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Beyond self assembly: From microtubules to morphogenesis
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This is an excellent review that summarizes models of how Op18 and XKCM1 regulate microtubule dynamics. The author provides a model to explain how distinct mechanisms of catastrophe promotion can affect either one or both ends of a microtubule.
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McNally F.J. Microtubule dynamics: controlling split ends. Curr Biol. 9:1999;R274-R276. This is an excellent review that summarizes models of how Op18 and XKCM1 regulate microtubule dynamics. The author provides a model to explain how distinct mechanisms of catastrophe promotion can affect either one or both ends of a microtubule.
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Identification of a protein that interacts with tubulin dimers and increases the catastrophe rate of microtubules
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Serine 25 of oncoprotein 18 is a major cytosolic target for the mitogen-activated protein kinase
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Marklund U., Brattsand G., Shingler V., Gullberg M. Serine 25 of oncoprotein 18 is a major cytosolic target for the mitogen-activated protein kinase. J Biol Chem. 268:1993;15039-15047.
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Marklund, U.1
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The phenotype of a 'Cdc2 kinase target site-deficient' mutant of oncoprotein 18 reveals a role of this protein in cell cycle control
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Marklund U., Osterman O., Melander H., Bergh A., Gullberg M. The phenotype of a 'Cdc2 kinase target site-deficient' mutant of oncoprotein 18 reveals a role of this protein in cell cycle control. J Biol Chem. 269:1994;30626-30635.
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Marklund, U.1
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15
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0030748898
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Mitotic chromatin regulates phosphorylation of Stathmin/Op18
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Andersen S.S.L., Ashford A.J., Tournebize R., Gavet O.A.S., Hyman A.A., Karsenti E. Mitotic chromatin regulates phosphorylation of Stathmin/Op18. Nature. 389:1997;640-643.
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Andersen, S.S.L.1
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Hyman, A.A.5
Karsenti, E.6
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16
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The stathmin/tubulin interaction in vitro
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Curmi P.A., Andersen S.S., Lachkar S., Gavet O., Karsenti E., Knossow M., Sobel A. The stathmin/tubulin interaction in vitro. J Biol Chem. 272:1997;25029-25036.
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Curmi, P.A.1
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Sobel, A.7
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17
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Stathmin: A tubulin-sequestering protein which forms a ternary T2S complex with two tubulin molecules
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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.
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Jourdain, L.1
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0032923913
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Dissociation of the tubulin-sequestering and microtubule catastrophe-promoting activities of oncoprotein 18/stathmin
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This paper describes an in vitro study in which the authors are able to dissect the catastrophe-promoting activity of Op18 from its tubulin sequestering activity. They show that, at pH 6.8, Op18 acted primarily via tubulin sequestering but, at pH 7.5, it was primarily a catastrophe factor. In addition, they showed that truncation of the carboxy-terminal domain caused a loss of tubulin sequestering activity, whereas truncation of the amino-terminal domain resulted in a protein that was unable to cause catastrophes at pH 7.5.
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Howell B., Larsson N., Gullberg M., Cassimeris L. Dissociation of the tubulin-sequestering and microtubule catastrophe-promoting activities of oncoprotein 18/stathmin. Mol Biol Cell. 10:1999;105-118. This paper describes an in vitro study in which the authors are able to dissect the catastrophe-promoting activity of Op18 from its tubulin sequestering activity. They show that, at pH 6.8, Op18 acted primarily via tubulin sequestering but, at pH 7.5, it was primarily a catastrophe factor. In addition, they showed that truncation of the carboxy-terminal domain caused a loss of tubulin sequestering activity, whereas truncation of the amino-terminal domain resulted in a protein that was unable to cause catastrophes at pH 7.5.
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Mol Biol Cell
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Howell, B.1
Larsson, N.2
Gullberg, M.3
Cassimeris, L.4
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19
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0033019054
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Mutations of oncoprotein 18/stathmin identify tubulin-directed regulatory activities distinct from tubulin association
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These authors generated a series of mutations of the gene encoding Op18. The mutant proteins were altered either in the putative coiled-coil domain or at all four phosphorylation sites. Both had only a slightly decreased tubulin binding activity. In addition, the coiled-coil mutant had a marked effect on microtubule destabilizing activity, demonstrating that tubulin binding and microtubule destabilization activity could be separated.
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Larsson N., Segerman B., Gradin H.M., Wandzioch E., Cassimeris L., Gulberg M. Mutations of oncoprotein 18/stathmin identify tubulin-directed regulatory activities distinct from tubulin association. Mol Cell Biol. 19:1999;2242-2250. These authors generated a series of mutations of the gene encoding Op18. The mutant proteins were altered either in the putative coiled-coil domain or at all four phosphorylation sites. Both had only a slightly decreased tubulin binding activity. In addition, the coiled-coil mutant had a marked effect on microtubule destabilizing activity, demonstrating that tubulin binding and microtubule destabilization activity could be separated.
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Mol Cell Biol
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Larsson, N.1
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Gulberg, M.6
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20
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Decreasing oncoprotein 18/stathmin levels reduces microtubule catastrophes and increases microtubule polymer in vivo
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Op18 antibodies were injected into interphase newt lung cells. The authors found that inhibition of Op18 via microinjection resulted in an increase in microtubule polymer levels and a reduction in the catastrophe frequency of individual microtubules. Treatment of cells with Op18 antisense oligonucleotides also reduced the catastrophe frequency of microtubules.
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Howell B., Deacon H., Cassimeris L. Decreasing oncoprotein 18/stathmin levels reduces microtubule catastrophes and increases microtubule polymer in vivo. J Cell Sci. 112:1999;3713-3722. Op18 antibodies were injected into interphase newt lung cells. The authors found that inhibition of Op18 via microinjection resulted in an increase in microtubule polymer levels and a reduction in the catastrophe frequency of individual microtubules. Treatment of cells with Op18 antisense oligonucleotides also reduced the catastrophe frequency of microtubules.
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Howell, B.1
Deacon, H.2
Cassimeris, L.3
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21
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Op18/stathmin mediates multiple region-specific tubulin and microtubule regulating activities
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These authors carried out deletion analysis of Op18 to determine its effect on tubulin binding, GTP hydrolysis and exchange, and microtubule destabilization activity. Deletion mutants, in which either the amino terminus or the carboxyl terminus was removed, were unable to complex with tubulin in cells, yet they were able to affect the microtubule cytoskeleton. The deletion analysis also revealed that Op18 contains domains that can either inhibit nucleotide exchange, stimulate GTP hydrolysis, or inhibit GTP hydrolysis.
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Larsson N., Segerman B., Howell B., Fridell K., Cassimeris L., Gullberg M. Op18/stathmin mediates multiple region-specific tubulin and microtubule regulating activities. J Cell Biol. 146:1999;1286-1302. These authors carried out deletion analysis of Op18 to determine its effect on tubulin binding, GTP hydrolysis and exchange, and microtubule destabilization activity. Deletion mutants, in which either the amino terminus or the carboxyl terminus was removed, were unable to complex with tubulin in cells, yet they were able to affect the microtubule cytoskeleton. The deletion analysis also revealed that Op18 contains domains that can either inhibit nucleotide exchange, stimulate GTP hydrolysis, or inhibit GTP hydrolysis.
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J Cell Biol
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Larsson, N.1
Segerman, B.2
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Gullberg, M.6
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22
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Tubulin dynamics in cultured mammalian cells
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0025109181
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Real-time visualization of cell cycle dependent changes in microtubule dynamics in cytoplasmic extracts
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Belmont L.D., Hyman A.A., Sawin K.E., Mitchison T.J. Real-time visualization of cell cycle dependent changes in microtubule dynamics in cytoplasmic extracts. Cell. 62:1990;579-589.
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24
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0026775358
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Control of microtubule dynamics and length by cyclin A- And cyclin B-dependent kinases in Xenopus egg extracts
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Verde F., Dogterom M., Stelzer E., Karsenti E., Leibler S. Control of microtubule dynamics and length by cyclin A- and cyclin B-dependent kinases in Xenopus egg extracts. J Cell Biol. 118:1992;1097-1108.
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25
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0030750560
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Control of microtubule dynamics by oncoprotein 18: Dissection of the regulatory role of multisite phosphorylation during mitosis
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Larsson N., Marklund U., Gradin H.M., 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.
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Gullberg, M.5
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26
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0031941941
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Regulation of microtubule dynamics by extracellular signals: CAMP-dependent protein kinase switches off the activity of oncoprotein 18 in intact cells
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This study shows that phosphorylation of Op18 on Ser16 and Ser63 by protein kinase A results in downregulation of Op18 activity toward microtubules both in vitro with purified tubulin and by transfection into tissue culture cells.
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Melander Gradin H., Larsson N., Marklund U., Gullberg M. Regulation of microtubule dynamics by extracellular signals: cAMP-dependent protein kinase switches off the activity of oncoprotein 18 in intact cells. J Cell Biol. 140:1998;131-141. This study shows that phosphorylation of Op18 on Ser16 and Ser63 by protein kinase A results in downregulation of Op18 activity toward microtubules both in vitro with purified tubulin and by transfection into tissue culture cells.
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J Cell Biol
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Melander Gradin, H.1
Larsson, N.2
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28
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The stathmin phosphoprotein family: Intracellular localization and effects on the microtubule network
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Gavet O., Ozon S., Manceau V., Lawler S., Curmi P., Sobel A. The stathmin phosphoprotein family: intracellular localization and effects on the microtubule network. J Cell Sci. 111:1998;3333-3346.
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Gavet, O.1
Ozon, S.2
Manceau, V.3
Lawler, S.4
Curmi, P.5
Sobel, A.6
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29
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0030031999
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XKCM1: A Xenopus kinesin-related protein that regulates microtubule dynamics during mitotic spindle assembly
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Walczak C.E., Mitchison T.J., Desai A. XKCM1: a Xenopus kinesin-related protein that regulates microtubule dynamics during mitotic spindle assembly. Cell. 84:1996;37-47.
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Walczak, C.E.1
Mitchison, T.J.2
Desai, A.3
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30
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0033534575
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Kin I kinesins are microtubule-destabilizing enzymes
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The authors used a series of in vitro assays to demonstrate that two members of the Kin I subfamily of kinesins act exclusively as microtubule-destabilizing enzymes. The mechanism of microtubule destabilization is distinct from the mechanisms of motility established for other kinesins.
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Desai A., Verma S., Mitchison T.J., Walczak C.E. Kin I kinesins are microtubule-destabilizing enzymes. Cell. 96:1999;69-78. The authors used a series of in vitro assays to demonstrate that two members of the Kin I subfamily of kinesins act exclusively as microtubule-destabilizing enzymes. The mechanism of microtubule destabilization is distinct from the mechanisms of motility established for other kinesins.
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(1999)
Cell
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Desai, A.1
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Control of microtubule dynamics requires the antagonistic activities of XMAP215 and XKCM1
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in press. The authors use the Xenopus egg extract system to explore the relationship between the stabilizing effects of MAPs versus the destabilizing effects of the catastrophe promoter XKCM1. They find that XKCM1 is active as a catastrophe promoter during interphase but that it does not stimulate catastrophes because of the stabilizing influence of MAPs.
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Tournebize R., Popov A., Kinoshita K., Ashford A.J., Rybina S., Mayer T., Walczak C.E., Karsenti E., Hyman A.A. Control of microtubule dynamics requires the antagonistic activities of XMAP215 and XKCM1. Nat Cell Biol. 2000;. in press. The authors use the Xenopus egg extract system to explore the relationship between the stabilizing effects of MAPs versus the destabilizing effects of the catastrophe promoter XKCM1. They find that XKCM1 is active as a catastrophe promoter during interphase but that it does not stimulate catastrophes because of the stabilizing influence of MAPs.
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(2000)
Nat Cell Biol
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Tournebize, R.1
Popov, A.2
Kinoshita, K.3
Ashford, A.J.4
Rybina, S.5
Mayer, T.6
Walczak, C.E.7
Karsenti, E.8
Hyman, A.A.9
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