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Cell motility: Can Rho GTPases and microtubules point the way?
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Diamantopoulos G.S., Perez F., Goodson H.V., Batelier G., Melki R., Kreis T.E., Rickard J.E. Dynamic localization of CLIP-170 to microtubule plus ends is coupled to microtubule assembly. J. Cell Biol. 144:1999;99-112.
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Schuyler, S.C.1
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CLIP-170 links endocytic vesicles to microtubules
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0037073702
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Crystal structure of the cytoskeleton-associated protein (CAP-Gly) domain
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published online September 7 2002, 10.1074/jbc.M208512200
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Li S, Finley J, Liu ZJ, Qiu SH, Chen H, Luan CH, Carson M, Tsao J, Johnson D, Lin G et al.: Crystal structure of the cytoskeleton-associated protein (CAP-Gly) domain. J Biol Chem 2002, published online September 7 2002, 10.1074/jbc.M208512200.
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Li, S.1
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Liu, Z.J.3
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Chen, H.5
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Carson, M.7
Tsao, J.8
Johnson, D.9
Lin, G.10
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9
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0037128212
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CLIPR-59, a new trans-Golgi/TGN cytoplasmic linker protein belonging to the CLIP-170 family
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Perez F., Pernet-Gallay K., Nizak C., Goodson H.V., Kreis T.E., Goud B. CLIPR-59, a new trans-Golgi/TGN cytoplasmic linker protein belonging to the CLIP-170 family. J. Cell Biol. 156:2002;631-642.
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Perez, F.1
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Kreis, T.E.5
Goud, B.6
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10
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0033545205
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Alf1p, a CLIP-170 domain-containing protein, is functionally and physically associated with alpha-tubulin
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Feierbach B., Nogales E., Downing K.H., Stearns T. Alf1p, a CLIP-170 domain-containing protein, is functionally and physically associated with alpha-tubulin. J. Cell Biol. 144:1999;113-124.
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12
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Rickard, J.E.1
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0036774805
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The FKBP12-rapamycin-associated protein (FRAP) is a CLIP-170 kinase
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Choi J.H., Bertram P.G., Drenan R., Carvalho J., Zhou H.H., Zheng X.F. The FKBP12-rapamycin-associated protein (FRAP) is a CLIP-170 kinase. EMBO Rep. 13:2002;13.
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Choi, J.H.1
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Zhou, H.H.5
Zheng, X.F.6
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14
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0037157845
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glued to microtubule plus ends in organelle transport
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glued-labelled microtubules just before transport, implicating microtubules and dynactin in a search-and-capture mechanism for minus-end-directed organelles.
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glued-labelled microtubules just before transport, implicating microtubules and dynactin in a search-and-capture mechanism for minus-end-directed organelles.
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Vaughan, P.S.1
Miura, P.2
Henderson, M.3
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Vaughan, K.T.5
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15
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0036270763
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The subcellular destinations of APC proteins
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Bienz M. The subcellular destinations of APC proteins. Nat. Rev. Mol. Cell Biol. 3:2002;328-338.
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Bienz, M.1
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16
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0029066006
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APC binds to the novel protein EB1
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Su L.K., Burrell M., Hill D.E., Gyuris J., Brent R., Wiltshire R., Trent J., Vogelstein B., Kinzler K.W. APC binds to the novel protein EB1. Cancer Res. 55:1995;2972-2977.
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Su, L.K.1
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Brent, R.5
Wiltshire, R.6
Trent, J.7
Vogelstein, B.8
Kinzler, K.W.9
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17
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0034614936
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Adenomatous polyposis coli (APC) protein moves along microtubules and concentrates at their growing ends in epithelial cells
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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.
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Mimori-Kiyosue, Y.1
Shiina, N.2
Tsukita, S.3
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18
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0037089076
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Dissecting interactions between EB1, microtubules and APC in cortical clusters at the plasma membrane
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Barth A.I., Siemers K.A., Nelson W.J. Dissecting interactions between EB1, microtubules and APC in cortical clusters at the plasma membrane. J. Cell Sci. 115:2002;1583-1590.
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Barth, A.I.1
Siemers, K.A.2
Nelson, W.J.3
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19
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0036226855
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Identification of a link between the tumour suppressor APC and the kinesin superfamily
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APC, a tumour suppressor protein, is known to interact with the microtubule cytoskeleton. It has been localised to cortical protein clusters, absent in APC-deficient cancer cells, near the distal ends of microtubules, at the edges of migrating epithelial cells. The authors show that APC interacts with the kinesin superfamily KIF3A and KIF3B proteins, through an association with the kinesin-superfamily-associated protein 3 (KAP3), and that KAP3 is necessary for peripheral APC localisation. The APC-KIF3A/3B-KAP3 complex also contains β-catenin, raising the intriguing possibility that KAP3-KIF3A/KIF3B transport APC-β-catenin to the leading edge to regulate cell migration.
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Jimbo T., Kawasaki Y., Koyama R., Sato R., Takada S., Haraguchi K., Akiyama T. Identification of a link between the tumour suppressor APC and the kinesin superfamily. Nat. Cell Biol. 4:2002;323-327 APC, a tumour suppressor protein, is known to interact with the microtubule cytoskeleton. It has been localised to cortical protein clusters, absent in APC-deficient cancer cells, near the distal ends of microtubules, at the edges of migrating epithelial cells. The authors show that APC interacts with the kinesin superfamily KIF3A and KIF3B proteins, through an association with the kinesin-superfamily-associated protein 3 (KAP3), and that KAP3 is necessary for peripheral APC localisation. The APC-KIF3A/3B-KAP3 complex also contains β-catenin, raising the intriguing possibility that KAP3-KIF3A/KIF3B transport APC-β-catenin to the leading edge to regulate cell migration.
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Nat. Cell Biol.
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Jimbo, T.1
Kawasaki, Y.2
Koyama, R.3
Sato, R.4
Takada, S.5
Haraguchi, K.6
Akiyama, T.7
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20
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0036711845
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Life cycle of MTs: Persistent growth in the cell interior, asymmetric transition frequencies and effects of the cell boundary
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Combining different imaging methods, microtubule dynamics were investigated in CHO and NRK cells both at cell centre and edge. Microtubule dynamics is very different at the cell centre, were growth is persistent, and at the cell periphery where it appeared more stochastic, with frequent shortening and rescues.
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Komarova Y.A., Vorobjev I.A., Borisy G.G. Life cycle of MTs: persistent growth in the cell interior, asymmetric transition frequencies and effects of the cell boundary. J. Cell Sci. 115:2002;3527-3539 Combining different imaging methods, microtubule dynamics were investigated in CHO and NRK cells both at cell centre and edge. Microtubule dynamics is very different at the cell centre, were growth is persistent, and at the cell periphery where it appeared more stochastic, with frequent shortening and rescues.
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J. Cell Sci.
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Komarova, Y.A.1
Vorobjev, I.A.2
Borisy, G.G.3
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21
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0034644119
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The dynamic behavior of the APC-binding protein EB1 on the distal ends of microtubules
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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.
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Mimori-Kiyosue, Y.1
Shiina, N.2
Tsukita, S.3
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22
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0036798432
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EB1-microtubule interactions in Xenopus egg extracts: Role of EB1 in microtubule stabilization and mechanisms of targeting to microtubules
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A detailed analysis of EB1 binding to microtubules (MTs) in the presence of Xenopus extracts reveals different modes of distribution over the MT lattice and divergent effects on MT polymerisation, depending on the extract used. Plus-end accumulation is explained by a higher affinity for a structural and/or chemical property of the tip, although EB1 also has affinity for the 'older' MT wall. Release from the MT lattice occurs with first-order kinetics.
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Tirnauer J.S., Grego S., Salmon E.D., Mitchison T.J. EB1-microtubule interactions in Xenopus egg extracts: role of EB1 in microtubule stabilization and mechanisms of targeting to microtubules. Mol. Biol. Cell. 13:2002;3614-3626 A detailed analysis of EB1 binding to microtubules (MTs) in the presence of Xenopus extracts reveals different modes of distribution over the MT lattice and divergent effects on MT polymerisation, depending on the extract used. Plus-end accumulation is explained by a higher affinity for a structural and/or chemical property of the tip, although EB1 also has affinity for the 'older' MT wall. Release from the MT lattice occurs with first-order kinetics.
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(2002)
Mol. Biol. Cell
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Tirnauer, J.S.1
Grego, S.2
Salmon, E.D.3
Mitchison, T.J.4
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24
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0037182583
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Roles of fission yeast tea1p in the localization of polarity factors and in organizing the microtubular cytoskeleton
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Tea1p is a cell-end marker involved in microtubule organisation in the yeast S. pombe. This study shows that it localises at microtubule polymerising ends and that its movement is independent of the Tea2p kinesin. The authors also show that localisation at plus end and to the cell cortex depends on different domains, and fulfil different functions: maintenance of linear growth and retention of cortical factors, respectively.
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Behrens R., Nurse P. Roles of fission yeast tea1p in the localization of polarity factors and in organizing the microtubular cytoskeleton. J. Cell Biol. 157:2002;783-793 Tea1p is a cell-end marker involved in microtubule organisation in the yeast S. pombe. This study shows that it localises at microtubule polymerising ends and that its movement is independent of the Tea2p kinesin. The authors also show that localisation at plus end and to the cell cortex depends on different domains, and fulfil different functions: maintenance of linear growth and retention of cortical factors, respectively.
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J. Cell Biol.
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Behrens, R.1
Nurse, P.2
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25
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0036645506
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Microtubule capture by the cleavage apparatus is required for proper spindle positioning in yeast
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This study defines a new microtubule capture site at the yeast bud neck and shows it is required to position the spindle relative to the cleavage apparatus. Capture requires the septins and the microtubule (MT)-associated protein Kar9. MT attachment at the bud neck is followed by shrinkage and a pulling action on the spindle, which requires the Par1- related, septin-dependent kinases Hsl1 and Gin4. These results indicate that septins and septin-dependent kinases may coordinate MT and actin functions in cell division.
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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 This study defines a new microtubule capture site at the yeast bud neck and shows it is required to position the spindle relative to the cleavage apparatus. Capture requires the septins and the microtubule (MT)-associated protein Kar9. MT attachment at the bud neck is followed by shrinkage and a pulling action on the spindle, which requires the Par1- related, septin-dependent kinases Hsl1 and Gin4. These results indicate that septins and septin-dependent kinases may coordinate MT and actin functions in cell division.
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Genes Dev.
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Kusch, J.1
Meyer, A.2
Snyder, M.P.3
Barral, Y.4
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26
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0034266786
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CLIP170-like tip1p spatially organizes microtubular dynamics in fission yeast
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Brunner D., Nurse P. CLIP170-like tip1p spatially organizes microtubular dynamics in fission yeast. Cell. 102:2000;695-704.
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Cell
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Brunner, D.1
Nurse, P.2
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27
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0012356446
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CLIPs promote MT rescue in vivo
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in press
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Komarova YA, Akhmanova AS, Kojima S-I, Galjart N, Borisy GG: CLIPs promote MT rescue in vivo. J Cell Biol 2002, in press.
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(2002)
J Cell Biol
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Komarova, Y.A.1
Akhmanova, A.S.2
Kojima, S.-I.3
Galjart, N.4
Borisy, G.G.5
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28
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0037009077
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Drosophila EB1 is important for proper assembly, dynamics, and positioning of the mitotic spindle
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Depletion of EB1 by RNA-mediated inhibition (RNAi) in interphase cells causes a dramatic increase in nondynamic microtubules (MTs), although it does not alter the overall MT organisation. In mitotic cells, strong defects in spindle MT organisation and positioning are observed upon EB1 depletion. Similar results are obtained after EB1 perturbation in the embryo, where its inhibition leads to defects in spindle elongation and chromosomal segregation.
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Rogers S.L., Rogers G.C., Sharp D.J., Vale R.D. Drosophila EB1 is important for proper assembly, dynamics, and positioning of the mitotic spindle. J. Cell Biol. 158:2002;873-884 Depletion of EB1 by RNA-mediated inhibition (RNAi) in interphase cells causes a dramatic increase in nondynamic microtubules (MTs), although it does not alter the overall MT organisation. In mitotic cells, strong defects in spindle MT organisation and positioning are observed upon EB1 depletion. Similar results are obtained after EB1 perturbation in the embryo, where its inhibition leads to defects in spindle elongation and chromosomal segregation.
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J. Cell Biol.
, vol.158
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Rogers, S.L.1
Rogers, G.C.2
Sharp, D.J.3
Vale, R.D.4
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29
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0033620650
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Yeast Bim1p promotes the G1-specific dynamics of microtubules
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Tirnauer J.S., O'Toole E., Berrueta L., Bierer B.E., Pellman D. Yeast Bim1p promotes the G1-specific dynamics of microtubules. J. Cell Biol. 145:1999;993-1007.
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Tirnauer, J.S.1
O'Toole, E.2
Berrueta, L.3
Bierer, B.E.4
Pellman, D.5
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30
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18444369936
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Rac1 and Cdc42 capture microtubules through IQGAP1 and CLIP-170
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This study links the actin-based control of cell polarity to microtubule (MT) plus-end dynamics by documenting the interaction of activated Rac1/Cdc42, their effector IQGAP1 and the plus-end tracking protein CLIP-170. This interaction seems necessary to ensure efficient control of MT dynamics and growth polarity.
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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 study links the actin-based control of cell polarity to microtubule (MT) plus-end dynamics by documenting the interaction of activated Rac1/Cdc42, their effector IQGAP1 and the plus-end tracking protein CLIP-170. This interaction seems necessary to ensure efficient control of MT dynamics and growth polarity.
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Cell
, vol.109
, pp. 873-885
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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
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31
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0035985157
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Centrosome reorientation in wound-edge cells is cell type specific
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The re-orientation of the microtubule (MT)-organising centre and the re-organisation of the MT network during cell migration into a wound are compared between Chinese hamster ovary (CHO) and PtK (rat kangeroo) cell lines. This study shows that these cytoskeletal rearrangements are not universal but depend on cell type. Photoactivation experiments shows that coherent movement of MTs in the direction of migration is observed in CHO cells and not in Ptk cells. In CHO cells, centrosome movement requires dynamic MTs and cytoplasmic dynein, and can be prevented by increasing cell-cell adhesion.
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Yvon A.M., Walker J.W., Danowski B., Fagerstrom C., Khodjakov A., Wadsworth P. Centrosome reorientation in wound-edge cells is cell type specific. Mol. Biol. Cell. 13:2002;1871-1880 The re-orientation of the microtubule (MT)-organising centre and the re-organisation of the MT network during cell migration into a wound are compared between Chinese hamster ovary (CHO) and PtK (rat kangeroo) cell lines. This study shows that these cytoskeletal rearrangements are not universal but depend on cell type. Photoactivation experiments shows that coherent movement of MTs in the direction of migration is observed in CHO cells and not in Ptk cells. In CHO cells, centrosome movement requires dynamic MTs and cytoplasmic dynein, and can be prevented by increasing cell-cell adhesion.
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(2002)
Mol. Biol. Cell
, vol.13
, pp. 1871-1880
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Yvon, A.M.1
Walker, J.W.2
Danowski, B.3
Fagerstrom, C.4
Khodjakov, A.5
Wadsworth, P.6
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32
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0035797905
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Cdc42, dynein, and dynactin regulate MTOC reorientation independent of Rho-regulated microtubule stabilization
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Palazzo A.F., Joseph H.L., Chen Y.J., Dujardin D.L., Alberts A.S., Pfister K.K., Vallee R.B., Gundersen G.G. Cdc42, dynein, and dynactin regulate MTOC reorientation independent of Rho-regulated microtubule stabilization. Curr. Biol. 11:2001;1536-1541.
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Palazzo, A.F.1
Joseph, H.L.2
Chen, Y.J.3
Dujardin, D.L.4
Alberts, A.S.5
Pfister, K.K.6
Vallee, R.B.7
Gundersen, G.G.8
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33
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0035943401
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Integrin-mediated activation of Cdc42 controls cell polarity in migrating astrocytes through PKCzeta
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Etienne-Manneville S., Hall A. Integrin-mediated activation of Cdc42 controls cell polarity in migrating astrocytes through PKCzeta. Cell. 106:2001;489-498.
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Cell
, vol.106
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Etienne-Manneville, S.1
Hall, A.2
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34
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0032756658
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Role of dynactin in endocytic traffic: Effects of dynamitin overexpression and colocalization with CLIP-170
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Valetti C., Wetzel D.M., Schrader M., Hasbani M.J., Gill S.R., Kreis T.E., Schroer T.A. Role of dynactin in endocytic traffic: effects of dynamitin overexpression and colocalization with CLIP-170. Mol. Biol. Cell. 10:1999;4107-4120.
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Mol. Biol. Cell
, vol.10
, pp. 4107-4120
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Valetti, C.1
Wetzel, D.M.2
Schrader, M.3
Hasbani, M.J.4
Gill, S.R.5
Kreis, T.E.6
Schroer, T.A.7
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35
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0033051741
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Colocalization of cytoplasmic dynein with dynactin and CLIP-170 at microtubule distal ends
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Vaughan K.T., Tynan S.H., Faulkner N.E., Echeverri C.J., Vallee R.B. Colocalization of cytoplasmic dynein with dynactin and CLIP-170 at microtubule distal ends. J. Cell Sci. 112:1999;1437-1447.
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, vol.112
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Vaughan, K.T.1
Tynan, S.H.2
Faulkner, N.E.3
Echeverri, C.J.4
Vallee, R.B.5
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36
-
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0036724985
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Targeted mutation of Cyln2 in the Williams syndrome critical region links CLIP-115 haploinsufficiency to neurodevelopmental abnormalities in mice
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Hoogenraad C.C., Koekkoek B., Akhmanova A., Krugers H., Dortland B., Miedema M., Van Alphen A., Kistler W.M., Jaegle M., Koutsourakis M.et al. Targeted mutation of Cyln2 in the Williams syndrome critical region links CLIP-115 haploinsufficiency to neurodevelopmental abnormalities in mice. Nat. Genet. 32:2002;116-127.
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Nat. Genet.
, vol.32
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Hoogenraad, C.C.1
Koekkoek, B.2
Akhmanova, A.3
Krugers, H.4
Dortland, B.5
Miedema, M.6
Van Alphen, A.7
Kistler, W.M.8
Jaegle, M.9
Koutsourakis, M.10
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37
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17744372880
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Clasps are CLIP-115 and -170 associating proteins involved in the regional regulation of microtubule dynamics in motile fibroblasts
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Akhmanova A., Hoogenraad C.C., Drabek K., Stepanova T., Dortland B., Verkerk T., Vermeulen W., Burgering B.M., De Zeeuw C.I., Grosveld F., Galjart N. Clasps are CLIP-115 and -170 associating proteins involved in the regional regulation of microtubule dynamics in motile fibroblasts. Cell. 104:2001;923-935.
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Cell
, vol.104
, pp. 923-935
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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
Galjart, N.11
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38
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0033594549
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The APC-associated protein EB1 associates with components of the dynactin complex and cytoplasmic dynein intermediate chain
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Berrueta L., Tirnauer J.S., Schuyler S.C., Pellman D., Bierer B.E. The APC-associated protein EB1 associates with components of the dynactin complex and cytoplasmic dynein intermediate chain. Curr. Biol. 9:1999;425-428.
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