메뉴 건너뛰기




Volumn 11, Issue 1, 1999, Pages 134-141

Accessory protein regulation of microtubule dynamics throughout the cell cycle

Author keywords

[No Author keywords available]

Indexed keywords

MICROTUBULE ASSOCIATED PROTEIN; TUBULIN;

EID: 0033005733     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(99)80017-9     Document Type: Article
Times cited : (162)

References (62)
  • 1
    • 0031809137 scopus 로고    scopus 로고
    • Focusing on spindle poles
    • Compton D Focusing on spindle poles. J Cell Sci. 111:1998;1477-1481.
    • (1998) J Cell Sci , vol.111 , pp. 1477-1481
    • Compton, D.1
  • 2
    • 0031466304 scopus 로고    scopus 로고
    • Microtubule polymerization dynamics
    • An excellent and thorough review of microtubule structure, assembly dynamics and functions of accessory proteins.
    • Desai A, Mitchison TJ Microtubule polymerization dynamics. Annu Rev Cell Biol. 13:1997;83-117. An excellent and thorough review of microtubule structure, assembly dynamics and functions of accessory proteins.
    • (1997) Annu Rev Cell Biol , vol.13 , pp. 83-117
    • Desai, A.1    Mitchison, T.J.2
  • 3
    • 0032966238 scopus 로고    scopus 로고
    • Actin-microtubule-intermediate filament interactions during cell spreading and motility
    • Waterman-Storer CM Actin-microtubule-intermediate filament interactions during cell spreading and motility. Curr Opin Cell Biol. 11:1999;61-67.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 61-67
    • Waterman-Storer, C.M.1
  • 4
    • 0027458626 scopus 로고
    • Observation and quantification of individual microtubule behavior in vivo: Microtubule dynamics are cell-type specific
    • Shelden E, Wadsworth P Observation and quantification of individual microtubule behavior in vivo: microtubule dynamics are cell-type specific. J Cell Biol. 120:1993;935-945.
    • (1993) J Cell Biol , vol.120 , pp. 935-945
    • Shelden, E.1    Wadsworth, P.2
  • 5
    • 0032489802 scopus 로고    scopus 로고
    • Rho guanosine triphosphate mediates the selective stabilization of microtubules induced by lysophosphatidic acid
    • Cook TA, Nagasaki T, Gundersen GG Rho guanosine triphosphate mediates the selective stabilization of microtubules induced by lysophosphatidic acid. J Cell Biol. 141:1998;175-185.
    • (1998) J Cell Biol , vol.141 , pp. 175-185
    • Cook, T.A.1    Nagasaki, T.2    Gundersen, G.G.3
  • 6
    • 0026722242 scopus 로고
    • Poleward kinetochore fiber movement occurs during both metaphase and anaphase-A in newt lung cell mitosis
    • Mitchison T, Salmon ED Poleward kinetochore fiber movement occurs during both metaphase and anaphase-A in newt lung cell mitosis. J Cell Biol. 119:1992;569-582.
    • (1992) J Cell Biol , vol.119 , pp. 569-582
    • Mitchison, T.1    Salmon, E.D.2
  • 7
    • 0030727892 scopus 로고    scopus 로고
    • Actomyosin-based retrograde flow of microtubules in the lamella of migrating epithelial cells influences microtubule dynamic instability and turnover and is associated with microtubule breakage and treadmilling
    • Waterman-Storer CM, Salmon ED Actomyosin-based retrograde flow of microtubules in the lamella of migrating epithelial cells influences microtubule dynamic instability and turnover and is associated with microtubule breakage and treadmilling. J Cell Biol. 139:1997;417-434.
    • (1997) J Cell Biol , vol.139 , pp. 417-434
    • Waterman-Storer, C.M.1    Salmon, E.D.2
  • 8
    • 0030665266 scopus 로고    scopus 로고
    • Cytoplasmic assembly of microtubules in cultured cells
    • Vorobjev IA, Svitkina TM, Borisy GG Cytoplasmic assembly of microtubules in cultured cells. J Cell Sci. 110:1997;2635-2645.
    • (1997) J Cell Sci , vol.110 , pp. 2635-2645
    • Vorobjev, I.A.1    Svitkina, T.M.2    Borisy, G.G.3
  • 9
    • 0000885332 scopus 로고    scopus 로고
    • Non-centrosomal microtubule formation and measurement of minus end microtubule dynamics in A498 cells
    • Yvon A-MC, Wadsworth P Non-centrosomal microtubule formation and measurement of minus end microtubule dynamics in A498 cells. J Cell Sci. 110:1997;2391-2401.
    • (1997) J Cell Sci , vol.110 , pp. 2391-2401
    • Yvon, A.-M.1    Wadsworth, P.2
  • 10
    • 0027385963 scopus 로고
    • How the transition frequencies of microtubule dynamic instability (nucleation, catastrophe and rescue) regulate microtubule dynamics in interphase and mitosis: Analysis using a Monte Carlo computer simulation
    • Gliksman NR, Skibbens RV, Salmon ED How the transition frequencies of microtubule dynamic instability (nucleation, catastrophe and rescue) regulate microtubule dynamics in interphase and mitosis: analysis using a Monte Carlo computer simulation. Mol Biol Cell. 4:1993;1035-1050.
    • (1993) Mol Biol Cell , vol.4 , pp. 1035-1050
    • Gliksman, N.R.1    Skibbens, R.V.2    Salmon, E.D.3
  • 11
    • 0032555923 scopus 로고    scopus 로고
    • Stepwise reconstitution of interphase microtubule dynamics in permeabilized cells and comparison to dynamic mechanisms in intact cells
    • Saoudi Y, Fotedar R, Abrieu A, Doree M, Wehland J, Margolis RL, Job D Stepwise reconstitution of interphase microtubule dynamics in permeabilized cells and comparison to dynamic mechanisms in intact cells. J Cell Biol. 142:1998;1519-1532.
    • (1998) J Cell Biol , vol.142 , pp. 1519-1532
    • Saoudi, Y.1    Fotedar, R.2    Abrieu, A.3    Doree, M.4    Wehland, J.5    Margolis, R.L.6    Job, D.7
  • 12
    • 0028231706 scopus 로고
    • Quantitative determination of the proportion of microtubule polymer during the mitosis-interphase transition
    • Zhai Y, Borisy GG Quantitative determination of the proportion of microtubule polymer during the mitosis-interphase transition. J Cell Sci. 107:1994;881-890.
    • (1994) J Cell Sci , vol.107 , pp. 881-890
    • Zhai, Y.1    Borisy, G.G.2
  • 13
    • 0029662197 scopus 로고    scopus 로고
    • 2/M transition: Abrupt breakdown of cytoplasmic microtubules at nuclear envelope breakdown and implications for spindle morphogenesis
    • 2/M transition: abrupt breakdown of cytoplasmic microtubules at nuclear envelope breakdown and implications for spindle morphogenesis. J Cell Biol. 135:1996;201-214.
    • (1996) J Cell Biol , vol.135 , pp. 201-214
    • Zhai, Y.1    Kronebusch, P.J.2    Simon, P.M.3    Borisy, G.G.4
  • 14
    • 0025109181 scopus 로고
    • Real time visualization of cell cycle dependent changes in microtubule dynamics in cytoplasmic extracts
    • Belmont LD, Hyman AA, Sawin KE, Mitchison TJ Real time visualization of cell cycle dependent changes in microtubule dynamics in cytoplasmic extracts. Cell. 62:1990;579-589.
    • (1990) Cell , vol.62 , pp. 579-589
    • Belmont, L.D.1    Hyman, A.A.2    Sawin, K.E.3    Mitchison, T.J.4
  • 15
    • 0031012281 scopus 로고    scopus 로고
    • Microtubule assembly in clarified Xenopus egg extracts
    • Parsons SF, Salmon ED Microtubule assembly in clarified Xenopus egg extracts. Cell Motil Cytoskeleton. 36:1997;1-11.
    • (1997) Cell Motil Cytoskeleton , vol.36 , pp. 1-11
    • Parsons, S.F.1    Salmon, E.D.2
  • 17
    • 0026016405 scopus 로고    scopus 로고
    • Severing of stable microtubules by a mitotically activated protein in Xenopus egg extracts
    • Vale R Severing of stable microtubules by a mitotically activated protein in Xenopus egg extracts. Cell. 4:1997;827-839.
    • (1997) Cell , vol.4 , pp. 827-839
    • Vale, R.1
  • 18
    • 0025037989 scopus 로고
    • Regulation of microtubule dynamics by cdc2 kinase in cell free extracts of Xenopus eggs
    • Verde F, Labbe J, Doree M, Karsenti E Regulation of microtubule dynamics by cdc2 kinase in cell free extracts of Xenopus eggs. Nature. 343:1990;233-238.
    • (1990) Nature , vol.343 , pp. 233-238
    • Verde, F.1    Labbe, J.2    Doree, M.3    Karsenti, E.4
  • 20
    • 0345038725 scopus 로고
    • Microtubules
    • J.S. Hymans, & C.W. Lloyd. New York: Wiley-Liss, Inc
    • Bulinski JC MAP4. Hymans JS, Lloyd CW Microtubules. 1994;167-182 Wiley-Liss, Inc, New York.
    • (1994) Wiley-Liss, Inc, New York. , pp. 167-182
    • Bulinski, J.C.1
  • 22
    • 0030925589 scopus 로고    scopus 로고
    • Mapmodulin: A possible modulator of the interaction of microtubule-associated proteins with microtubules
    • Ulitzur N, Humbert M, Pfeffer SR Mapmodulin: a possible modulator of the interaction of microtubule-associated proteins with microtubules. Proc Natl Acad Sci USA. 94:1997;5084-5089.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 5084-5089
    • Ulitzur, N.1    Humbert, M.2    Pfeffer, S.R.3
  • 23
    • 0031056220 scopus 로고    scopus 로고
    • Overexpression of full- Or partial-length MAP4 stabilizes microtubules and alters cell growth
    • Nguyen H-L, Chari S, Gruber D, Lue C-M, Chapin SJ, Bulinski JC Overexpression of full- or partial-length MAP4 stabilizes microtubules and alters cell growth. J Cell Sci. 110:1997;281-294.
    • (1997) J Cell Sci , vol.110 , pp. 281-294
    • Nguyen, H.-L.1    Chari, S.2    Gruber, D.3    Lue, C.-M.4    Chapin, S.J.5    Bulinski, J.C.6
  • 25
    • 0028037828 scopus 로고
    • Stable expression of heterologous microtubule-associated proteins (MAPs) in chinese hamster ovary cells: Evidence for differing roles of MAPs in microtubule organization
    • Barlow S, Gonzalez-Garay ML, West RR, Olmsted JB, Cabral F Stable expression of heterologous microtubule-associated proteins (MAPs) in chinese hamster ovary cells: evidence for differing roles of MAPs in microtubule organization. J Cell Biol. 126:1994;1017-1029.
    • (1994) J Cell Biol , vol.126 , pp. 1017-1029
    • Barlow, S.1    Gonzalez-Garay, M.L.2    West, R.R.3    Olmsted, J.B.4    Cabral, F.5
  • 26
    • 0011214518 scopus 로고    scopus 로고
    • Removal of MAP4 from microtubules in vivo produces no discernable phenotype at the cellular level
    • Wang XM, Peloquin JG, Zhai Y, Bulinski JC, Borisy GG Removal of MAP4 from microtubules in vivo produces no discernable phenotype at the cellular level. J Cell Biol. 132:1996;349-358.
    • (1996) J Cell Biol , vol.132 , pp. 349-358
    • Wang, X.M.1    Peloquin, J.G.2    Zhai, Y.3    Bulinski, J.C.4    Borisy, G.G.5
  • 27
    • 0027985351 scopus 로고
    • Effect on microtubule dynamics of XMAP230, a microtubule-associated protein present in Xenopus laevis eggs and dividing cells
    • Andersen SSL, Buendia B, Dominguez JE, Sawyer A, Karsenti E Effect on microtubule dynamics of XMAP230, a microtubule-associated protein present in Xenopus laevis eggs and dividing cells. J Cell Biol. 127:1994;1289-1299.
    • (1994) J Cell Biol , vol.127 , pp. 1289-1299
    • Andersen, S.S.L.1    Buendia, B.2    Dominguez, J.E.3    Sawyer, A.4    Karsenti, E.5
  • 28
    • 0030663597 scopus 로고    scopus 로고
    • XMAP310: A Xenopus rescue-promoting factor localized to the mitotic spindle
    • The authors purified a third high molecular weight MAP from Xenopus eggs, XMAP310, and examined its effects on microtubule assembly in vitro. These results, combined with those from previous studies, demonstrate that each of the high molecular weight egg MAPs has a distinct effect on microtubule assembly: XMAP215 speeds growth [29], XMAP230 inhibits catastrophes [27] and XMAP310 promotes rescues. XMAP310 is localized to the nucleus during interphase and only associates with microtubules after nuclear envelope breakdown. XMAP310 is phosphorylated during mitosis, but it is not yet known whether phosphorylation modifies its microtubule stabilizing activity.
    • Andersen SSL, Karsenti E XMAP310: a Xenopus rescue-promoting factor localized to the mitotic spindle. J Cell Biol. 139:1997;975-983. The authors purified a third high molecular weight MAP from Xenopus eggs, XMAP310, and examined its effects on microtubule assembly in vitro. These results, combined with those from previous studies, demonstrate that each of the high molecular weight egg MAPs has a distinct effect on microtubule assembly: XMAP215 speeds growth [29], XMAP230 inhibits catastrophes [27] and XMAP310 promotes rescues. XMAP310 is localized to the nucleus during interphase and only associates with microtubules after nuclear envelope breakdown. XMAP310 is phosphorylated during mitosis, but it is not yet known whether phosphorylation modifies its microtubule stabilizing activity.
    • (1997) J Cell Biol , vol.139 , pp. 975-983
    • Andersen, S.S.L.1    Karsenti, E.2
  • 29
    • 0028062756 scopus 로고
    • XMAP from Xenopus eggs promote rapid plus end assembly of microtubules and rapid microtubule polymer turnover
    • Vasquez RJ, Gard DL, Cassimeris L XMAP from Xenopus eggs promote rapid plus end assembly of microtubules and rapid microtubule polymer turnover. J Cell Biol. 127:1994;985-993.
    • (1994) J Cell Biol , vol.127 , pp. 985-993
    • Vasquez, R.J.1    Gard, D.L.2    Cassimeris, L.3
  • 31
    • 0032101370 scopus 로고    scopus 로고
    • ZYG-9, a Caenorhabditis elegans protein required for microtubule organization and function, is a component of meitotic and mitotic spindle poles
    • The zyg-9 gene encodes a 155 kDa protein which is localized to spindle poles and spindle microtubules during metaphase and early anaphase. ZYG-9 has homology to several other proteins identified in humans, Xenopus and yeasts - TOGp [30], XMAP215, p93dis1 [33] and Stu2p [32] - suggesting that these proteins may represent a family of microtubule-associated proteins which function similarly to XMAP215 and speed microtubule assembly. The previously characterized phenotypes of zyg-9 mutants suggest that the protein is active in mitosis as only short meitoic or mitotic spindles are assembled in these mutant embyros. ZYG-9 also may be active during interphase as zyg-9 mutants assemble only a short sperm aster at fertilization.
    • Matthews LR, Carter P, Thierry-Mieg D, Kemphues K ZYG-9, a Caenorhabditis elegans protein required for microtubule organization and function, is a component of meitotic and mitotic spindle poles. J Cell Biol. 141:1998;1159-1168. The zyg-9 gene encodes a 155 kDa protein which is localized to spindle poles and spindle microtubules during metaphase and early anaphase. ZYG-9 has homology to several other proteins identified in humans, Xenopus and yeasts - TOGp [30], XMAP215, p93dis1 [33] and Stu2p [32] - suggesting that these proteins may represent a family of microtubule-associated proteins which function similarly to XMAP215 and speed microtubule assembly. The previously characterized phenotypes of zyg-9 mutants suggest that the protein is active in mitosis as only short meitoic or mitotic spindles are assembled in these mutant embyros. ZYG-9 also may be active during interphase as zyg-9 mutants assemble only a short sperm aster at fertilization.
    • (1998) J Cell Biol , vol.141 , pp. 1159-1168
    • Matthews, L.R.1    Carter, P.2    Thierry-Mieg, D.3    Kemphues, K.4
  • 32
    • 0030728492 scopus 로고    scopus 로고
    • Stu2p: A microtubule-binding protein that is an essential component of the yeast spindle pole body
    • Wang PJ, Huffaker TC Stu2p: a microtubule-binding protein that is an essential component of the yeast spindle pole body. J Cell Biol. 139:1997;1271-1280.
    • (1997) J Cell Biol , vol.139 , pp. 1271-1280
    • Wang, P.J.1    Huffaker, T.C.2
  • 33
    • 0028983320 scopus 로고
    • dis1, which is required for sister chromatid separation, is a novel microtubule and spindle pole body-associating protein phosphorylated at the cdc2 target sites
    • dis1, which is required for sister chromatid separation, is a novel microtubule and spindle pole body-associating protein phosphorylated at the cdc2 target sites. Genes Dev. 9:1995;1572-1585.
    • (1995) Genes Dev , vol.9 , pp. 1572-1585
    • Nabeshima, K.1    Kurooka, H.2    Takeuchi, M.3    Kinoshita, K.4    Nakaseko, Y.5    Yanagida, M.6
  • 34
    • 0030611667 scopus 로고    scopus 로고
    • Mal3, the fission yeast homolog of the human APC-interacting protein EB-1 is required for microtubule integrity and the maintenance of cell form
    • MAL3 was isolated in a screen to find genes required for chromosome segregation in fission yeast. The MAL3 protein is localized to microtubules in vivo. Deletion of mal3+ resulted in short cytoplasmic microtubules, and overexpression of mal3+ disrupted spindle assembly. The results are consistent with MAL3 functioning to stabilize microtubules, but it is not yet known if this is through a direct interaction between MAL3 and microtubules. That overexpression of MAL3 disrupts spindle assembly is consistent with several other recent studies suggesting that a balance of microtubule stabilizers and destabilizers is necessary for spindle assembly.
    • Beinhauer JD, Hagan IM, Hegemann JH, Fleig U Mal3, the fission yeast homolog of the human APC-interacting protein EB-1 is required for microtubule integrity and the maintenance of cell form. J Cell Biol. 139:1997;717-728. MAL3 was isolated in a screen to find genes required for chromosome segregation in fission yeast. The MAL3 protein is localized to microtubules in vivo. Deletion of mal3+ resulted in short cytoplasmic microtubules, and overexpression of mal3+ disrupted spindle assembly. The results are consistent with MAL3 functioning to stabilize microtubules, but it is not yet known if this is through a direct interaction between MAL3 and microtubules. That overexpression of MAL3 disrupts spindle assembly is consistent with several other recent studies suggesting that a balance of microtubule stabilizers and destabilizers is necessary for spindle assembly.
    • (1997) J Cell Biol , vol.139 , pp. 717-728
    • Beinhauer, J.D.1    Hagan, I.M.2    Hegemann, J.H.3    Fleig, U.4
  • 35
    • 0030668145 scopus 로고    scopus 로고
    • BIM1 encodes a microtubule binding protein in yeast
    • Schwartz K, Richards K, Botstein D BIM1 encodes a microtubule binding protein in yeast. Mol Biol Cell. 8:1997;2677-2691.
    • (1997) Mol Biol Cell , vol.8 , pp. 2677-2691
    • Schwartz, K.1    Richards, K.2    Botstein, D.3
  • 36
    • 0030031999 scopus 로고    scopus 로고
    • XKCM1: A Xenopus kinesin-related protein that regulates microtubule dynamics during mitotic spindle assembly
    • Walczak CE, Mitchison TJ, Desai A XKCM1: a Xenopus kinesin-related protein that regulates microtubule dynamics during mitotic spindle assembly. Cell. 84:1996;37-47.
    • (1996) Cell , vol.84 , pp. 37-47
    • Walczak, C.E.1    Mitchison, T.J.2    Desai, A.3
  • 37
    • 0030048731 scopus 로고    scopus 로고
    • Identification of a protein that interacts with tubulin dimers and increases the catastrophe rates of microtubules
    • Belmont L, Mitchison T Identification of a protein that interacts with tubulin dimers and increases the catastrophe rates of microtubules. Cell. 84:1996;623-631.
    • (1996) Cell , vol.84 , pp. 623-631
    • Belmont, L.1    Mitchison, T.2
  • 38
    • 0028245510 scopus 로고
    • Yeast Kar3 is a minus-end microtubule motor protein that destabilizes microtubules preferentially at the minus end
    • Endow S, Kand S, Satterwhite L, Rose M, Skeen V, Salmon E Yeast Kar3 is a minus-end microtubule motor protein that destabilizes microtubules preferentially at the minus end. EMBO J. 13:1994;2708-2713.
    • (1994) EMBO J , vol.13 , pp. 2708-2713
    • Endow, S.1    Kand, S.2    Satterwhite, L.3    Rose, M.4    Skeen, V.5    Salmon, E.6
  • 39
    • 0031820278 scopus 로고    scopus 로고
    • Katanin is responsible for the M-phase microtubule severing activity in Xenopus eggs
    • cdc2 kinase and therefore it was not known whether any of these proteins was responsible for microtubule severing in M-phase Xenopus extracts. Immunodepletion studies by McNally and Thomas clearly demonstrate that this M-phase microtubule severing activity is due to the protein katanin, and suggest that an indirect mechanism, such as inactivation of microtubule stabilizing MAPs, must be responsible for activation of katanin-dependent severing during mitosis.
    • cdc2 kinase and therefore it was not known whether any of these proteins was responsible for microtubule severing in M-phase Xenopus extracts. Immunodepletion studies by McNally and Thomas clearly demonstrate that this M-phase microtubule severing activity is due to the protein katanin, and suggest that an indirect mechanism, such as inactivation of microtubule stabilizing MAPs, must be responsible for activation of katanin-dependent severing during mitosis.
    • (1998) Mol Biol Cell , vol.9 , pp. 1847-1861
    • McNally, F.J.1    Thomas, S.2
  • 40
    • 0027049935 scopus 로고
    • A novel homo-oligomeric protein responsible for an MPF-dependent microtubule severing activity
    • Shiina N, Gotoh Y, Nisida E A novel homo-oligomeric protein responsible for an MPF-dependent microtubule severing activity. EMBO J. 11:1992;4723-4731.
    • (1992) EMBO J , vol.11 , pp. 4723-4731
    • Shiina, N.1    Gotoh, Y.2    Nisida, E.3
  • 42
    • 0031873388 scopus 로고    scopus 로고
    • Mitotic centromere-associated kinesin is important for anaphase chromosome segregation
    • Maney T, Hunter AW, Wagenbach M, Wordeman L Mitotic centromere-associated kinesin is important for anaphase chromosome segregation. J Cell Biol. 142:1998;787-801.
    • (1998) J Cell Biol , vol.142 , pp. 787-801
    • Maney, T.1    Hunter, A.W.2    Wagenbach, M.3    Wordeman, L.4
  • 43
    • 0028887847 scopus 로고
    • Identification and partial characterization of mitotic centromere-associated kinesin, a kinesin-related protein that associates with centromeres during mitosis
    • Wordeman L, Mitchison T Identification and partial characterization of mitotic centromere-associated kinesin, a kinesin-related protein that associates with centromeres during mitosis. J Cell Biol. 128:1995;95-105.
    • (1995) J Cell Biol , vol.128 , pp. 95-105
    • Wordeman, L.1    Mitchison, T.2
  • 44
    • 0025745372 scopus 로고    scopus 로고
    • Stathmin: A relay phosphoprotein for multiple signal transduction?
    • Sobel, A: Stathmin: a relay phosphoprotein for multiple signal transduction? Trends Biochem Sci 16:301-305.
    • Trends Biochem Sci , vol.16 , pp. 301-305
    • Sobel, A.1
  • 46
    • 0030783012 scopus 로고    scopus 로고
    • Stathmin: A tubulin-sequestering protein which forms a ternary T2S complex with two tubulin molecules
    • Jourdain L, Curmi P, Sobel A, Pantaloni D, Carlier M-F Stathmin: a tubulin-sequestering protein which forms a ternary T2S complex with two tubulin molecules. Biochemistry. 36:1997;10817-10821.
    • (1997) Biochemistry , vol.36 , pp. 10817-10821
    • Jourdain, L.1    Curmi, P.2    Sobel, A.3    Pantaloni, D.4    Carlier, M.-F.5
  • 47
    • 0030750560 scopus 로고    scopus 로고
    • Control of microtubule dynamics by oncoprotein 18: Dissection of the regulatory role of multisite phosphorylation during mitosis
    • Using a series of kinase-site-deficient mutants of oncoprotein18/stathmin, the authors probed the functions of the four serine phosphorylation sites in this protein after mitotic phosphorylations. The cyclin-dependent kinase phosphorylation sites (Ser25 and Ser38) are required for subsequent phosphorylation of Ser16 and -68 by a second kinase. Phosphorylation at Ser25 and -38 is not sufficient to inactivate oncoprotein18/stathmin either in vivo or in vitro, while phosphorylation at Ser16 and -68 greatly diminishes the microtubule-destabilizing activity of this protein.
    • Larsson N, Marklund U, Melander Gradin H, Brattsand G, Gullberg M Control of microtubule dynamics by oncoprotein 18: dissection of the regulatory role of multisite phosphorylation during mitosis. Mol Cell Biol. 17:1997;5530-5539. Using a series of kinase-site-deficient mutants of oncoprotein18/stathmin, the authors probed the functions of the four serine phosphorylation sites in this protein after mitotic phosphorylations. The cyclin-dependent kinase phosphorylation sites (Ser25 and Ser38) are required for subsequent phosphorylation of Ser16 and -68 by a second kinase. Phosphorylation at Ser25 and -38 is not sufficient to inactivate oncoprotein18/stathmin either in vivo or in vitro, while phosphorylation at Ser16 and -68 greatly diminishes the microtubule-destabilizing activity of this protein.
    • (1997) Mol Cell Biol , vol.17 , pp. 5530-5539
    • Larsson, N.1    Marklund, U.2    Melander Gradin, H.3    Brattsand, G.4    Gullberg, M.5
  • 48
    • 0029811662 scopus 로고    scopus 로고
    • Oncoprotein 18 is a phosphorylation-responsive regulator of microtubule dynamics
    • Marklund U, Larsson N, Melander Gradin H, Brattsand G, Gullberg M Oncoprotein 18 is a phosphorylation-responsive regulator of microtubule dynamics. EMBO J. 15:1996;5290-5298.
    • (1996) EMBO J , vol.15 , pp. 5290-5298
    • Marklund, U.1    Larsson, N.2    Melander Gradin, H.3    Brattsand, G.4    Gullberg, M.5
  • 49
    • 0029062165 scopus 로고
    • 2/M transition requires multisite phosphorylation of oncoprotein 18 by two distinct protein kinase systems
    • 2/M transition requires multisite phosphorylation of oncoprotein 18 by two distinct protein kinase systems. J Biol Chem. 270:1995;14175-14183.
    • (1995) J Biol Chem , vol.270 , pp. 14175-14183
    • Larsson, N.1    Melander, H.2    Marklund, U.3    Osterman, O.4    Gullberg, M.5
  • 50
    • 0030968633 scopus 로고    scopus 로고
    • The microtubule-destabilizing activity of metablastin (p19) is controlled by phosphorylation
    • Horowitz SB, Shen H-J, He L, Dittmar P, Neef R, Chen J, Schubart UK The microtubule-destabilizing activity of metablastin (p19) is controlled by phosphorylation. J Biol Chem. 272:1997;8129-8132.
    • (1997) J Biol Chem , vol.272 , pp. 8129-8132
    • Horowitz, S.B.1    Shen, H.-J.2    He, L.3    Dittmar, P.4    Neef, R.5    Chen, J.6    Schubart, U.K.7
  • 51
    • 0030781157 scopus 로고    scopus 로고
    • Phosphorylation regulates the microtubule-destabilizing activity of stathmin and its interaction with tubulin
    • DiPaolo G, Antonsson B, Kassel D, Riederer BM, Grenningloh G Phosphorylation regulates the microtubule-destabilizing activity of stathmin and its interaction with tubulin. FEBS Lett. 416:1997;149-152.
    • (1997) FEBS Lett , vol.416 , pp. 149-152
    • Dipaolo, G.1    Antonsson, B.2    Kassel, D.3    Riederer, B.M.4    Grenningloh, G.5
  • 52
    • 0030748898 scopus 로고    scopus 로고
    • Mitotic chromatin regulates phosphorylation of stathmin/Op18
    • Using Xenopus egg extracts, the authors demonstrate that oncoprotein18/stathmin is phosphorylated (inactivated) by an activity associated with mitotic chromatin, suggesting a mechanism to spatially modify microtubule assembly dynamics. See also [57] for a related study in Xenopus egg extracts demonstrating that microtubule assembly dynamics are modified by mitotic chromatin, resulting in preferential microtubule assembly towards chromatin.
    • Andersen SSL, Ashford AJ, Tournebize R, Gavet O, Sobel A, Hyman AA, Karsenti E Mitotic chromatin regulates phosphorylation of stathmin/Op18. Nature. 389:1997;640-643. Using Xenopus egg extracts, the authors demonstrate that oncoprotein18/stathmin is phosphorylated (inactivated) by an activity associated with mitotic chromatin, suggesting a mechanism to spatially modify microtubule assembly dynamics. See also [57] for a related study in Xenopus egg extracts demonstrating that microtubule assembly dynamics are modified by mitotic chromatin, resulting in preferential microtubule assembly towards chromatin.
    • (1997) Nature , vol.389 , pp. 640-643
    • Andersen, S.S.L.1    Ashford, A.J.2    Tournebize, R.3    Gavet, O.4    Sobel, A.5    Hyman, A.A.6    Karsenti, E.7
  • 53
    • 0024094432 scopus 로고    scopus 로고
    • Dynamic instability of individual, MAP-free microtubules analyzed by video light microscopy: Rate constants and transition frequencies
    • Walker RA, O'Brien ET, Pryer NK, Soboeiro MF, Voter WA, Erickson HP, Salmon ED Dynamic instability of individual, MAP-free microtubules analyzed by video light microscopy: rate constants and transition frequencies. J Cell Biol. 107:1998;1437-1448.
    • (1998) J Cell Biol , vol.107 , pp. 1437-1448
    • Walker, R.A.1    O'Brien, E.T.2    Pryer, N.K.3    Soboeiro, M.F.4    Voter, W.A.5    Erickson, H.P.6    Salmon, E.D.7
  • 54
    • 0030933383 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae kinesin-related motor kar3p acts at pre-anaphase spindle poles to limit the number and length of cytoplasmic microtubules
    • Saunders W, Hornack D, Lengyel V, Deng C The Saccharomyces cerevisiae kinesin-related motor kar3p acts at pre-anaphase spindle poles to limit the number and length of cytoplasmic microtubules. J Cell Biol. 137:1997;417-431.
    • (1997) J Cell Biol , vol.137 , pp. 417-431
    • Saunders, W.1    Hornack, D.2    Lengyel, V.3    Deng, C.4
  • 56
    • 0026561879 scopus 로고
    • Protein phosphatase type 1 in mammalian cell mitosis: Chromosomal localization and involvement in mitotic exit
    • Fernandez A, Brautigan DL, Lamb NJC Protein phosphatase type 1 in mammalian cell mitosis: chromosomal localization and involvement in mitotic exit. J Cell Biol. 116:1992;1421-1430.
    • (1992) J Cell Biol , vol.116 , pp. 1421-1430
    • Fernandez, A.1    Brautigan, D.L.2    Lamb, N.J.C.3
  • 57
    • 0029869434 scopus 로고    scopus 로고
    • Influence of M-phase chromatin on the anisotropy of microtubule asters
    • Dogterom M, Felix M-A, Guet CC, Leibler S Influence of M-phase chromatin on the anisotropy of microtubule asters. J Cell Biol. 133:1996;125-140.
    • (1996) J Cell Biol , vol.133 , pp. 125-140
    • Dogterom, M.1    Felix, M.-A.2    Guet, C.C.3    Leibler, S.4
  • 58
    • 0030066248 scopus 로고
    • Confocal immunofluorescence microscopy of microtubules, microtubule-associated proteins, and microtubule-organizing centers during amphibian oogenesis and early development
    • Gard DL, Cha BJ, Schroeder MM Confocal immunofluorescence microscopy of microtubules, microtubule-associated proteins, and microtubule-organizing centers during amphibian oogenesis and early development. Curr Top Dev Biol. 31:1995;383-431.
    • (1995) Curr Top Dev Biol , vol.31 , pp. 383-431
    • Gard, D.L.1    Cha, B.J.2    Schroeder, M.M.3
  • 59
    • 0029943566 scopus 로고    scopus 로고
    • The pool of MAP kinase associated with microtubules is small but constitutively active
    • Morishima-Kawashima M, Kosik KS The pool of MAP kinase associated with microtubules is small but constitutively active. Mol Biol Cell. 7:1996;893-905.
    • (1996) Mol Biol Cell , vol.7 , pp. 893-905
    • Morishima-Kawashima, M.1    Kosik, K.S.2
  • 60
    • 0032101295 scopus 로고    scopus 로고
    • Differential subcellular localization of protein phosphatase-1α, γ1, and δ isoforms during both interphase and mitosis in mammalian cells
    • Andreassen PR, Lacroix FB, Villa-Moruzzi E, Margolis RL Differential subcellular localization of protein phosphatase-1α, γ1, and δ isoforms during both interphase and mitosis in mammalian cells. J Cell Biol. 141:1998;1207-1215.
    • (1998) J Cell Biol , vol.141 , pp. 1207-1215
    • Andreassen, P.R.1    Lacroix, F.B.2    Villa-Moruzzi, E.3    Margolis, R.L.4
  • 61
    • 0028924295 scopus 로고
    • A novel pool of protein phosphatase 2A is associated with microtubules and is regulated during the cell cycle
    • Sontag E, Nunbhakdi-Craig V, Bloom GS, Mumby MC A novel pool of protein phosphatase 2A is associated with microtubules and is regulated during the cell cycle. J Cell Biol. 128:1995;1131-1144.
    • (1995) J Cell Biol , vol.128 , pp. 1131-1144
    • Sontag, E.1    Nunbhakdi-Craig, V.2    Bloom, G.S.3    Mumby, M.C.4
  • 62
    • 0032923913 scopus 로고    scopus 로고
    • Dissociation of the tubulin sequestering and microtubule catastrophe-promoting activities of oncoprotein18/stathmin
    • in press.
    • Howell B, Larsson N, Gullberg M, Cassimeris L Dissociation of the tubulin sequestering and microtubule catastrophe-promoting activities of oncoprotein18/stathmin. Mol Biol Cell. 1999;. in press.
    • (1999) Mol Biol Cell
    • Howell, B.1    Larsson, N.2    Gullberg, M.3    Cassimeris, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.