메뉴 건너뛰기




Volumn 15, Issue 1, 2003, Pages 40-47

Microtubules meet substrate adhesions to arrange cell polarity

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; GUANOSINE TRIPHOSPHATASE; RHO FACTOR;

EID: 0037221714     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(02)00008-X     Document Type: Review
Times cited : (186)

References (63)
  • 2
    • 0036273491 scopus 로고    scopus 로고
    • Evolutionary conservation of microtubule-capture mechanisms
    • •]) present mechanisms of microtubule interaction with actin and their mutual regulation. The authors uncover interesting analogies in different cell types.
    • •]) present mechanisms of microtubule interaction with actin and their mutual regulation. The authors uncover interesting analogies in different cell types.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 296-304
    • Gundersen, G.G.1
  • 3
    • 0035975991 scopus 로고    scopus 로고
    • Roles of the fission yeast formin for3p in cell polarity, actin cable formation and symmetric cell division
    • Feierbach B., Chang F. Roles of the fission yeast formin for3p in cell polarity, actin cable formation and symmetric cell division. Curr. Biol. 11:2001;1656-1665.
    • (2001) Curr. Biol. , vol.11 , pp. 1656-1665
    • Feierbach, B.1    Chang, F.2
  • 5
    • 0036514271 scopus 로고    scopus 로고
    • Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast
    • Evangelista M., Pruyne D., Amberg D.C., Boone C., Bretscher A. Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast. Nat. Cell Biol. 4:2002;260-269.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 260-269
    • Evangelista, M.1    Pruyne, D.2    Amberg, D.C.3    Boone, C.4    Bretscher, A.5
  • 7
    • 0028961293 scopus 로고
    • Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes C.D., Hall A. Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell. 81:1995;53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 8
    • 0030940218 scopus 로고    scopus 로고
    • Rho, Rac and Cdc42 regulate actin organization and cell adhesion in macrophages
    • Allen W.E., Jones G.E., Pollard J.W., Ridley A.J. Rho, Rac and Cdc42 regulate actin organization and cell adhesion in macrophages. J. Cell Sci. 110:1997;707-720.
    • (1997) J. Cell Sci. , vol.110 , pp. 707-720
    • Allen, W.E.1    Jones, G.E.2    Pollard, J.W.3    Ridley, A.J.4
  • 9
    • 0033577975 scopus 로고    scopus 로고
    • Interplay between Rac and Rho in the control of substrate contact dynamics
    • Rottner K., Hall A., Small J.V. Interplay between Rac and Rho in the control of substrate contact dynamics. Curr. Biol. 9:1999;640-648.
    • (1999) Curr. Biol. , vol.9 , pp. 640-648
    • Rottner, K.1    Hall, A.2    Small, J.V.3
  • 11
    • 0036222784 scopus 로고    scopus 로고
    • Adhesion assembly, disassembly and turnover in migrating cells - Over and over and over again
    • This is a very informative, up-to date review on adhesion dynamics and its regulation in motile cells.
    • Webb D.J., Parsons J.T., Horwitz A.F. Adhesion assembly, disassembly and turnover in migrating cells - over and over and over again. Nat. Cell Biol. 4:2002;E97-E100 This is a very informative, up-to date review on adhesion dynamics and its regulation in motile cells.
    • (2002) Nat. Cell Biol. , vol.4
    • Webb, D.J.1    Parsons, J.T.2    Horwitz, A.F.3
  • 12
    • 0033160196 scopus 로고    scopus 로고
    • Cooperation between mDia1 and ROCK in Rho-induced actin reorganization
    • Watanabe N., Kato T., Fujita A., Ishizaki T., Narumiya S. Cooperation between mDia1 and ROCK in Rho-induced actin reorganization. Nat. Cell Biol. 1:1999;136-143.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 136-143
    • Watanabe, N.1    Kato, T.2    Fujita, A.3    Ishizaki, T.4    Narumiya, S.5
  • 13
    • 0035479910 scopus 로고    scopus 로고
    • Assembly and mechanosensory function of focal contacts
    • Geiger B., Bershadsky A. Assembly and mechanosensory function of focal contacts. Curr. Opin. Cell Biol. 13:2001;584-592.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 584-592
    • Geiger, B.1    Bershadsky, A.2
  • 14
    • 0035158377 scopus 로고    scopus 로고
    • RhoA inactivation by p190RhoGAP regulates cell spreading and migration by promoting membrane protrusion and polarity
    • This is a fascinating study that elaborates on the adhesion-induced mechanism of Rho suppression that is transmitted via integrin-triggered Rho GAP activation. It is shown that Rho downregulation is necessary for both spreading and the establishment of cell polarity, and therefore for motility.
    • Arthur W.T., Burridge K. RhoA inactivation by p190RhoGAP regulates cell spreading and migration by promoting membrane protrusion and polarity. Mol. Biol. Cell. 12:2001;2711-2720 This is a fascinating study that elaborates on the adhesion-induced mechanism of Rho suppression that is transmitted via integrin-triggered Rho GAP activation. It is shown that Rho downregulation is necessary for both spreading and the establishment of cell polarity, and therefore for motility.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2711-2720
    • Arthur, W.T.1    Burridge, K.2
  • 15
    • 18444414614 scopus 로고    scopus 로고
    • ROCK and mDia1 antagonize in Rho-dependent Rac activation in Swiss 3T3 fibroblasts
    • This, a very interesting paper, provides new insights on the interplay between Rho family GTPases. mDia is shown to induce Rac activation, in a new pathway downstream from Rho.
    • Tsuji T., Ishizaki T., Okamoto M., Higashida C., Kimura K., Furuyashiki T., Arakawa Y., Birge R.B., Nakamoto T., Hirai H.et al. ROCK and mDia1 antagonize in Rho-dependent Rac activation in Swiss 3T3 fibroblasts. J. Cell Biol. 157:2002;819-830 This, a very interesting paper, provides new insights on the interplay between Rho family GTPases. mDia is shown to induce Rac activation, in a new pathway downstream from Rho.
    • (2002) J. Cell Biol. , vol.157 , pp. 819-830
    • Tsuji, T.1    Ishizaki, T.2    Okamoto, M.3    Higashida, C.4    Kimura, K.5    Furuyashiki, T.6    Arakawa, Y.7    Birge, R.B.8    Nakamoto, T.9    Hirai, H.10
  • 16
    • 0033594123 scopus 로고    scopus 로고
    • Rho GTPases control polarity, protrusion, and adhesion during cell movement
    • Nobes C.D., Hall A. Rho GTPases control polarity, protrusion, and adhesion during cell movement. J. Cell Biol. 144:1999;1235-1244.
    • (1999) J. Cell Biol. , vol.144 , pp. 1235-1244
    • Nobes, C.D.1    Hall, A.2
  • 17
    • 0034865456 scopus 로고    scopus 로고
    • Rho GTPases and cell migration
    • Ridley A.J. Rho GTPases and cell migration. J. Cell Sci. 114:2001;2713-2722.
    • (2001) J. Cell Sci. , vol.114 , pp. 2713-2722
    • Ridley, A.J.1
  • 18
    • 0035858878 scopus 로고    scopus 로고
    • Nascent focal adhesions are responsible for the generation of strong propulsive forces in migrating fibroblasts
    • Beningo K.A., Dembo M., Kaverina I., Small J.V., Wang Y.L. Nascent focal adhesions are responsible for the generation of strong propulsive forces in migrating fibroblasts. J. Cell Biol. 153:2001;881-888.
    • (2001) J. Cell Biol. , vol.153 , pp. 881-888
    • Beningo, K.A.1    Dembo, M.2    Kaverina, I.3    Small, J.V.4    Wang, Y.L.5
  • 20
    • 0035945353 scopus 로고    scopus 로고
    • Marching at the front and dragging behind: Differential alphaVbeta3-integrin turnover regulates focal adhesion behavior
    • The authors describe high-quality imaging of the distribution and properties of β3 integrins throughout the development of substrate adhesions from focal complexes to trailing focal adhesions. Adhesions are classified according to integrin density, and the apparent sliding of trailing adhesions is shown to correlate with a linear turnover of adhesion components. The role of tensile stress on integrin density is also emphasised.
    • Ballestrem C., Hinz B., Imhof B.A., Wehrle-Haller B. Marching at the front and dragging behind: differential alphaVbeta3-integrin turnover regulates focal adhesion behavior. J. Cell Biol. 155:2001;1319-1332 The authors describe high-quality imaging of the distribution and properties of β3 integrins throughout the development of substrate adhesions from focal complexes to trailing focal adhesions. Adhesions are classified according to integrin density, and the apparent sliding of trailing adhesions is shown to correlate with a linear turnover of adhesion components. The role of tensile stress on integrin density is also emphasised.
    • (2001) J. Cell Biol. , vol.155 , pp. 1319-1332
    • Ballestrem, C.1    Hinz, B.2    Imhof, B.A.3    Wehrle-Haller, B.4
  • 22
    • 0035833247 scopus 로고    scopus 로고
    • RhoA is required for monocyte tail retraction during transendothelial migration
    • Worthylake R.A., Lemoine S., Watson J.M., Burridge K. RhoA is required for monocyte tail retraction during transendothelial migration. J. Cell Biol. 54:2001;147-160.
    • (2001) J. Cell Biol. , vol.54 , pp. 147-160
    • Worthylake, R.A.1    Lemoine, S.2    Watson, J.M.3    Burridge, K.4
  • 23
    • 0036070518 scopus 로고    scopus 로고
    • Spatiotemporal regulation of moesin phosphorylation and rear release by Rho and serine/threonine phosphatase during neutrophil migration
    • Yoshinaga-Ohara N., Takahashi A., Uchiyama T., Sasada M. Spatiotemporal regulation of moesin phosphorylation and rear release by Rho and serine/threonine phosphatase during neutrophil migration. Exp. Cell Res. 278:2002;112-122.
    • (2002) Exp. Cell Res. , vol.278 , pp. 112-122
    • Yoshinaga-Ohara, N.1    Takahashi, A.2    Uchiyama, T.3    Sasada, M.4
  • 24
    • 0027366484 scopus 로고
    • Microtubules, centrosomes and intermediate filaments in directed cell movement
    • Schliwa MaH B. Microtubules, centrosomes and intermediate filaments in directed cell movement. Trends Cell Biol. 3:1993;377-380.
    • (1993) Trends Cell Biol. , vol.3 , pp. 377-380
    • Schliwa MaH, B.1
  • 26
    • 0035178210 scopus 로고    scopus 로고
    • Cell motility: Can Rho GTPases and microtubules point the way?
    • This is a thorough review that focuses on the role of Rho GTPase signalling in the interplay and feedback between microtubules and actin in cell polarisation and motility. It includes interesting and alternative speculations about the influence of microtubules on actin cytoskeleton dynamics.
    • Wittmann T., Waterman-Storer C.M. Cell motility: can Rho GTPases and microtubules point the way? J. Cell Sci. 114:2001;3795-3803 This is a thorough review that focuses on the role of Rho GTPase signalling in the interplay and feedback between microtubules and actin in cell polarisation and motility. It includes interesting and alternative speculations about the influence of microtubules on actin cytoskeleton dynamics.
    • (2001) J. Cell Sci. , vol.114 , pp. 3795-3803
    • Wittmann, T.1    Waterman-Storer, C.M.2
  • 28
    • 0035910554 scopus 로고    scopus 로고
    • Rac/Cdc42 and p65PAK regulate the microtubule-destabilizing protein stathmin through phosphorylation at serine 16
    • This study shows that microtubule-destabilising activity of stathmin can be inhibited by specific PAK-dependent phosphorylation downstream of Rac/Cdc42. These data provide evidence for Rac/Cdc42-regulated microtubule dynamics.
    • Daub H., Gevaert K., Vandekerckhove J., Sobel A., Hall A. Rac/Cdc42 and p65PAK regulate the microtubule-destabilizing protein stathmin through phosphorylation at serine 16. J. Biol. Chem. 276:2001;1677-1680 This study shows that microtubule-destabilising activity of stathmin can be inhibited by specific PAK-dependent phosphorylation downstream of Rac/Cdc42. These data provide evidence for Rac/Cdc42-regulated microtubule dynamics.
    • (2001) J. Biol. Chem. , vol.276 , pp. 1677-1680
    • Daub, H.1    Gevaert, K.2    Vandekerckhove, J.3    Sobel, A.4    Hall, A.5
  • 29
    • 0034492210 scopus 로고    scopus 로고
    • Actin-dependent lamellipodia formation and microtubule-dependent tail retraction control-directed cell migration
    • Ballestrem C., Wehrle-Haller B., Hinz B., Imhof B.A. Actin-dependent lamellipodia formation and microtubule-dependent tail retraction control-directed cell migration. Mol. Biol. Cell. 11:2000;2999-3012.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2999-3012
    • Ballestrem, C.1    Wehrle-Haller, B.2    Hinz, B.3    Imhof, B.A.4
  • 30
    • 0032872870 scopus 로고    scopus 로고
    • Microtubule targeting of substrate contacts promotes their relaxation and dissociation
    • Kaverina I., Krylyshkina O., Small J.V. Microtubule targeting of substrate contacts promotes their relaxation and dissociation. J. Cell Biol. 146:1999;1033-1044.
    • (1999) J. Cell Biol. , vol.146 , pp. 1033-1044
    • Kaverina, I.1    Krylyshkina, O.2    Small, J.V.3
  • 32
    • 0035838422 scopus 로고    scopus 로고
    • Critical role for the EB1 and APC interaction in the regulation of microtubule polymerization
    • Nakamura M., Zhou X.Z., Lu K.P. Critical role for the EB1 and APC interaction in the regulation of microtubule polymerization. Curr. Biol. 11:2001;1062-1067.
    • (2001) Curr. Biol. , vol.11 , pp. 1062-1067
    • Nakamura, M.1    Zhou, X.Z.2    Lu, K.P.3
  • 33
    • 0034614936 scopus 로고    scopus 로고
    • Adenomatous polyposis coli (APC) protein moves along microtubules and concentrates at their growing ends in epithelial cells
    • Mimori-Kiyosue Y., Shiina N., Tsukita S. Adenomatous polyposis coli (APC) protein moves along microtubules and concentrates at their growing ends in epithelial cells. J. Cell Biol. 148:2000;505-518.
    • (2000) J. Cell Biol. , vol.148 , pp. 505-518
    • Mimori-Kiyosue, Y.1    Shiina, N.2    Tsukita, S.3
  • 35
    • 0033615966 scopus 로고    scopus 로고
    • Rac downregulates Rho activity: Reciprocal balance between both GTPases determines cellular morphology and migratory behavior
    • Sander E.E., ten Klooster J.P., van Delft S., van der Kammen R.A., Collard J.G. Rac downregulates Rho activity: reciprocal balance between both GTPases determines cellular morphology and migratory behavior. J. Cell Biol. 147:1999;1009-1022.
    • (1999) J. Cell Biol. , vol.147 , pp. 1009-1022
    • Sander, E.E.1    Ten Klooster, J.P.2    Van Delft, S.3    Van der Kammen, R.A.4    Collard, J.G.5
  • 36
    • 18444369936 scopus 로고    scopus 로고
    • Rac1 and Cdc42 capture microtubules through IQGAP1 and CLIP-170
    • This paper provides strong evidence for the Rac/Cdc42-dependent binding of the effector protein IQGAP1 with microtubule tips via CLIP-170. The disturbance of this association leads to the lost of cell polarity.
    • Fukata M., Watanabe T., Noritake J., Nakagawa M., Yamaga M., Kuroda S., Matsuura Y., Iwamatsu A., Perez F., Kaibuchi K. Rac1 and Cdc42 capture microtubules through IQGAP1 and CLIP-170. Cell. 109:2002;873-885 This paper provides strong evidence for the Rac/Cdc42-dependent binding of the effector protein IQGAP1 with microtubule tips via CLIP-170. The disturbance of this association leads to the lost of cell polarity.
    • (2002) Cell , vol.109 , pp. 873-885
    • Fukata, M.1    Watanabe, T.2    Noritake, J.3    Nakagawa, M.4    Yamaga, M.5    Kuroda, S.6    Matsuura, Y.7    Iwamatsu, A.8    Perez, F.9    Kaibuchi, K.10
  • 37
    • 0034266786 scopus 로고    scopus 로고
    • CLIP170-like tip1p spatially organizes microtubular dynamics in fission yeast
    • Brunner D., Nurse P. CLIP170-like tip1p spatially organizes microtubular dynamics in fission yeast. Cell. 102:2000;695-704.
    • (2000) Cell , vol.102 , pp. 695-704
    • Brunner, D.1    Nurse, P.2
  • 38
    • 17744372880 scopus 로고    scopus 로고
    • CLASPs are CLIP-115 and -170 associating proteins involved in the regional regulation of microtubule dynamics in motile fibroblasts
    • A new family of microtubule-tip proteins (CLASPs) is essential for the asymmetric orientation of stable microtubule arrays in a wound healing assay. CLASPs localise to a subset of plus-ends, preferentially in the front part of the cell and therefore may be involved in certain aspects of microtubule-dependent cell polarisation.
    • Akhmanova A., Hoogenraad C.C., Drabek K., Stepanova T., Dortland B., Verkerk T., Vermeulen W., Burgering B.M., De Zeeuw C.I., Grosveld F.et al. CLASPs are CLIP-115 and -170 associating proteins involved in the regional regulation of microtubule dynamics in motile fibroblasts. Cell. 104:2001;923-935 A new family of microtubule-tip proteins (CLASPs) is essential for the asymmetric orientation of stable microtubule arrays in a wound healing assay. CLASPs localise to a subset of plus-ends, preferentially in the front part of the cell and therefore may be involved in certain aspects of microtubule-dependent cell polarisation.
    • (2001) Cell , vol.104 , pp. 923-935
    • Akhmanova, A.1    Hoogenraad, C.C.2    Drabek, K.3    Stepanova, T.4    Dortland, B.5    Verkerk, T.6    Vermeulen, W.7    Burgering, B.M.8    De Zeeuw, C.I.9    Grosveld, F.10
  • 39
    • 0032567341 scopus 로고    scopus 로고
    • Cloning and characterization of GEF-H1, a microtubule-associated guanine nucleotide exchange factor for Rac and Rho GTPases
    • Ren Y., Li R., Zheng Y., Busch H. Cloning and characterization of GEF-H1, a microtubule-associated guanine nucleotide exchange factor for Rac and Rho GTPases. J. Biol. Chem. 273:1998;34954-34960.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34954-34960
    • Ren, Y.1    Li, R.2    Zheng, Y.3    Busch, H.4
  • 40
    • 0033593337 scopus 로고    scopus 로고
    • The Dbl-related protein, Lfc, localizes to microtubules and mediates the activation of Rac signaling pathways in cells
    • Glaven J.A., Whitehead I., Bagrodia S., Kay R., Cerione R.A. The Dbl-related protein, Lfc, localizes to microtubules and mediates the activation of Rac signaling pathways in cells. J. Biol. Chem. 274:1999;2279-2285.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2279-2285
    • Glaven, J.A.1    Whitehead, I.2    Bagrodia, S.3    Kay, R.4    Cerione, R.A.5
  • 41
    • 0035895915 scopus 로고    scopus 로고
    • Characterization of p190RhoGEF, a RhoA-specific guanine nucleotide exchange factor that interacts with microtubules
    • van Horck F.P., Ahmadian M.R., Haeusler L.C., Moolenaar W.H., Kranenburg O. Characterization of p190RhoGEF, a RhoA-specific guanine nucleotide exchange factor that interacts with microtubules. J. Biol. Chem. 276:2001;4948-4956.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4948-4956
    • Van Horck, F.P.1    Ahmadian, M.R.2    Haeusler, L.C.3    Moolenaar, W.H.4    Kranenburg, O.5
  • 42
    • 0036228955 scopus 로고    scopus 로고
    • Nucleotide exchange factor GEF-H1 mediates cross-talk between microtubules and the actin cytoskeleton
    • The authors describe the first direct evidence that microtubule binding of a regulatory molecule can modulate the activity of a Rho-family GTPase. The Rho-specific exchange factor GEF H1 is active only when it is not bound to microtubules.
    • Krendel M., Zenke F.T., Bokoch G.M. Nucleotide exchange factor GEF-H1 mediates cross-talk between microtubules and the actin cytoskeleton. Nat. Cell Biol. 4:2002;294-301 The authors describe the first direct evidence that microtubule binding of a regulatory molecule can modulate the activity of a Rho-family GTPase. The Rho-specific exchange factor GEF H1 is active only when it is not bound to microtubules.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 294-301
    • Krendel, M.1    Zenke, F.T.2    Bokoch, G.M.3
  • 43
    • 0030462929 scopus 로고    scopus 로고
    • Microtubule disruption induces the formation of actin stress fibers and focal adhesions in cultured cells: Possible involvement of the Rho signal cascade
    • Enomoto T. Microtubule disruption induces the formation of actin stress fibers and focal adhesions in cultured cells: possible involvement of the Rho signal cascade. Cell Struct. Funct. 21:1996;317-326.
    • (1996) Cell Struct. Funct. , vol.21 , pp. 317-326
    • Enomoto, T.1
  • 44
    • 0032514208 scopus 로고    scopus 로고
    • Targeting, capture, and stabilization of microtubules at early focal adhesions
    • Kaverina I., Rottner K., Small J.V. Targeting, capture, and stabilization of microtubules at early focal adhesions. J. Cell Biol. 142:1998;181-190.
    • (1998) J. Cell Biol. , vol.142 , pp. 181-190
    • Kaverina, I.1    Rottner, K.2    Small, J.V.3
  • 45
    • 0037148524 scopus 로고    scopus 로고
    • Modulation of substrate adhesion dynamics via microtubule targeting requires kinesin-1
    • This study shows that the influence of microtubules on adhesion dynamics is dependent on kinesin-1. A block of kinesin, but not of dynein, caused similar changes in adhesion patterns to those observed following microtubule disruption with nocodazole.
    • Krylyshkina O., Kaverina I., Kranewitter W., Steffen W., Alonso M.C., Cross R.A., Small J.V. Modulation of substrate adhesion dynamics via microtubule targeting requires kinesin-1. J. Cell Biol. 156:2002;349-360 This study shows that the influence of microtubules on adhesion dynamics is dependent on kinesin-1. A block of kinesin, but not of dynein, caused similar changes in adhesion patterns to those observed following microtubule disruption with nocodazole.
    • (2002) J. Cell Biol. , vol.156 , pp. 349-360
    • Krylyshkina, O.1    Kaverina, I.2    Kranewitter, W.3    Steffen, W.4    Alonso, M.C.5    Cross, R.A.6    Small, J.V.7
  • 46
  • 48
    • 0034739851 scopus 로고    scopus 로고
    • Temporal and spatial distribution of activated Pak1 in fibroblasts
    • Sells M.A., Pfaff A., Chernoff J. Temporal and spatial distribution of activated Pak1 in fibroblasts. J. Cell Biol. 151:2000;1449-1458.
    • (2000) J. Cell Biol. , vol.151 , pp. 1449-1458
    • Sells, M.A.1    Pfaff, A.2    Chernoff, J.3
  • 49
    • 0035999990 scopus 로고    scopus 로고
    • Paxillin-dependent paxillin kinase linker and p21-activated kinase localization to focal adhesions involves a multistep activation pathway
    • Brown M.C., West K.A., Turner C.E. Paxillin-dependent paxillin kinase linker and p21-activated kinase localization to focal adhesions involves a multistep activation pathway. Mol. Biol. Cell. 13:2002;1550-1565.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1550-1565
    • Brown, M.C.1    West, K.A.2    Turner, C.E.3
  • 50
    • 0035844869 scopus 로고    scopus 로고
    • Focal contacts as mechanosensors: Externally applied local mechanical force induces growth of focal contacts by an mDia1-dependent and ROCK-independent mechanism
    • Riveline D., Zamir E., Balaban N.Q., Schwarz U.S., Ishizaki T., Narumiya S., Kam Z., Geiger B., Bershadsky A.D. Focal contacts as mechanosensors: externally applied local mechanical force induces growth of focal contacts by an mDia1-dependent and ROCK-independent mechanism. J. Cell Biol. 153:2001;1175-1186.
    • (2001) J. Cell Biol. , vol.153 , pp. 1175-1186
    • Riveline, D.1    Zamir, E.2    Balaban, N.Q.3    Schwarz, U.S.4    Ishizaki, T.5    Narumiya, S.6    Kam, Z.7    Geiger, B.8    Bershadsky, A.D.9
  • 51
    • 0036591961 scopus 로고    scopus 로고
    • Tensile stress stimulates microtubule outgrowth in living cells
    • This work shows that tensile stress applied to cells promotes microtubule polymerisation into the stressed regions and into adhesion foci amplified by stress. Microtubule polymerisation dynamics is therefore influenced by a mechanical force factor and thus joins the group of processes in which stress-induced conformational changes are associated with signal transmission.
    • Kaverina I., Krylyshkina O., Beningo K., Anderson K., Wang Y.-L., Small J.V. Tensile stress stimulates microtubule outgrowth in living cells. J. Cell Sci. 115:2002;2283-2291 This work shows that tensile stress applied to cells promotes microtubule polymerisation into the stressed regions and into adhesion foci amplified by stress. Microtubule polymerisation dynamics is therefore influenced by a mechanical force factor and thus joins the group of processes in which stress-induced conformational changes are associated with signal transmission.
    • (2002) J. Cell Sci. , vol.115 , pp. 2283-2291
    • Kaverina, I.1    Krylyshkina, O.2    Beningo, K.3    Anderson, K.4    Wang, Y.-L.5    Small, J.V.6
  • 52
    • 0034907213 scopus 로고    scopus 로고
    • MDia mediates Rho-regulated formation and orientation of stable microtubules
    • Palazzo A.F., Cook T.A., Alberts A.S., Gundersen G.G. mDia mediates Rho-regulated formation and orientation of stable microtubules. Nat. Cell Biol. 3:2001;723-729.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 723-729
    • Palazzo, A.F.1    Cook, T.A.2    Alberts, A.S.3    Gundersen, G.G.4
  • 54
    • 0037043342 scopus 로고    scopus 로고
    • Dual-wavelength fluorescent speckle microscopy reveals coupling of microtubule and actin movements in migrating cells
    • Salmon W.C., Adams M.C., Waterman-Storer C.M. Dual-wavelength fluorescent speckle microscopy reveals coupling of microtubule and actin movements in migrating cells. J. Cell Biol. 158:2002;31-37.
    • (2002) J. Cell Biol. , vol.158 , pp. 31-37
    • Salmon, W.C.1    Adams, M.C.2    Waterman-Storer, C.M.3
  • 55
    • 0037043343 scopus 로고    scopus 로고
    • Filopodia and actin arcs guide the assembly and transport of two populations of microtubules with unique dynamic parameters in neuronal growth cones
    • Schaefer A.W., Kabir N., Forscher P. Filopodia and actin arcs guide the assembly and transport of two populations of microtubules with unique dynamic parameters in neuronal growth cones. J. Cell Biol. 158:2002;139-152.
    • (2002) J. Cell Biol. , vol.158 , pp. 139-152
    • Schaefer, A.W.1    Kabir, N.2    Forscher, P.3
  • 57
    • 0036227387 scopus 로고    scopus 로고
    • Roles for the tubulin- and PTP-PEST-binding paxillin LIM domains in cell adhesion and motility
    • Brown M.C., Turner C.E. Roles for the tubulin- and PTP-PEST-binding paxillin LIM domains in cell adhesion and motility. Int. J. Biochem. Cell Biol. 34:2002;855-863.
    • (2002) Int. J. Biochem. Cell Biol. , vol.34 , pp. 855-863
    • Brown, M.C.1    Turner, C.E.2
  • 59
    • 0033582659 scopus 로고    scopus 로고
    • CLIP-170 highlights growing microtubule ends in vivo
    • Perez F., Diamantopoulos G.S., Stalder R., Kreis T.E. CLIP-170 highlights growing microtubule ends in vivo. Cell. 96:1999;517-527.
    • (1999) Cell , vol.96 , pp. 517-527
    • Perez, F.1    Diamantopoulos, G.S.2    Stalder, R.3    Kreis, T.E.4
  • 60
    • 0034644119 scopus 로고    scopus 로고
    • The dynamic behavior of the APC-binding protein EB1 on the distal ends of microtubules
    • Mimori-Kiyosue Y., Shiina N., Tsukita S. The dynamic behavior of the APC-binding protein EB1 on the distal ends of microtubules. Curr. Biol. 10:2000;865-868.
    • (2000) Curr. Biol. , vol.10 , pp. 865-868
    • Mimori-Kiyosue, Y.1    Shiina, N.2    Tsukita, S.3
  • 61
    • 0036915826 scopus 로고    scopus 로고
    • Microtubule asymmetry during neutrophil polarization and migration
    • in press
    • Eddy JE, Pierini LM, Maxfield FR: Microtubule asymmetry during neutrophil polarization and migration. Mol Biol Cell 2002, in press.
    • (2002) Mol Biol Cell
    • Eddy, J.E.1    Pierini, L.M.2    Maxfield, F.R.3
  • 62
    • 0034739004 scopus 로고    scopus 로고
    • Myosin V orients the mitotic spindle in yeast
    • Yin H., Pruyne D., Huffaker T.C., Bretscher A. Myosin V orients the mitotic spindle in yeast. Nature. 406:2000;1013-1015.
    • (2000) Nature , vol.406 , pp. 1013-1015
    • Yin, H.1    Pruyne, D.2    Huffaker, T.C.3    Bretscher, A.4
  • 63
    • 0036645506 scopus 로고    scopus 로고
    • Microtubule capture by the cleavage apparatus is required for proper spindle positioning in yeast
    • Kusch J., Meyer A., Snyder M.P., Barral Y. Microtubule capture by the cleavage apparatus is required for proper spindle positioning in yeast. Genes Dev. 16:2002;1627-1639.
    • (2002) Genes Dev. , vol.16 , pp. 1627-1639
    • Kusch, J.1    Meyer, A.2    Snyder, M.P.3    Barral, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.