메뉴 건너뛰기




Volumn 287, Issue 18, 2012, Pages 14923-14936

Molecular basis of dynamic relocalization of Dictyostelium Myosin IB

Author keywords

[No Author keywords available]

Indexed keywords

ACANTHAMOEBA; ACIDIC PHOSPHOLIPIDS; ACTIN-BINDING SITES; ATP-ASE ACTIVITY; BISPHOSPHATES; CELL-CELL CONTACT; CLASS I; DICTYOSTELIUM; DYNAMIC LOCALIZATION; F-ACTIN; HEAVY CHAIN; HYDROPHOBIC AMINO ACIDS; IN-VITRO; IN-VIVO; LIVE CELL; MOLECULAR BASIS; MOTOR ACTIVITY; MOTOR DOMAIN; N-TERMINALS; PHOSPHOINOSITIDES; POLARIZED CELLS; RE-LOCALIZATION; RESTING CELLS; SHORT SEQUENCES;

EID: 84860365174     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.318667     Document Type: Article
Times cited : (13)

References (85)
  • 2
    • 47749143279 scopus 로고    scopus 로고
    • Myosin I: From yeast to human
    • Kim, S. V., and Flavell, R. A. (2008) Myosin I: from yeast to human. Cell. Mol. Life Sci. 65, 2128-2137
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 2128-2137
    • Kim, S.V.1    Flavell, R.A.2
  • 3
    • 74849099389 scopus 로고    scopus 로고
    • Coluccio, L. M., ed Springer, Dordrecht, The Netherlands
    • Coluccio L. (2008) in Myosins: A Superfamily of Molecular Motors (Coluccio, L. M., ed) pp. 95-124, Springer, Dordrecht, The Netherlands
    • (2008) Myosins: A Superfamily of Molecular Motors , pp. 95-124
    • Coluccio, L.1
  • 4
    • 0035869375 scopus 로고    scopus 로고
    • Regulation of Dictyostelium myosin I and II
    • de la Roche, M. A., and Côté, G. P. (2001) Regulation of Dictyostelium myosin I and II. Biochim. Biophys. Acta 1525, 245-261
    • (2001) Biochim. Biophys. Acta , vol.1525 , pp. 245-261
    • De La Roche, M.A.1    Côté, G.P.2
  • 5
    • 33750515229 scopus 로고    scopus 로고
    • Myo1c binds phosphoinositides through a putative pleckstrin homology domain
    • DOI 10.1091/mbc.E06-05-0449
    • Hokanson, D. E., Laakso, J. M., Lin, T., Sept, D., and Ostap, E. M. (2006) Myo1c binds phosphoinositides through a putative pleckstrin homology domain. Mol. Biol. Cell 17, 4856-4865 (Pubitemid 44665754)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.11 , pp. 4856-4865
    • Hokanson, D.E.1    Laakso, J.M.2    Lin, T.3    Sept, D.4    Ostap, E.M.5
  • 6
    • 74249105441 scopus 로고    scopus 로고
    • Myosin 1G (Myo1G) is a haematopoietic specific myosin that localises to the plasma membrane and regulates cell elasticity
    • Olety, B., Wälte, M., Honnert, U., Schillers, H., and Bähler, M. (2010) Myosin 1G (Myo1G) is a haematopoietic specific myosin that localises to the plasma membrane and regulates cell elasticity. FEBS Lett. 584, 493-499
    • (2010) FEBS Lett. , vol.584 , pp. 493-499
    • Olety, B.1    Wälte, M.2    Honnert, U.3    Schillers, H.4    Bähler, M.5
  • 7
    • 77950573946 scopus 로고    scopus 로고
    • Myosin 1G is an abundant class I myosin in lymphocytes whose localization at the plasma membrane depends on its ancient divergent pleckstrin homology (PH) domain (Myo1PH)
    • Patino-Lopez, G., Aravind, L., Dong, X., Kruhlak, M. J., Ostap, E. M., and Shaw, S. (2010) Myosin 1G is an abundant class I myosin in lymphocytes whose localization at the plasma membrane depends on its ancient divergent pleckstrin homology (PH) domain (Myo1PH). J. Biol. Chem. 285, 8675-8686
    • (2010) J. Biol. Chem. , vol.285 , pp. 8675-8686
    • Patino-Lopez, G.1    Aravind, L.2    Dong, X.3    Kruhlak, M.J.4    Ostap, E.M.5    Shaw, S.6
  • 9
    • 57649133951 scopus 로고    scopus 로고
    • Acanthamoeba myosin IC colocalizes with phosphatidylinositol 4,5-bisphosphate at the plasma membrane due to the high concentration of negative charge
    • Brzeska, H., Hwang, K. J., and Korn, E. D. (2008) Acanthamoeba myosin IC colocalizes with phosphatidylinositol 4,5-bisphosphate at the plasma membrane due to the high concentration of negative charge. J. Biol. Chem. 283, 32014-32023
    • (2008) J. Biol. Chem. , vol.283 , pp. 32014-32023
    • Brzeska, H.1    Hwang, K.J.2    Korn, E.D.3
  • 10
    • 77949319432 scopus 로고    scopus 로고
    • An experimentally based computer search identifies unstructured membrane binding sites in proteins: Application to class I myosins, PAKS, and CARMIL
    • Brzeska, H., Guag, J., Remmert, K., Chacko, S., and Korn, E. D. (2010) An experimentally based computer search identifies unstructured membrane binding sites in proteins: application to class I myosins, PAKS, and CARMIL. J. Biol. Chem. 285, 5738-5747
    • (2010) J. Biol. Chem. , vol.285 , pp. 5738-5747
    • Brzeska, H.1    Guag, J.2    Remmert, K.3    Chacko, S.4    Korn, E.D.5
  • 11
    • 78049263512 scopus 로고    scopus 로고
    • Myo1e binds anionic phospholipids with high affinity
    • Feeser, E. A., Ignacio, C. M., Krendel, M., and Ostap, E. M. (2010) Myo1e binds anionic phospholipids with high affinity. Biochemistry 49, 9353-9360
    • (2010) Biochemistry , vol.49 , pp. 9353-9360
    • Feeser, E.A.1    Ignacio, C.M.2    Krendel, M.3    Ostap, E.M.4
  • 12
    • 70350367835 scopus 로고    scopus 로고
    • Collective cell migration in development
    • Weijer, C. J. (2009) Collective cell migration in development. J. Cell Sci. 122, 3215-3223
    • (2009) J. Cell Sci. , vol.122 , pp. 3215-3223
    • Weijer, C.J.1
  • 13
    • 44449172361 scopus 로고    scopus 로고
    • Directional sensing during chemotaxis
    • Janetopoulos, C., and Firtel, R. A. (2008) Directional sensing during chemotaxis. FEBS Lett. 582, 2075-2085
    • (2008) FEBS Lett. , vol.582 , pp. 2075-2085
    • Janetopoulos, C.1    Firtel, R.A.2
  • 16
    • 0025371423 scopus 로고
    • Generation and characterization of Dictyostelium cells deficient in a myosin I heavy chain isoform
    • Jung, G., and Hammer, J. A., 3rd (1990) Generation and characterization of Dictyostelium cells deficient in a myosin I heavy chain isoform. J. Cell Biol. 110, 1955-1964
    • (1990) J. Cell Biol. , vol.110 , pp. 1955-1964
    • Jung, G.1    Hammer III, J.A.2
  • 17
    • 0031933790 scopus 로고    scopus 로고
    • The myosin I SH3 domain and TEDS rule phosphorylation site are required for in vivo function
    • Novak, K. D., and Titus, M. A. (1998) The myosin I SH3 domain and TEDS rule phosphorylation site are required for in vivo function. Mol. Biol. Cell 9, 75-88 (Pubitemid 28065282)
    • (1998) Molecular Biology of the Cell , vol.9 , Issue.1 , pp. 75-88
    • Novak, K.D.1    Titus, M.A.2
  • 18
    • 0024956931 scopus 로고
    • Myosin I is located at the leading edges of locomoting Dictyostelium amoebae
    • DOI 10.1038/341328a0
    • Fukui, Y., Lynch, T. J., Brzeska, H., and Korn, E. D. (1989) Myosin I is located at the leading edges of locomoting Dictyostelium amoebae. Nature 341, 328-331 (Pubitemid 20102101)
    • (1989) Nature , vol.341 , Issue.6240 , pp. 328-331
    • Fukui, Y.1    Lynch, T.J.2    Brzeska, H.3    Korn, E.D.4
  • 19
    • 0029857607 scopus 로고    scopus 로고
    • Localization of Dictyostelium myoB and myoD to filopodia and cell-cell contact sites using isoform-specific antibodies
    • Morita, Y. S., Jung, G., Hammer, J. A., 3rd, and Fukui, Y. (1996) Localization of Dictyostelium myoB and myoD to filopodia and cell-cell contact sites using isoform-specific antibodies. Eur. J. Cell Biol. 71, 371-379 (Pubitemid 26420047)
    • (1996) European Journal of Cell Biology , vol.71 , Issue.4 , pp. 371-379
    • Morita, Y.S.1    Jung, G.2    Hammer III, J.A.3    Fukui, Y.4
  • 20
    • 0028838302 scopus 로고
    • Dictyostelium myosin I double mutants exhibit conditional defects in pinocytosis
    • Novak, K. D., Peterson, M. D., Reedy, M. C., and Titus, M. A. (1995) Dictyostelium myosin I double mutants exhibit conditional defects in pinocytosis. J. Cell Biol. 131, 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
  • 21
    • 0033635977 scopus 로고    scopus 로고
    • Green fluorescent protein and epitope tag fusion vectors for Dictyostelium discoideum
    • Levi, S., Polyakov, M., and Egelhoff, T. T. (2000) Green fluorescent protein and epitope tag fusion vectors for Dictyostelium discoideum. Plasmid 44, 231-238
    • (2000) Plasmid , vol.44 , pp. 231-238
    • Levi, S.1    Polyakov, M.2    Egelhoff, T.T.3
  • 22
    • 0029040241 scopus 로고
    • A novel positive selection for identifying cold-sensitive myosin II mutants in Dictyostelium
    • Patterson, B., and Spudich, J. A. (1995) A novel positive selection for identifying cold-sensitive myosin II mutants in Dictyostelium. Genetics 140, 505-515
    • (1995) Genetics , vol.140 , pp. 505-515
    • Patterson, B.1    Spudich, J.A.2
  • 23
    • 12544249887 scopus 로고    scopus 로고
    • ThePI3K-mediated activation of CRAC independently regulates adenylyl cyclase activation and chemotaxis
    • Comer, F. I., Lippincott, C. K., Masbad, J. J., and Parent, C. A. (2005) ThePI3K-mediated activation of CRAC independently regulates adenylyl cyclase activation and chemotaxis. Curr. Biol. 15, 134-139
    • (2005) Curr. Biol. , vol.15 , pp. 134-139
    • Comer, F.I.1    Lippincott, C.K.2    Masbad, J.J.3    Parent, C.A.4
  • 24
    • 0023073916 scopus 로고
    • Cultivation and synchronous morphogenesis of Dictyostelium under controlled experimental conditions
    • Sussman, M. (1987) Cultivation and synchronous morphogenesis of Dictyostelium under controlled experimental conditions. Methods Cell Biol. 28, 9-29
    • (1987) Methods Cell Biol. , vol.28 , pp. 9-29
    • Sussman, M.1
  • 25
    • 34247361650 scopus 로고    scopus 로고
    • Chemotaxis in the Absence of PIP3 Gradients
    • DOI 10.1016/j.cub.2007.04.004, PII S0960982207012109
    • Hoeller, O., and Kay, R. R. (2007) Chemotaxis in the absence of PIP3 gradients. Curr. Biol. 17, 813-817 (Pubitemid 46635122)
    • (2007) Current Biology , vol.17 , Issue.9 , pp. 813-817
    • Hoeller, O.1    Kay, R.R.2
  • 26
    • 0001462976 scopus 로고    scopus 로고
    • Use of a fusion protein between GFP and an actin-binding domain to visualize transient filamentous-actin structures
    • Pang, K. M., Lee, E., and Knecht, D. A. (1998) Use of a fusion protein between GFP and an actin binding domain to visualize transient filamentous-actin structures. Curr. Biol. 8, 405-408 (Pubitemid 28173999)
    • (1998) Current Biology , vol.8 , Issue.7 , pp. 405-408
    • Pang, K.M.1    Lee, E.2    Knecht, D.A.3
  • 27
    • 0031045035 scopus 로고    scopus 로고
    • Myosin I overexpression impairs cell migration
    • DOI 10.1083/jcb.136.3.633
    • Novak, K. D., and Titus, M. A. (1997) Myosin I overexpression impairs cell migration. J. Cell Biol. 136, 633-647 (Pubitemid 27083764)
    • (1997) Journal of Cell Biology , vol.136 , Issue.3 , pp. 633-647
    • Novak, K.D.1    Titus, M.A.2
  • 28
    • 0029925627 scopus 로고    scopus 로고
    • Dictyostelium mutants lacking multiple classic myosin I isoforms reveal combinations of shared and distinct functions
    • DOI 10.1083/jcb.133.2.305
    • Jung, G., Wu, X., and Hammer, J. A., 3rd (1996) Dictyostelium mutants lacking multiple classic myosin I isoforms reveal combinations of shared and distinct functions. J. Cell Biol. 133, 305-323 (Pubitemid 26131615)
    • (1996) Journal of Cell Biology , vol.133 , Issue.2 , pp. 305-323
    • Jung, G.1    Wu, X.2    Hammer III, J.A.3
  • 29
    • 0043132952 scopus 로고    scopus 로고
    • Shared, unique and redundant functions of three members of the class I myosins (MyoA, MyoB, and MyoF) in motility and chemotaxis in Dictyostelium
    • DOI 10.1242/jcs.00696
    • Falk, D. L., Wessels, D., Jenkins, L., Pham, T., Kuhl, S., Titus, M. A., and Soll, D. R. (2003) Shared, unique and redundant functions of three members of the class I myosins (MyoA, MyoB, and MyoF) in motility and chemotaxis in Dictyostelium. J. Cell Sci. 116, 3985-3999 (Pubitemid 37279313)
    • (2003) Journal of Cell Science , vol.116 , Issue.19 , pp. 3985-3999
    • Falk, D.L.1    Wessels, D.2    Jenkins, L.3    Pham, T.4    Kuhl, S.5    Titus, M.A.6    Soll, D.R.7
  • 30
    • 3042847368 scopus 로고    scopus 로고
    • Rac-induced increase of phosphorylation of myosin regulatory light chain in HeLa cells
    • DOI 10.1002/cm.20009
    • Brzeska, H., Szczepanowska, J., Matsumura, F., and Korn, E. D. (2004) Rac-induced increase of phosphorylation of myosin regulatory light chain in HeLa cells. Cell Motil. Cytoskeleton 58, 186-199 (Pubitemid 38849956)
    • (2004) Cell Motility and the Cytoskeleton , vol.58 , Issue.3 , pp. 186-199
    • Brzeska, H.1    Szczepanowska, J.2    Matsumura, F.3    Korn, E.D.4
  • 31
    • 34250765348 scopus 로고    scopus 로고
    • Transformation of Dictyostelium discoideum with plasmid DNA
    • DOI 10.1038/nprot.2007.179, PII NPROT.2007.179
    • Gaudet, P., Pilcher, K. E., Fey, P., and Chisholm, R. L. (2007) Transformation of Dictyostelium discoideum with plasmid DNA. Nat. Protoc. 2, 1317-1324 (Pubitemid 46952312)
    • (2007) Nature Protocols , vol.2 , Issue.6 , pp. 1317-1324
    • Gaudet, P.1    Pilcher, K.E.2    Fey, P.3    Chisholm, R.L.4
  • 32
    • 52649143876 scopus 로고    scopus 로고
    • Eukaryotic chemotaxis at a glance
    • Bagorda, A., and Parent, C. A. (2008) Eukaryotic chemotaxis at a glance. J. Cell Sci. 121, 2621-2624
    • (2008) J. Cell Sci. , vol.121 , pp. 2621-2624
    • Bagorda, A.1    Parent, C.A.2
  • 33
    • 0035954433 scopus 로고    scopus 로고
    • The Dictyostelium CARMIL protein links capping protein and the Arp2/3 complex to type I myosins through their SH3 domains
    • DOI 10.1083/jcb.153.7.1479
    • Jung, G., Remmert, K., Wu, X., Volosky, J. M., and Hammer, J. A., 3rd (2001) The Dictyostelium CARMIL protein links capping protein and the Arp2/3 complex to type I myosins through their SH3 domains. J. Cell Biol. 153, 1479-1497 (Pubitemid 34286131)
    • (2001) Journal of Cell Biology , vol.153 , Issue.7 , pp. 1479-1497
    • Jung, G.1    Remmert, K.2    Wu, X.3    Volosky, J.M.4    Hammer III, J.A.5
  • 34
    • 0028231727 scopus 로고
    • The GPQ-rich segment of Dictyostelium myosin IB contains an actin binding site
    • Rosenfeld, S. S., and Rener, B. (1994) The GPQ-rich segment of Dictyostelium myosin IB contains an actin binding site. Biochemistry 33, 2322-2328 (Pubitemid 24099634)
    • (1994) Biochemistry , vol.33 , Issue.8 , pp. 2322-2328
    • Rosenfeld, S.S.1    Rener, B.2
  • 35
    • 0024971666 scopus 로고
    • The localization and sequence of the phosphorylation sites of Acanthamoeba myosins I: An improved method for locating the phosphorylated amino acid
    • Brzeska, H., Lynch, T. J., Martin, B., and Korn, E. D. (1989) The localization and sequence of the phosphorylation sites of Acanthamoeba myosins I: an improved method for locating the phosphorylated amino acid. J. Biol. Chem. 264, 19340-19348
    • (1989) J. Biol. Chem. , vol.264 , pp. 19340-19348
    • Brzeska, H.1    Lynch, T.J.2    Martin, B.3    Korn, E.D.4
  • 36
    • 0030054719 scopus 로고    scopus 로고
    • Regulation of class I and class II myosins by heavy chain phosphorylation
    • DOI 10.1074/jbc.271.29.16983
    • Brzeska, H., and Korn, E. D. (1996) Regulation of class I and class II myosins by heavy chain phosphorylation. J. Biol. Chem. 271, 16983-16986 (Pubitemid 26244239)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.29 , pp. 16983-16986
    • Brzeska, H.1    Korn, E.D.2
  • 37
    • 0029006373 scopus 로고
    • TEDS rule: A molecular rationale for differential regulation of myosins by phosphorylation of the heavy chain head
    • Bement, W. M., and Mooseker, M. S. (1995) TEDS rule: a molecular rationale for differential regulation of myosins by phosphorylation of the heavy chain head. Cell Motil. Cytoskeleton 31, 87-92
    • (1995) Cell Motil. Cytoskeleton , vol.31 , pp. 87-92
    • Bement, W.M.1    Mooseker, M.S.2
  • 39
    • 0032493318 scopus 로고    scopus 로고
    • Kinetic characterization of myosin head fragments with long-lived myosin ATP states
    • DOI 10.1021/bi973143f
    • Friedman, A. L., Geeves, M. A., Manstein, D. J., and Spudich, J. A. (1998) Kinetic characterization of myosin head fragments with long-lived myosin ATP states. Biochemistry 37, 9679-9687 (Pubitemid 28319612)
    • (1998) Biochemistry , vol.37 , Issue.27 , pp. 9679-9687
    • Friedman, A.L.1    Geeves, M.A.2    Manstein, D.J.3    Spudich, J.A.4
  • 40
    • 0030035665 scopus 로고    scopus 로고
    • Structure-function studies of the myosin motor domain: Importance of the 50-kDa cleft
    • Ruppel, K. M., and Spudich, J. A. (1996) Structure-function studies of the myosin motor domain: importance of the 50-kDa cleft. Mol. Biol. Cell 7, 1123-1136 (Pubitemid 26244208)
    • (1996) Molecular Biology of the Cell , vol.7 , Issue.7 , pp. 1123-1136
    • Ruppel, K.M.1    Spudich, J.A.2
  • 43
    • 79959954909 scopus 로고    scopus 로고
    • Myosin 1b promotes the formation of post-Golgi carriers by regulating actin assembly and membrane remodelling at the trans-Golgi network
    • Almeida, C. G., Yamada, A., Tenza, D., Louvard, D., Raposo, G., and Coudrier, E. (2011) Myosin 1b promotes the formation of post-Golgi carriers by regulating actin assembly and membrane remodelling at the trans-Golgi network. Nat. Cell Biol. 13, 779-789
    • (2011) Nat. Cell Biol. , vol.13 , pp. 779-789
    • Almeida, C.G.1    Yamada, A.2    Tenza, D.3    Louvard, D.4    Raposo, G.5    Coudrier, E.6
  • 44
    • 0030664537 scopus 로고    scopus 로고
    • Alanine scanning mutagenesis of the switch I region in the ATPase site of Dictyostelium discoideum myosin II
    • DOI 10.1021/bi971837i
    • Shimada, T., Sasaki, N., Ohkura, R., and Sutoh, K. (1997) Alanine scanning mutagenesis of the switch I region in the ATPase site of Dictyostelium discoideum myosin II. Biochemistry 36, 14037-14043 (Pubitemid 27509838)
    • (1997) Biochemistry , vol.36 , Issue.46 , pp. 14037-14043
    • Shimada, T.1    Sasaki, N.2    Ohkura, R.3    Sutoh, K.4
  • 45
    • 0035951831 scopus 로고    scopus 로고
    • Recruitment of a specific amoeboid myosin I isoform to the plasma membrane in chemotactic Dictyostelium cells
    • Senda, S., Lee, S. F., Côté, G. P., and Titus, M. A. (2001) Recruitment of a specific amoeboid myosin I isoform to the plasma membrane in chemotactic Dictyostelium cells. J. Biol. Chem. 276, 2898-2904
    • (2001) J. Biol. Chem. , vol.276 , pp. 2898-2904
    • Senda, S.1    Lee, S.F.2    Côté, G.P.3    Titus, M.A.4
  • 47
    • 0037162284 scopus 로고    scopus 로고
    • Visualizing PI3 kinase-mediated cell-cell signaling during Dictyostelium development
    • DOI 10.1016/S0960-9822(02)00950-8, PII S0960982202009508
    • Dormann, D., Weijer, G., Parent, C. A., Devreotes, P. N., and Weijer, C. J. (2002) Visualizing PI3 kinase-mediated cell-cell signaling during Dictyostelium development. Curr. Biol. 12, 1178-1188 (Pubitemid 34801165)
    • (2002) Current Biology , vol.12 , Issue.14 , pp. 1178-1188
    • Dormann, D.1    Weijer, G.2    Parent, C.A.3    Devreotes, P.N.4    Weijer, C.J.5
  • 50
    • 0036349419 scopus 로고    scopus 로고
    • Eukaryotic cell locomotion depends on the propagation of self-organized reaction-diffusion waves and oscillations of actin filament assembly
    • Vicker, M. G. (2002) Eukaryotic cell locomotion depends on the propagation of self-organized reaction-diffusion waves and oscillations of actin filament assembly. Exp. Cell Res. 275, 54-66
    • (2002) Exp. Cell Res. , vol.275 , pp. 54-66
    • Vicker, M.G.1
  • 51
    • 79955847965 scopus 로고    scopus 로고
    • Propagating waves separate two states of actin organization in living cells
    • Schroth-Diez, B., Gerwig, S., Ecke, M., Hegerl, R., Diez, S., and Gerisch, G. (2009) Propagating waves separate two states of actin organization in living cells. HFSP J. 3, 412-427
    • (2009) HFSP J. , vol.3 , pp. 412-427
    • Schroth-Diez, B.1    Gerwig, S.2    Ecke, M.3    Hegerl, R.4    Diez, S.5    Gerisch, G.6
  • 52
    • 80053523626 scopus 로고    scopus 로고
    • Different modes of state transitions determine pattern in the phosphatidylinositide-actin system
    • Gerisch, G., Ecke, M., Wischnewski, D., and Schroth-Diez, B. (2011) Different modes of state transitions determine pattern in the phosphatidylinositide-actin system. BMC Cell Biol. 12, 42
    • (2011) BMC Cell Biol. , vol.12 , pp. 42
    • Gerisch, G.1    Ecke, M.2    Wischnewski, D.3    Schroth-Diez, B.4
  • 53
    • 16344384079 scopus 로고    scopus 로고
    • Mobile actin clusters and traveling waves in cells recovering from actin depolymerization
    • DOI 10.1529/biophysj.104.047589
    • Gerisch, G., Bretschneider, T., Müller-Taubenberger, A., Simmeth, E., Ecke, M., Diez, S., and Anderson, K. (2004) Mobile actin clusters and traveling waves in cells recovering from actin depolymerization. Biophys. J. 87, 3493-3503 (Pubitemid 40468602)
    • (2004) Biophysical Journal , vol.87 , Issue.5 , pp. 3493-3503
    • Gerisch, G.1    Bretschneider, T.2    Muller-Taubenberger, A.3    Simmeth, E.4    Ecke, M.5    Diez, S.6    Anderson, K.7
  • 55
    • 13544249968 scopus 로고    scopus 로고
    • In vivo analysis of 3-phosphoinositide dynamics during Dictyostelium phagocytosis and chemotaxis
    • DOI 10.1242/jcs.01579
    • Dormann, D., Weijer, G., Dowler, S., and Weijer, C. J. (2004) In vivo analysis of 3-phosphoinositide dynamics during Dictyostelium phagocytosis and chemotaxis. J. Cell Sci. 117, 6497-6509 (Pubitemid 40220275)
    • (2004) Journal of Cell Science , vol.117 , Issue.26 , pp. 6497-6509
    • Dormann, D.1    Weijer, G.2    Dowler, S.3    Weijer, C.J.4
  • 56
    • 0034635567 scopus 로고    scopus 로고
    • Localization of the G protein βγ complex in living cells during chemotaxis
    • DOI 10.1126/science.287.5455.1034
    • Jin, T., Zhang, N., Long, Y., Parent, C. A., and Devreotes, P. N. (2000) Localization of the G protein βγ complex in living cells during chemotaxis. Science 287, 1034-1036 (Pubitemid 30094358)
    • (2000) Science , vol.287 , Issue.5455 , pp. 1034-1036
    • Jin, T.1    Zhang, N.2    Long, Y.3    Parent, C.A.4    Devreotes, P.N.5
  • 58
    • 0034602558 scopus 로고    scopus 로고
    • A potential mechanism for regulating myosin I binding to membranes in vivo
    • Senda, S., and Titus, M. A. (2000) A potential mechanism for regulating myosin I binding to membranes in vivo. FEBS Lett. 484, 125-128
    • (2000) FEBS Lett. , vol.484 , pp. 125-128
    • Senda, S.1    Titus, M.A.2
  • 59
    • 0038281249 scopus 로고    scopus 로고
    • Phosphoinositide recognition domains
    • Lemmon, M. A. (2003) Phosphoinositide recognition domains. Traffic 4, 201-213
    • (2003) Traffic , vol.4 , pp. 201-213
    • Lemmon, M.A.1
  • 60
    • 0035943018 scopus 로고    scopus 로고
    • Motor domain-dependent localization of myo1b (myr-1)
    • DOI 10.1016/S0960-9822(01)00320-7
    • Tang, N., and Ostap, E. M. (2001) Motor domain-dependent localization of myo1b (myr-1). Curr. Biol. 11, 1131-1135 (Pubitemid 32675767)
    • (2001) Current Biology , vol.11 , Issue.14 , pp. 1131-1135
    • Tang, N.1    Ostap, E.M.2
  • 61
    • 0036218579 scopus 로고    scopus 로고
    • MYO1A (brush border myosin I) dynamics in the brush border of LLC-PK1-CL4 cells
    • Tyska, M. J., and Mooseker, M. S. (2002) MYO1A (brush border myosin I) dynamics in the brush border of LLC-PK1-CL4 cells. Biophys. J. 82, 1869-1883 (Pubitemid 34280803)
    • (2002) Biophysical Journal , vol.82 , Issue.4 , pp. 1869-1883
    • Tyska, M.J.1    Mooseker, M.S.2
  • 62
    • 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. U.S.A. 106, 9685-9690
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 9685-9690
    • Brawley, C.M.1    Rock, R.S.2
  • 63
    • 33846821794 scopus 로고    scopus 로고
    • Myosin 1E interacts with synaptojanin-1 and dynamin and is involved in endocytosis
    • DOI 10.1016/j.febslet.2007.01.021, PII S0014579307000543
    • Krendel, M., Osterweil, E. K., and Mooseker, M. S. (2007) Myosin 1E interacts with synaptojanin-1 and dynamin and is involved in endocytosis. FEBS Lett. 581, 644-650 (Pubitemid 46216290)
    • (2007) FEBS Letters , vol.581 , Issue.4 , pp. 644-650
    • Krendel, M.1    Osterweil, E.K.2    Mooseker, M.S.3
  • 64
    • 0034605066 scopus 로고    scopus 로고
    • Amyosin I is involved in membrane recycling from early endosomes
    • Neuhaus, E. M., and Soldati, T. (2000)Amyosin I is involved in membrane recycling from early endosomes. J. Cell Biol. 150, 1013-1026
    • (2000) J. Cell Biol. , vol.150 , pp. 1013-1026
    • Neuhaus, E.M.1    Soldati, T.2
  • 65
    • 0031004852 scopus 로고    scopus 로고
    • Amoeboid movement anchored by eupodia, new actin-rich knobby feet in Dictyostelium
    • DOI 10.1002/(SICI)1097-0169(1997)36:4<339::AID-CM4>3.0.CO;2-0
    • Fukui, Y., and Inoué, S. (1997) Amoeboid movement anchored by eupodia, new actin-rich knobby feet in Dictyostelium. Cell Motil. Cytoskeleton 36, 339-354 (Pubitemid 27155349)
    • (1997) Cell Motility and the Cytoskeleton , vol.36 , Issue.4 , pp. 339-354
    • Fukui, Y.1    Inoue, S.2
  • 66
    • 38349054763 scopus 로고    scopus 로고
    • Human deafness mutation E385D disrupts the mechanochemical coupling and subcellular targeting of myosin-1a
    • Yengo, C. M., Ananthanarayanan, S. K., Brosey, C. A., Mao, S., and Tyska, M. J. (2008) Human deafness mutation E385D disrupts the mechanochemical coupling and subcellular targeting of myosin-1a. Biophys. J. 94, L5-7
    • (2008) Biophys. J. , vol.94
    • Yengo, C.M.1    Ananthanarayanan, S.K.2    Brosey, C.A.3    Mao, S.4    Tyska, M.J.5
  • 67
    • 77956257788 scopus 로고    scopus 로고
    • Localization of myosin 1b to actin protrusions requires phosphoinositide binding
    • Komaba, S., and Coluccio, L. M. (2010) Localization of myosin 1b to actin protrusions requires phosphoinositide binding. J. Biol. Chem. 285, 27686-27693
    • (2010) J. Biol. Chem. , vol.285 , pp. 27686-27693
    • Komaba, S.1    Coluccio, L.M.2
  • 68
    • 77949443128 scopus 로고    scopus 로고
    • Differential localization and dynamics of class I myosins in the enterocyte microvillus
    • Benesh, A. E., Nambiar, R., McConnell, R. E., Mao, S., Tabb, D. L., and Tyska, M. J. (2010) Differential localization and dynamics of class I myosins in the enterocyte microvillus. Mol. Biol. Cell 21, 970-978
    • (2010) Mol. Biol. Cell , vol.21 , pp. 970-978
    • Benesh, A.E.1    Nambiar, R.2    McConnell, R.E.3    Mao, S.4    Tabb, D.L.5    Tyska, M.J.6
  • 69
    • 0037115637 scopus 로고    scopus 로고
    • Intracellular localization and dynamics of myosin-II and myosin-IC in live Acanthamoeba by transient transfection of EGFP fusion proteins
    • Kong, H. H., and Pollard, T. D. (2002) Intracellular localization and dynamics of myosin-II and myosin-IC in live Acanthamoeba by transient transfection of EGFP fusion proteins. J. Cell Sci. 115, 4993-5002
    • (2002) J. Cell Sci. , vol.115 , pp. 4993-5002
    • Kong, H.H.1    Pollard, T.D.2
  • 70
    • 0034645065 scopus 로고    scopus 로고
    • Fission yeast myosin-I, Myo1p, stimulates actin assembly by Arp2/3 complex and shares functions with WASp
    • Lee, W. L., Bezanilla, M., and Pollard, T. D. (2000) Fission yeast myosin-I, Myo1p, stimulates actin assembly by Arp2/3 complex and shares functions with WASp. J. Cell Biol. 151, 789-800
    • (2000) J. Cell Biol. , vol.151 , pp. 789-800
    • Lee, W.L.1    Bezanilla, M.2    Pollard, T.D.3
  • 71
    • 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
    • Stöffler, H. E., Honnert, U., Bauer, C. A., Höfer, D., Schwarz, H., Müller, R. T., Drenckhahn, D., and Bähler, M. (1998) Targeting of the myosin-I myr 3 to intercellular adherens type junctions induced by dominant active Cdc42 in HeLa cells. J. Cell Sci. 111, 2779-2788
    • (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
  • 72
    • 0029559076 scopus 로고
    • Localization of the rat myosin I molecules myr 1 and myr 2 and in vivo targeting of their tail domains
    • Ruppert, C., Godel, J., Müller, R. T., Kroschewski, R., Reinhard, J., and Bähler, M. (1995) Localization of the rat myosin I molecules myr 1 and myr 2 and in vivo targeting of their tail domains. J. Cell Sci. 108, 3775-3786 (Pubitemid 26003210)
    • (1995) Journal of Cell Science , vol.108 , Issue.12 , pp. 3775-3786
    • Ruppert, C.1    Godel, J.2    Muller, R.T.3    Kroschewski, R.4    Reinhard, J.5    Bahler, M.6
  • 73
    • 33750487863 scopus 로고    scopus 로고
    • Myosin-1c Couples Assembling Actin to Membranes to Drive Compensatory Endocytosis
    • DOI 10.1016/j.devcel.2006.09.002, PII S1534580706003959
    • Sokac, A. M., Schietroma, C., Gundersen, C. B., and Bement, W. M. (2006) Myosin-1c couples assembling actin to membranes to drive compensatory endocytosis. Dev. Cell 11, 629-640 (Pubitemid 44644962)
    • (2006) Developmental Cell , vol.11 , Issue.5 , pp. 629-640
    • Sokac, A.M.1    Schietroma, C.2    Gundersen, C.B.3    Bement, W.M.4
  • 74
    • 0033950782 scopus 로고    scopus 로고
    • Localization of wild type and mutant class I myosin proteins in Aspergillus nidulans using GFP-fusion proteins
    • DOI 10.1002/(SICI)1097-0169(200002)45:2<163::AID-CM7>3.0.CO;2-D
    • Yamashita, R. A., Osherov, N., and May, G. S. (2000) Localization of wild type and mutant class I myosin proteins in Aspergillus nidulans using GFP fusion proteins. Cell Motil. Cytoskeleton 45, 163-172 (Pubitemid 30084666)
    • (2000) Cell Motility and the Cytoskeleton , vol.45 , Issue.2 , pp. 163-172
    • Yamashita, R.A.1    Osherov, N.2    May, G.S.3
  • 75
    • 0026721410 scopus 로고
    • Localization and specificity of the phospholipid and actin binding sites on the tail of Acanthamoeba myosin IC
    • Doberstein, S. K., and Pollard, T. D. (1992) Localization and specificity of the phospholipid and actin binding sites on the tail of Acanthamoeba myosin IC. J. Cell Biol. 117, 1241-1249
    • (1992) J. Cell Biol. , vol.117 , pp. 1241-1249
    • Doberstein, S.K.1    Pollard, T.D.2
  • 76
    • 80053078222 scopus 로고    scopus 로고
    • Myosin 1c participates in B cell cytoskeleton rearrangements, is recruited to the immunologic synapse, and contributes to antigen presentation
    • Maravillas-Montero, J. L., Gillespie, P. G., Patiño-López, G., Shaw, S., and Santos-Argumedo, L. (2011) Myosin 1c participates in B cell cytoskeleton rearrangements, is recruited to the immunologic synapse, and contributes to antigen presentation. J. Immunol. 187, 3053-3063
    • (2011) J. Immunol. , vol.187 , pp. 3053-3063
    • Maravillas-Montero, J.L.1    Gillespie, P.G.2    Patiño-López, G.3    Shaw, S.4    Santos-Argumedo, L.5
  • 77
    • 0029987840 scopus 로고    scopus 로고
    • Overlapping functions of myosin-I isoforms?
    • DOI 10.1083/jcb.133.2.221
    • Ostap, E. M., and Pollard, T. D. (1996) Overlapping functions of myosin-I isoforms? J. Cell Biol. 133, 221-224 (Pubitemid 26131610)
    • (1996) Journal of Cell Biology , vol.133 , Issue.2 , pp. 221-224
    • Ostap, E.M.1    Pollard, T.D.2
  • 78
    • 33845315084 scopus 로고    scopus 로고
    • Powering membrane traffic in endocytosis and recycling
    • DOI 10.1038/nrm2060, PII NRM2060
    • Soldati, T., and Schliwa, M. (2006) Powering membrane traffic in endocytosis and recycling. Nat. Rev. Mol. Cell Biol. 7, 897-908 (Pubitemid 44871416)
    • (2006) Nature Reviews Molecular Cell Biology , vol.7 , Issue.12 , pp. 897-908
    • Soldati, T.1    Schliwa, M.2
  • 79
    • 0033754575 scopus 로고    scopus 로고
    • Unconventional myosins: Anchors in the membrane traffic relay
    • Tuxworth, R. I., and Titus, M. A. (2000) Unconventional myosins: anchors in the membrane traffic relay. Traffic 1, 11-18
    • (2000) Traffic , vol.1 , pp. 11-18
    • Tuxworth, R.I.1    Titus, M.A.2
  • 80
    • 24044500344 scopus 로고    scopus 로고
    • Myosins: Tails (and heads) of functional diversity
    • Krendel, M., and Mooseker, M. S. (2005) Myosins: tails (and heads) of functional diversity. Physiology 20, 239-251 (Pubitemid 41215198)
    • (2005) Physiology , Issue.4 , pp. 239-251
    • Krendel, M.1    Mooseker, M.S.2
  • 81
    • 70349448090 scopus 로고    scopus 로고
    • Mechanotransduction by hair cells: Models, molecules, and mechanisms
    • Gillespie, P. G., and Müller, U. (2009) Mechanotransduction by hair cells: models, molecules, and mechanisms. Cell 139, 33-44
    • (2009) Cell , vol.139 , pp. 33-44
    • Gillespie, P.G.1    Müller, U.2
  • 82
    • 33750488465 scopus 로고    scopus 로고
    • Myosin I and actin dynamics: The frogs weigh in
    • Titus, M. A. (2006) Myosin I and actin dynamics: the frogs weigh in. Dev. Cell 11, 594-595
    • (2006) Dev. Cell , vol.11 , pp. 594-595
    • Titus, M.A.1
  • 83
    • 0034111791 scopus 로고    scopus 로고
    • A dibasic motif in the tail of a class XIV apicomplexan myosin is an essential determinant of plasma membrane localization
    • Hettmann, C., Herm, A., Geiter, A., Frank, B., Schwarz, E., Soldati, T., and Soldati, D. (2000) A dibasic motif in the tail of a class XIV apicomplexan myosin is an essential determinant of plasma membrane localization. Mol. Biol. Cell 11, 1385-1400 (Pubitemid 30211037)
    • (2000) Molecular Biology of the Cell , vol.11 , Issue.4 , pp. 1385-1400
    • Hettmann, C.1    Herm, A.2    Geiter, A.3    Frank, B.4    Schwarz, E.5    Soldati, T.6    Soldati, D.7
  • 84
    • 18244378218 scopus 로고    scopus 로고
    • A Dictyostelium homologue of WASP is required for polarized F-actin assembly during chemotaxis
    • DOI 10.1091/mbc.E04-09-0844
    • Myers, S. A., Han, J. W., Lee, Y., Firtel, R. A., and Chung, C. Y. (2005) A Dictyostelium homologue of WASP is required for polarized F-actin assembly during chemotaxis. Mol. Biol. Cell 16, 2191-2206 (Pubitemid 40632205)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.5 , pp. 2191-2206
    • Myers, S.A.1    Han, J.W.2    Lee, Y.3    Firtel, R.A.4    Chung, C.Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.