메뉴 건너뛰기




Volumn 141, Issue 1, 1998, Pages 175-185

Rho guanosine triphosphatase mediates the selective stabilization of microtubules induced by lysophosphatidic acid

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL CELL; ARTICLE; CELL POLARITY; CELL STRAIN 3T3; CYTOSKELETON; FIBROBLAST; MEMBRANE STABILIZATION; MICROTUBULE ASSEMBLY; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROCESSING; PROTEIN STABILITY;

EID: 0032489802     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.141.1.175     Document Type: Article
Times cited : (218)

References (68)
  • 3
    • 0025313509 scopus 로고
    • Individual microtubules in the axon consist of domains that differ in both composition and stability
    • Baas, P.W., and M.M. Black. 1990. Individual microtubules in the axon consist of domains that differ in both composition and stability. J. Cell Biol. 111:495-509.
    • (1990) J. Cell Biol. , vol.111 , pp. 495-509
    • Baas, P.W.1    Black, M.M.2
  • 4
    • 0030266491 scopus 로고    scopus 로고
    • Involvement of microtubules in the control of adhesion-dependent signal transduction
    • Bershadsky, A., A. Chausobsky, E. Becker, A. Lyubimova, and B. Geiger. 1996. Involvement of microtubules in the control of adhesion-dependent signal transduction. Curr. Biol. 6:1279-1289.
    • (1996) Curr. Biol. , vol.6 , pp. 1279-1289
    • Bershadsky, A.1    Chausobsky, A.2    Becker, E.3    Lyubimova, A.4    Geiger, B.5
  • 5
    • 0027308924 scopus 로고
    • Abnormal tau phosphorylation at ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding
    • Bramblett, G.T., M. Goedert, R. Jakes, S.E. Merrick, J.Q. Trojanowski, and V.M.-Y. Lee. 1993. Abnormal tau phosphorylation at ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding. Neuron. 10:1089-1099.
    • (1993) Neuron , vol.10 , pp. 1089-1099
    • Bramblett, G.T.1    Goedert, M.2    Jakes, R.3    Merrick, S.E.4    Trojanowski, J.Q.5    Lee, V.M.-Y.6
  • 7
    • 0026181461 scopus 로고
    • Stabilization and posttranslational modification of microtubules during cellular morphogenesis
    • Bulinski, J.C., and G.G. Gundersen. 1991. Stabilization and posttranslational modification of microtubules during cellular morphogenesis. BioEssays 13:285-293.
    • (1991) BioEssays , vol.13 , pp. 285-293
    • Bulinski, J.C.1    Gundersen, G.G.2
  • 8
    • 0029670547 scopus 로고    scopus 로고
    • In search of membrane receptors for microtubule-based motors - Is kinectin a kinesin receptor?
    • Burkhardt, J.K. 1996. In search of membrane receptors for microtubule-based motors - is kinectin a kinesin receptor? Trends Cell Biol. 6:127-131.
    • (1996) Trends Cell Biol. , vol.6 , pp. 127-131
    • Burkhardt, J.K.1
  • 9
    • 0024202112 scopus 로고
    • Real-time observations of microtubule dynamic instability in living cells
    • Cassimeris, L., N.K. Pryer, and E.D. Salmon. 1988. Real-time observations of microtubule dynamic instability in living cells. J. Cell Biol. 107:2223-2231.
    • (1988) J. Cell Biol. , vol.107 , pp. 2223-2231
    • Cassimeris, L.1    Pryer, N.K.2    Salmon, E.D.3
  • 10
    • 0027333420 scopus 로고
    • Life at the leading edge: The formation of cell protrusions
    • Condeelis, J. 1993. Life at the leading edge: the formation of cell protrusions. Annu. Rev. Cell Biol. 9:411-444.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 411-444
    • Condeelis, J.1
  • 11
    • 0024325593 scopus 로고
    • Fibroblast contractility and actin organization are stimulated by microtubule inhibitors
    • Danowski, B.A. 1989. Fibroblast contractility and actin organization are stimulated by microtubule inhibitors. J. Cell Sci. 93:255-266.
    • (1989) J. Cell Sci. , vol.93 , pp. 255-266
    • Danowski, B.A.1
  • 12
    • 0028924141 scopus 로고
    • Modulation of microtubule dynamic instability in vivo by brain microtubule associated proteins
    • Dhamodharan, R., and P. Wadsworth. 1995. Modulation of microtubule dynamic instability in vivo by brain microtubule associated proteins. J. Cell Sci. 108:1679-1689.
    • (1995) J. Cell Sci. , vol.108 , pp. 1679-1689
    • Dhamodharan, R.1    Wadsworth, P.2
  • 13
    • 0022896901 scopus 로고
    • Tau protein function in living cells
    • Drubin, D.G., and M.W. Kirschner. 1986. Tau protein function in living cells. J. Cell Biol. 103:2739-2746.
    • (1986) J. Cell Biol. , vol.103 , pp. 2739-2746
    • Drubin, D.G.1    Kirschner, M.W.2
  • 14
    • 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. 1996. 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. 21:317-326.
    • (1996) Cell Struct. Funct. , vol.21 , pp. 317-326
    • Enomoto, T.1
  • 15
    • 0022872163 scopus 로고
    • Microtubule arrays in differentiated cells contain elevated levels of a post-translationally modified form of tubulin
    • Gundersen, G.G., and J.C. Bulinski. 1986. Microtubule arrays in differentiated cells contain elevated levels of a post-translationally modified form of tubulin. Eur. J. Cell Biol. 42:288-294.
    • (1986) Eur. J. Cell Biol. , vol.42 , pp. 288-294
    • Gundersen, G.G.1    Bulinski, J.C.2
  • 16
    • 0023794840 scopus 로고
    • Selective stabilization of microtubules oriented toward the direction of cell migration
    • Gundersen, G.G., and J.C. Bulinski. 1988. Selective stabilization of microtubules oriented toward the direction of cell migration. Proc. Natl. Acad. Sci. USA. 85:5946-5950.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5946-5950
    • Gundersen, G.G.1    Bulinski, J.C.2
  • 17
    • 0021752265 scopus 로고
    • Distinct populations of microtubules: Tyrosinated and nontyrosinated alpha-tubulin are distributed differently in vivo
    • Gundersen, G.G., M.H. Kalnoski, and J.C. Bulinski. 1984. Distinct populations of microtubules: tyrosinated and nontyrosinated alpha-tubulin are distributed differently in vivo. Cell. 38:779-789.
    • (1984) Cell , vol.38 , pp. 779-789
    • Gundersen, G.G.1    Kalnoski, M.H.2    Bulinski, J.C.3
  • 18
    • 0023371190 scopus 로고
    • Postpolymerization detyrosination of α-tubulin: A mechanism for subcellular differentiation of microtubules
    • Gundersen, G.G., S. Khawaja, and J.C. Bulinski. 1987. Postpolymerization detyrosination of α-tubulin: a mechanism for subcellular differentiation of microtubules. J. Cell Biol. 105:251-264.
    • (1987) J. Cell Biol. , vol.105 , pp. 251-264
    • Gundersen, G.G.1    Khawaja, S.2    Bulinski, J.C.3
  • 19
    • 0024453421 scopus 로고
    • Generation of a stable, posttranslationally modified microtubule array is an early event in myogenic differentiation
    • Gundersen, G.G., S. Khawaja, and J.C. Bulinski. 1989. Generation of a stable, posttranslationally modified microtubule array is an early event in myogenic differentiation. J. Cell Biol. 109:2275-2288.
    • (1989) J. Cell Biol. , vol.109 , pp. 2275-2288
    • Gundersen, G.G.1    Khawaja, S.2    Bulinski, J.C.3
  • 20
    • 0028274116 scopus 로고
    • Induction of stable microtubules in 3T3 fibroblasts by TGF-β and serum
    • Gundersen, G.G., I. Kim, and C.J. Chapin. 1994. Induction of stable microtubules in 3T3 fibroblasts by TGF-β and serum. J. Cell Sci. 107:645-649.
    • (1994) J. Cell Sci. , vol.107 , pp. 645-649
    • Gundersen, G.G.1    Kim, I.2    Chapin, C.J.3
  • 21
    • 0027515613 scopus 로고
    • Protein phosphatase inhibitors induce the selective breakdown of stable microtubules in fibroblasts and epithelial cells
    • Gurland, G., and G.G. Gundersen. 1993. Protein phosphatase inhibitors induce the selective breakdown of stable microtubules in fibroblasts and epithelial cells. Proc. Nat. Acad. Sci. USA. 90:8827-8831.
    • (1993) Proc. Nat. Acad. Sci. USA , vol.90 , pp. 8827-8831
    • Gurland, G.1    Gundersen, G.G.2
  • 22
    • 0028883469 scopus 로고
    • Stable, detyrosinated microtubules function to localize vimentin intermediate filaments in fibroblasts
    • Gurland, G., and G.G. Gundersen. 1995. Stable, detyrosinated microtubules function to localize vimentin intermediate filaments in fibroblasts. J. Cell Biol. 131:1275-1290.
    • (1995) J. Cell Biol. , vol.131 , pp. 1275-1290
    • Gurland, G.1    Gundersen, G.G.2
  • 23
    • 0028170820 scopus 로고
    • Small GTP-binding proteins and the regulation of the actin cytoskeleton
    • Hall, A. 1994. Small GTP-binding proteins and the regulation of the actin cytoskeleton. Annu. Rev. Cell Biol. 10:31-54.
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 31-54
    • Hall, A.1
  • 24
    • 0030570801 scopus 로고    scopus 로고
    • Interaction of the rho family small G proteins with kinectin, an anchoring protein of the kinesin motor
    • Hotta, K., K. Tanaka, A. Mino, H. Kohno, and Y. Takai. 1996. Interaction of the rho family small G proteins with kinectin, an anchoring protein of the kinesin motor. Biochem. Biophys. Res. Commun. 225:69-74.
    • (1996) Biochem. Biophys. Res. Commun. , vol.225 , pp. 69-74
    • Hotta, K.1    Tanaka, K.2    Mino, A.3    Kohno, H.4    Takai, Y.5
  • 25
    • 0024581772 scopus 로고
    • Posttranslational modification of distinct microtubule subpopulations during cell polarization and differentiation in the mouse preimplantation embryo
    • Houliston, E., and B. Maro. 1989. Posttranslational modification of distinct microtubule subpopulations during cell polarization and differentiation in the mouse preimplantation embryo. J. Cell Biol. 108:543-551.
    • (1989) J. Cell Biol. , vol.108 , pp. 543-551
    • Houliston, E.1    Maro, B.2
  • 27
    • 0024438227 scopus 로고
    • Expression of multiple tau isoforms and microtubule bundle formation in fibroblasts transfected with a single tau cDN A
    • Kanai, Y., R. Takemura, T. Oshima, H. Mori, Y. Ihara, M. Yanagisaw, Y. Masaki, and N. Hirokawa. 1989. Expression of multiple tau isoforms and microtubule bundle formation in fibroblasts transfected with a single tau cDN A. J. Cell Biol. 109:1173-1184.
    • (1989) J. Cell Biol. , vol.109 , pp. 1173-1184
    • Kanai, Y.1    Takemura, R.2    Oshima, T.3    Mori, H.4    Ihara, Y.5    Yanagisaw, M.6    Masaki, Y.7    Hirokawa, N.8
  • 28
    • 0023877365 scopus 로고
    • Enhanced stability of microtubules enriched in detyrosinated tubulin is not a direct function of detyrosination level
    • Khawaja, S., G.G. Gundersen, and J.C. Bulinski. 1988. Enhanced stability of microtubules enriched in detyrosinated tubulin is not a direct function of detyrosination level. J. Cell Biol. 106:141-149.
    • (1988) J. Cell Biol. , vol.106 , pp. 141-149
    • Khawaja, S.1    Gundersen, G.G.2    Bulinski, J.C.3
  • 29
    • 0020265993 scopus 로고
    • Rat monoclonal antitubulin antibodies derived by using a nonsecreting rat cell line
    • Kilmartin, J.V., B. Wright, and C. Milstein. 1982. Rat monoclonal antitubulin antibodies derived by using a nonsecreting rat cell line. J. Cell Biol. 93:576-582.
    • (1982) J. Cell Biol. , vol.93 , pp. 576-582
    • Kilmartin, J.V.1    Wright, B.2    Milstein, C.3
  • 31
    • 0000315614 scopus 로고    scopus 로고
    • Dissociation of LPA-induced cytoskeletal contraction from stress fiber formation by differential localization of RhoA
    • Kranenburg, O., M. Poland, M., Gebbink, L. Oomen, and W.H. Moolenar. 1997. Dissociation of LPA-induced cytoskeletal contraction from stress fiber formation by differential localization of RhoA. J. Cell Sci. 110:2417-2427.
    • (1997) J. Cell Sci. , vol.110 , pp. 2417-2427
    • Kranenburg, O.1    Poland, M.2    Gebbink, M.3    Oomen, L.4    Moolenar, W.H.5
  • 32
    • 0023403268 scopus 로고
    • Microtubules containing detyrosinated tubulin are less dynamic
    • Kreis, T. 1987. Microtubules containing detyrosinated tubulin are less dynamic. EMBO (Eur. Mol. Biol. Organ.) J. 6:2597-2606.
    • (1987) EMBO (Eur. Mol. Biol. Organ.) J. , vol.6 , pp. 2597-2606
    • Kreis, T.1
  • 34
    • 0023803882 scopus 로고
    • Two monoclonal antibodies to actin: One muscle selective and one generally reactive
    • Lessard, J.L. 1988. Two monoclonal antibodies to actin: one muscle selective and one generally reactive. Cell Motil. Cytoskeleton. 10:349-362.
    • (1988) Cell Motil. Cytoskeleton , vol.10 , pp. 349-362
    • Lessard, J.L.1
  • 35
    • 0028863142 scopus 로고
    • A novel serine/threonine kinase binding the ras-related rho A GTPase which translocates the kinase to peripheral membranes
    • Leung, T., E. Manser, L. Tan, and L. Lim. 1995. A novel serine/threonine kinase binding the ras-related rho A GTPase which translocates the kinase to peripheral membranes. J. Biol. Chem. 270:29051-29054.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29051-29054
    • Leung, T.1    Manser, E.2    Tan, L.3    Lim, L.4
  • 36
    • 0029789678 scopus 로고    scopus 로고
    • The p160 rhoA-binding kinase ROKa is a member of a kinase family and is involved in the reorganization of the cytoskeleton
    • Leung, T., X.-Q. Chen, E. Manser, and L. Lim. 1996. The p160 rhoA-binding kinase ROKa is a member of a kinase family and is involved in the reorganization of the cytoskeleton. Mol. Cell. Biol. 16:5313-5327.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5313-5327
    • Leung, T.1    Chen, X.-Q.2    Manser, E.3    Lim, L.4
  • 37
    • 0026019425 scopus 로고
    • Spatial distribution of posttranslationally modified tubulins in polarized cells of developing Artemia
    • MacRae, T.H., C.M. Langdon, and F.A. Freeman. 1991. Spatial distribution of posttranslationally modified tubulins in polarized cells of developing Artemia. Cell Motil. Cytoskeleton. 18:189-203.
    • (1991) Cell Motil. Cytoskeleton , vol.18 , pp. 189-203
    • MacRae, T.H.1    Langdon, C.M.2    Freeman, F.A.3
  • 40
    • 0028785435 scopus 로고
    • Centripetal transport of microtubules in motile cells
    • Mikhailov, A., and G.G. Gundersen. 1995. Centripetal transport of microtubules in motile cells. Cell Motil. Cytoskeleton. 32:173-186.
    • (1995) Cell Motil. Cytoskeleton , vol.32 , pp. 173-186
    • Mikhailov, A.1    Gundersen, G.G.2
  • 41
    • 0025149387 scopus 로고
    • Morphological alterations of Xenopus oocytes induced by valine-14 p21 rho depend on isoprenylation and are inhibited by Clostridium botulinum C3 ADP-ribosyltransferase
    • Mohr, C., I. Just, A. Hall, and K. Aktories. 1990. Morphological alterations of Xenopus oocytes induced by valine-14 p21 rho depend on isoprenylation and are inhibited by Clostridium botulinum C3 ADP-ribosyltransferase. FEBS Lett. 275:168-172.
    • (1990) FEBS Lett. , vol.275 , pp. 168-172
    • Mohr, C.1    Just, I.2    Hall, A.3    Aktories, K.4
  • 43
    • 0029960434 scopus 로고    scopus 로고
    • Depletion of lysophosphatidic acid triggers a loss of oriented detyrosinated microtubules in motile fibroblasts
    • Nagasaki, T., and G.G. Gundersen. 1996. Depletion of lysophosphatidic acid triggers a loss of oriented detyrosinated microtubules in motile fibroblasts. J. Cell Sci. 109:2461-2469.
    • (1996) J. Cell Sci. , vol.109 , pp. 2461-2469
    • Nagasaki, T.1    Gundersen, G.G.2
  • 44
    • 0026793992 scopus 로고
    • Distribution of detyrosinated microtubules in motile NRK fibroblasts is rapidly altered upon cell-cell contact: Implications for contact inhibition of locomotion
    • Nagasaki, T., C.J. Chapin., and G.G. Gundersen. 1992. Distribution of detyrosinated microtubules in motile NRK fibroblasts is rapidly altered upon cell-cell contact: implications for contact inhibition of locomotion. Cell Motil. Cytoskeleton. 23:45-60.
    • (1992) Cell Motil. Cytoskeleton , vol.23 , pp. 45-60
    • Nagasaki, T.1    Chapin, C.J.2    Gundersen, G.G.3
  • 45
    • 0028556970 scopus 로고
    • Isolated plasma membranes induce loss of oriented detyrosinated microtubules and other contact inhibition-like responses in migrating NRK cells
    • Nagasaki, T., G. Liao, and G.G. Gundersen. 1994. Isolated plasma membranes induce loss of oriented detyrosinated microtubules and other contact inhibition-like responses in migrating NRK cells. J. Cell Sci. 107:3413-3423.
    • (1994) J. Cell Sci. , vol.107 , pp. 3413-3423
    • Nagasaki, T.1    Liao, G.2    Gundersen, G.G.3
  • 46
    • 0025688199 scopus 로고
    • Microtubules are stabilized in confluent epithelial cells but not in fibroblasts
    • Pepperkok, R., M.H. Bre, J. Davoust, and T.E. Kreis. 1990. Microtubules are stabilized in confluent epithelial cells but not in fibroblasts. J. Cell Biol. 111:3003-3012.
    • (1990) J. Cell Biol. , vol.111 , pp. 3003-3012
    • Pepperkok, R.1    Bre, M.H.2    Davoust, J.3    Kreis, T.E.4
  • 47
    • 0023293040 scopus 로고
    • Microtubules containing acetylated α tubulin in mammalian cells in culture
    • Piperno, G., M.H. Bre, J. Davoust, and T.E. Kreis. 1987. Microtubules containing acetylated α tubulin in mammalian cells in culture. J. Cell. Biol. 104:289-302.
    • (1987) J. Cell. Biol. , vol.104 , pp. 289-302
    • Piperno, G.1    Bre, M.H.2    Davoust, J.3    Kreis, T.E.4
  • 48
    • 0019842813 scopus 로고
    • All classes of IFs share a common antigenic determinant defines by a monoclonal antibody
    • Pruss, R.M., R. Mirsky, M.C. Raff, R. Thorpe, A.J. Dowding, and B.H. Anderton. 1981. All classes of IFs share a common antigenic determinant defines by a monoclonal antibody. Cell. 27:419-428.
    • (1981) Cell , vol.27 , pp. 419-428
    • Pruss, R.M.1    Mirsky, R.2    Raff, M.C.3    Thorpe, R.4    Dowding, A.J.5    Anderton, B.H.6
  • 49
    • 0029889591 scopus 로고    scopus 로고
    • Rhotekin, a new putative target for rho bearing homology to a serine/threonine kinase, PKN, and rhophilin in the rho-binding domain
    • Reid, T., T. Furuyashiki, T. Ishizaki, G. Watanabe, K. Fujiwawa, N. Morii, P. Madaule, and S. Narumiya. 1996. Rhotekin, a new putative target for rho bearing homology to a serine/threonine kinase, PKN, and rhophilin in the rho-binding domain. J. Biol. Chem. 271:13556-13560.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13556-13560
    • Reid, T.1    Furuyashiki, T.2    Ishizaki, T.3    Watanabe, G.4    Fujiwawa, K.5    Morii, N.6    Madaule, P.7    Narumiya, S.8
  • 50
    • 0030001638 scopus 로고    scopus 로고
    • Physical association of the small GTPase rho with a 68-kDa phosphatidylinositol 4-phosphate 5-kinase in Swiss 3T3 cells
    • Ren, X.-D., G.M. Bokoch, A. Traynor-Kaplan, G.J. Jenkins, R.A. Anderson, and M.A. Schwartz. 1996. Physical association of the small GTPase rho with a 68-kDa phosphatidylinositol 4-phosphate 5-kinase in Swiss 3T3 cells. Mol. Biol. Cell. 7:435-442.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 435-442
    • Ren, X.-D.1    Bokoch, G.M.2    Traynor-Kaplan, A.3    Jenkins, G.J.4    Anderson, R.A.5    Schwartz, M.A.6
  • 51
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley, A.J., H.F. Paterson, C.L. Johnston, D. Diekmann, and A. Hall. 1992. The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell. 70:401-410.
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 52
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley, A.J., and A. Hall. 1992. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell. 70:389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 53
    • 0023779031 scopus 로고
    • Functional modification of a 21-kilodalton G protein when ADP-ribosylated by exoenzyme C3 of Clostridium botulinum
    • Rubin, E.J., D.M. Gill, P. Boquet, and M.R. Popoff. 1988. Functional modification of a 21-kilodalton G protein when ADP-ribosylated by exoenzyme C3 of Clostridium botulinum. Mol. Cell. Biol. 8:418-426.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 418-426
    • Rubin, E.J.1    Gill, D.M.2    Boquet, P.3    Popoff, M.R.4
  • 54
    • 0023885426 scopus 로고
    • Direct observation of microtubule dynamics in living cells
    • Sammak, P.J., and G.G. Borisy. 1988. Direct observation of microtubule dynamics in living cells. Nature. 332:724-726.
    • (1988) Nature , vol.332 , pp. 724-726
    • Sammak, P.J.1    Borisy, G.G.2
  • 56
    • 0022481480 scopus 로고
    • Microtubule dynamics in interphase cells
    • Schulze, E., and M. Kirschner. 1986. Microtubule dynamics in interphase cells. J. Cell Biol. 102:1020-1031.
    • (1986) J. Cell Biol. , vol.102 , pp. 1020-1031
    • Schulze, E.1    Kirschner, M.2
  • 57
    • 0023788884 scopus 로고
    • New features of microtubule behaviour observed in vivo
    • Schulze, E., and M. Kirschner. 1988. New features of microtubule behaviour observed in vivo. Nature. 334:356-359.
    • (1988) Nature , vol.334 , pp. 356-359
    • Schulze, E.1    Kirschner, M.2
  • 58
    • 0023608861 scopus 로고
    • Posttranslational modifications and microtubule stability
    • Schulze, E., D.J. Asai, J.C. Bulinski, and M. Kirschner. 1987. Posttranslational modifications and microtubule stability. J. Cell Biol. 105:2167-2177.
    • (1987) J. Cell Biol. , vol.105 , pp. 2167-2177
    • Schulze, E.1    Asai, D.J.2    Bulinski, J.C.3    Kirschner, M.4
  • 59
    • 0027458626 scopus 로고
    • Observation and quantification of individual microtubule behavior in vivo: Microtubule dynamics are cell-type specific
    • Shelden, E., and P. Wadsworth. 1993. Observation and quantification of individual microtubule behavior in vivo: microtubule dynamics are cell-type specific. J. Cell Biol. 120:935-945.
    • (1993) J. Cell Biol. , vol.120 , pp. 935-945
    • Shelden, E.1    Wadsworth, P.2
  • 60
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusion proteins with glutathione-S-transferase
    • Smith, D.B., and K.S. Johnson. 1988. Single-step purification of polypeptides expressed in Escherichia coli as fusion proteins with glutathione-S-transferase. Gene. 67:31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 61
    • 0025833804 scopus 로고
    • ADP-ribosylation of a small size GTP-binding protein in bovine neutrophils by the C3 exoenzyme of Clostridium botulinum and effect on the cell motility
    • Stasia, M.-J., A. Jouan, N. Bourmeyster, P. Boquet, and P.V. Vignais. 1991. ADP-ribosylation of a small size GTP-binding protein in bovine neutrophils by the C3 exoenzyme of Clostridium botulinum and effect on the cell motility. Biochem. Biophys. Res. Commun. 180:615-622.
    • (1991) Biochem. Biophys. Res. Commun. , vol.180 , pp. 615-622
    • Stasia, M.-J.1    Jouan, A.2    Bourmeyster, N.3    Boquet, P.4    Vignais, P.V.5
  • 62
    • 0027391509 scopus 로고
    • Involvement of rho p21 and its inhibitory GDP/GTP exchange protein (rho GDI) in cell motility
    • Takaishi, K., A. Kikuchi, S. Kuroda, K. Kotani, T. Sasaki, and Y. Takai. 1993. Involvement of rho p21 and its inhibitory GDP/GTP exchange protein (rho GDI) in cell motility. Mol. Cell. Biol. 13:72-79.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 72-79
    • Takaishi, K.1    Kikuchi, A.2    Kuroda, S.3    Kotani, K.4    Sasaki, T.5    Takai, Y.6
  • 63
    • 0029131982 scopus 로고
    • Translocation of activated Rho from the cytoplasm to membrane ruffling area, cell-cell adhesion sites and cleavage furrows
    • Takaishi, K., T. Sasaki, M. Kato, W. Yamochi, S. Kuroda, T. Nakamura, M. Takeichi, and Y. Takai. 1995. Translocation of activated Rho from the cytoplasm to membrane ruffling area, cell-cell adhesion sites and cleavage furrows. Oncogene. 11:39-48.
    • (1995) Oncogene , vol.11 , pp. 39-48
    • Takaishi, K.1    Sasaki, T.2    Kato, M.3    Yamochi, W.4    Kuroda, S.5    Nakamura, T.6    Takeichi, M.7    Takai, Y.8
  • 64
    • 0025006680 scopus 로고
    • Distribution of microtubules containing post-translationally modified alpha-tubulin during Drosophila embryogenesis
    • Warn, R.M., A. Harrison, T. Planques, N. Robert-Nicoud, and J. Wheland. 1990. Distribution of microtubules containing post-translationally modified alpha-tubulin during Drosophila embryogenesis. Cell Motil. Cytoskeleton. 17:34-45.
    • (1990) Cell Motil. Cytoskeleton , vol.17 , pp. 34-45
    • Warn, R.M.1    Harrison, A.2    Planques, T.3    Robert-Nicoud, N.4    Wheland, J.5
  • 67
    • 0025294639 scopus 로고
    • Detyrosination of α tubulin does not stabilize microtubules in vivo
    • Webster, D.R., J. Wehland, K. Weber, and G.G. Borisy. 1990. Detyrosination of α tubulin does not stabilize microtubules in vivo. J. Cell Biol. 111:113-122.
    • (1990) J. Cell Biol. , vol.111 , pp. 113-122
    • Webster, D.R.1    Wehland, J.2    Weber, K.3    Borisy, G.G.4
  • 68
    • 0020580016 scopus 로고
    • Cells injected with guanosine 5′-[α,β-methylene]triphosphate, an α,β-nonhydrolyzable analog of GTP, show anomalous patterns of tubulin polymerization affecting cell translocation, intracellular movement, and the organization of Golgi elements
    • Wehland, J., and I.V. Sandoval. 1983. Cells injected with guanosine 5′-[α,β-methylene]triphosphate, an α,β-nonhydrolyzable analog of GTP, show anomalous patterns of tubulin polymerization affecting cell translocation, intracellular movement, and the organization of Golgi elements. Proc. Natl. Acad. Sci USA. 80:1938-1941.
    • (1983) Proc. Natl. Acad. Sci USA , vol.80 , pp. 1938-1941
    • Wehland, J.1    Sandoval, I.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.