery to initiate filopodia formation
    • Tokuo, H., Mabuchi, K. and Ikebe, M. (2007). The motor activity of myosin-X promotes actin fiber convergence at the cell periphery to initiate filopodia formation. J. Cell Biol. 179, 229-238.
    • (2007) J. Cell Biol. , vol.179 , pp. 229-238
    • Tokuo, H.1    Mabuchi, K.2    Ikebe, M.3
  • 72
    • 0037183926 scopus 로고    scopus 로고
    • Conversion of Unc104/KIF1A kinesin into a processive motor after dimerization
    • Tomishige, M., Klopfenstein, D. R. and Vale, R. D. (2002). Conversion of Unc104/KIF1A kinesin into a processive motor after dimerization. Science 297, 2263-2267.
    • (2002) Science , vol.297 , pp. 2263-2267
    • Tomishige, M.1    Klopfenstein, D.R.2    Vale, R.D.3
  • 73
    • 33947596005 scopus 로고    scopus 로고
    • Integrin-mediated adhesion orients the spindle parallel to the substratum in an EB1- and myosin X-dependent manner
    • Toyoshima, F. and Nishida, E. (2007). Integrin-mediated adhesion orients the spindle parallel to the substratum in an EB1- and myosin X-dependent manner. EMBO J. 26, 1487-1498.
    • (2007) EMBO J , vol.26 , pp. 1487-1498
    • Toyoshima, F.1    Nishida, E.2
  • 79
    • 67349174269 scopus 로고    scopus 로고
    • Involvement of headless myosin X in the motility of immortalized gonadotropin-releasing hormone neuronal cells
    • Wang, J. J., Fu, X. Q., Guo, Y. G., Yuan, L., Gao, Q. Q., Yu, H. L., Shi, H. L., Wang, X. Z., Xiong, W. C. and Zhu, X. J. (2009). Involvement of headless myosin X in the motility of immortalized gonadotropin-releasing hormone neuronal cells. Cell Biol. Int. 33, 578-585.
    • (2009) Cell Biol. Int. , vol.33 , pp. 578-585
    • Wang, J.J.1    Fu, X.Q.2    Guo, Y.G.3    Yuan, L.4    Gao, Q.Q.5    Yu, H.L.6    Shi, H.L.7    Wang, X.Z.8    Xiong, W.C.9    Zhu, X.J.10
  • 80
    • 77953509417 scopus 로고    scopus 로고
    • Myosin-X induces filopodia by multiple elongation mechanism
    • Watanabe, T. M., Tokuo, H., Gonda, K., Higuchi, H. and Ikebe, M. (2010). Myosin-X induces filopodia by multiple elongation mechanism. J. Biol. Chem. 285, 19605-19614.
    • (2010) J. Biol. Chem. , vol.285 , pp. 19605-19614
    • Watanabe, T.M.1    Tokuo, H.2    Gonda, K.3    Higuchi, H.4    Ikebe, M.5
  • 81
    • 4644326930 scopus 로고    scopus 로고
    • A microtubule-binding myosin required for nuclear anchoring and spindle assembly
    • Weber, K. L., Sokac, A. M., Berg, J. S., Cheney, R. E. and Bement, W. M. (2004). A microtubule-binding myosin required for nuclear anchoring and spindle assembly. Nature 431, 325-329.
    • (2004) Nature , vol.431 , pp. 325-329
    • Weber, K.L.1    Sokac, A.M.2    Berg, J.S.3    Cheney, R.E.4    Bement, W.M.5
  • 82
    • 79952761581 scopus 로고    scopus 로고
    • Cargo recognition mechanism of myosin X revealed by the structure of its tail MyTH4-FERM tandem in complex with the DCC P3 domain
    • Wei, Z., Yan, J., Lu, Q., Pan, L. and Zhang, M. (2011). Cargo recognition mechanism of myosin X revealed by the structure of its tail MyTH4-FERM tandem in complex with the DCC P3 domain. Proc. Natl. Acad. Sci. USA 108, 3572-3577.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 3572-3577
    • Wei, Z.1    Yan, J.2    Lu, Q.3    Pan, L.4    Zhang, M.5
  • 85
    • 47549089279 scopus 로고    scopus 로고
    • Myosin-10 and actin filaments are essential for mitotic spindle function
    • Woolner, S., O'Brien, L. L., Wiese, C. and Bement, W. M. (2008). Myosin-10 and actin filaments are essential for mitotic spindle function. J. Cell Biol. 182, 77-88.
    • (2008) J. Cell Biol. , vol.182 , pp. 77-88
    • Woolner, S.1    O'Brien, L.L.2    Wiese, C.3    Bement, W.M.4
  • 86
    • 79951506483 scopus 로고    scopus 로고
    • Structure of MyTH4-FERM domains in myosin VIIa tail bound to cargo
    • Wu, L., Pan, L., Wei, Z. and Zhang, M. (2011). Structure of MyTH4-FERM domains in myosin VIIa tail bound to cargo. Science 331, 757-760.
    • (2011) Science , vol.331 , pp. 757-760
    • Wu, L.1    Pan, L.2    Wei, Z.3    Zhang, M.4
  • 87
    • 53249124706 scopus 로고    scopus 로고
    • Mitosis: new roles for myosin-X and actin at the spindle
    • Wuhr, M., Mitchison, T. J. and Field, C. M. (2008). Mitosis: new roles for myosin-X and actin at the spindle. Curr. Biol. 18, R912-R914.
    • (2008) Curr. Biol. , vol.18
    • Wuhr, M.1    Mitchison, T.J.2    Field, C.M.3
  • 90
    • 0038670331 scopus 로고    scopus 로고
    • Possible involvement of myosin-X in intercellular adhesion: importance of serial pleckstrin homology regions for intracellular localization
    • Yonezawa, S., Yoshizaki, N., Sano, M., Hanai, A., Masaki, S., Takizawa, T., Kageyama, T. and Moriyama, A. (2003). Possible involvement of myosin-X in intercellular adhesion: importance of serial pleckstrin homology regions for intracellular localization. Dev. Growth Differ. 45, 175-185.
    • (2003) Dev. Growth Differ. , vol.45 , pp. 175-185
    • Yonezawa, S.1    Yoshizaki, N.2    Sano, M.3    Hanai, A.4    Masaki, S.5    Takizawa, T.6    Kageyama, T.7    Moriyama, A.8
  • 91
    • 68049105404 scopus 로고    scopus 로고
    • Myosin VI undergoes cargo-mediated dimerization
    • Yu, C., Feng, W., Wei, Z., Miyanoiri, Y., Wen, W., Zhao, Y. and Zhang, M. (2009). Myosin VI undergoes cargo-mediated dimerization. Cell 138, 537-548.
    • (2009) Cell , vol.138 , pp. 537-548
    • Yu, C.1    Feng, W.2    Wei, Z.3    Miyanoiri, Y.4    Wen, W.5    Zhao, Y.6    Zhang, M.7
  • 94
    • 67650899090 scopus 로고    scopus 로고
    • Molecular noise of capping protein binding induces macroscopic instability in filopodial dynamics
    • Zhuravlev, P. I. and Papoian, G. A. (2009). Molecular noise of capping protein binding induces macroscopic instability in filopodial dynamics. Proc. Natl. Acad. Sci. USA 106, 11570-11575.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 11570-11575
    • Zhuravlev, P.I.1    Papoian, G.A.2
  • 95
    • 77951647952 scopus 로고    scopus 로고
    • Design of active transport must be highly intricate: a possible role of myosin and Ena/VASP for G-actin transport in filopodia
    • Zhuravlev, P. I., Der, B. S. and Papoian, G. A. (2010). Design of active transport must be highly intricate: a possible role of myosin and Ena/VASP for G-actin transport in filopodia. Biophys. J. 98, 1439-1448.
    • (2010) Biophys. J. , vol.98 , pp. 1439-1448
    • Zhuravlev, P.I.1    Der, B.S.2    Papoian, G.A.3


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