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Volumn 15, Issue 1, 2003, Pages 54-59

Nuclear positioning: The means is at the ends

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; DYNEIN ADENOSINE TRIPHOSPHATASE;

EID: 0037220989     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(02)00004-2     Document Type: Review
Times cited : (81)

References (58)
  • 1
    • 0034739004 scopus 로고    scopus 로고
    • Myosin V orientates the mitotic spindle in yeast
    • Yin H., Pruyne D., Huffaker T.C., Bretscher A. Myosin V orientates the mitotic spindle in yeast. Nature. 406:2000;1013-1015.
    • (2000) Nature , vol.406 , pp. 1013-1015
    • Yin, H.1    Pruyne, D.2    Huffaker, T.C.3    Bretscher, A.4
  • 2
    • 0034735942 scopus 로고    scopus 로고
    • The role of the proteins Kar9 and Myo2 in orienting the mitotic spindle of budding yeast
    • Beach D.L., Thibodeaux J., Maddox P., Yeh E., Bloom K. The role of the proteins Kar9 and Myo2 in orienting the mitotic spindle of budding yeast. Curr Biol. 10:2000;1497-1506.
    • (2000) Curr Biol , vol.10 , pp. 1497-1506
    • Beach, D.L.1    Thibodeaux, J.2    Maddox, P.3    Yeh, E.4    Bloom, K.5
  • 3
    • 0034490532 scopus 로고    scopus 로고
    • Bim1p/Yeb1p mediates the Kar9p-dependent cortical attachment of cytoplasmic microtubules
    • Miller R.K., Cheng S.C., Rose M.D. Bim1p/Yeb1p mediates the Kar9p-dependent cortical attachment of cytoplasmic microtubules. Mol Biol Cell. 11:2000;2949-2959.
    • (2000) Mol Biol Cell , vol.11 , pp. 2949-2959
    • Miller, R.K.1    Cheng, S.C.2    Rose, M.D.3
  • 4
    • 0034708606 scopus 로고    scopus 로고
    • Positioning of the mitotic spindle by a cortical-microtubule capture mechanism
    • Lee L., Tirnauer J.S., Li J., Schuyler S.C., Liu J.Y., Pellman D. Positioning of the mitotic spindle by a cortical-microtubule capture mechanism. Science. 287:2000;2260-2262.
    • (2000) Science , vol.287 , pp. 2260-2262
    • Lee, L.1    Tirnauer, J.S.2    Li, J.3    Schuyler, S.C.4    Liu, J.Y.5    Pellman, D.6
  • 5
    • 0034708459 scopus 로고    scopus 로고
    • Molecular linkage underlying microtubule orientation toward cortical sites in yeast
    • Korinek W.S., Copeland M.J., Chaudhuri A., Chant J. Molecular linkage underlying microtubule orientation toward cortical sites in yeast. Science. 287:2000;2257-2259.
    • (2000) Science , vol.287 , pp. 2257-2259
    • Korinek, W.S.1    Copeland, M.J.2    Chaudhuri, A.3    Chant, J.4
  • 6
    • 0034657914 scopus 로고    scopus 로고
    • Microtubule interactions with the cell cortex causing nuclear movements in Saccharomyces cerevisiae
    • Adames N.R., Cooper J.A. Microtubule interactions with the cell cortex causing nuclear movements in Saccharomyces cerevisiae. J Cell Biol. 149:2000;863-874.
    • (2000) J Cell Biol , vol.149 , pp. 863-874
    • Adames, N.R.1    Cooper, J.A.2
  • 7
    • 0034638845 scopus 로고    scopus 로고
    • The cortical protein Num1p is essential for dynein-dependent interactions of microtubules with the cortex
    • Heil-Chapdelaine R.A., Oberle J.R., Cooper J.A. The cortical protein Num1p is essential for dynein-dependent interactions of microtubules with the cortex. J Cell Biol. 151:2000;1337-1344.
    • (2000) J Cell Biol , vol.151 , pp. 1337-1344
    • Heil-Chapdelaine, R.A.1    Oberle, J.R.2    Cooper, J.A.3
  • 8
    • 0035931754 scopus 로고    scopus 로고
    • Cortical Num1p interacts with the dynein intermediate chain Pac11p and cytoplasmic microtubules in budding yeast
    • In addition to the interaction described in the title of this paper, the authors also show, as in Adames and Cooper (2000) [6] and Farkasovsky and Kuntzel (2000) [7], that the bud tip location of GFP-Num1p does not require Kar9p, Dyn1p or cytoplasmic MTs, but does require the formin Bni1p.
    • Farkasovsky M., Kuntzel H. Cortical Num1p interacts with the dynein intermediate chain Pac11p and cytoplasmic microtubules in budding yeast. J Cell Biol. 152:2001;251-262 In addition to the interaction described in the title of this paper, the authors also show, as in Adames and Cooper (2000) [6] and Farkasovsky and Kuntzel (2000) [7], that the bud tip location of GFP-Num1p does not require Kar9p, Dyn1p or cytoplasmic MTs, but does require the formin Bni1p.
    • (2001) J Cell Biol , vol.152 , pp. 251-262
    • Farkasovsky, M.1    Kuntzel, H.2
  • 9
    • 0035661650 scopus 로고    scopus 로고
    • Dynamic behavior of microtubules during dynein-dependent nuclear migrations of meiotic prophase in fission yeast
    • Nuclei of Schizosaccharomyces pombe undergo vigorous oscillations between the poles of the cell at meiotic prophase. GFP-tagged spindle pole body MTs lead these nuclear oscillations and interact distally with the cell cortex in wild-type cells, but not in dynein mutants. The authors propose a model in which nuclear oscillations are driven by cortical/microtubule interactions and the dynamics of microtubule disassembly at the cortex.
    • Yamamoto A., Tsutsumi C., Kojima H., Oiwa K., Hiraoka Y. Dynamic behavior of microtubules during dynein-dependent nuclear migrations of meiotic prophase in fission yeast. Mol Biol Cell. 12:2001;3933-3946 Nuclei of Schizosaccharomyces pombe undergo vigorous oscillations between the poles of the cell at meiotic prophase. GFP-tagged spindle pole body MTs lead these nuclear oscillations and interact distally with the cell cortex in wild-type cells, but not in dynein mutants. The authors propose a model in which nuclear oscillations are driven by cortical/microtubule interactions and the dynamics of microtubule disassembly at the cortex.
    • (2001) Mol Biol Cell , vol.12 , pp. 3933-3946
    • Yamamoto, A.1    Tsutsumi, C.2    Kojima, H.3    Oiwa, K.4    Hiraoka, Y.5
  • 10
    • 0036195236 scopus 로고    scopus 로고
    • The 14-kDa dynein light chain-family protein Dlc1 is required for regular oscillatory nuclear movement and efficient recombination during meiotic prophase in Fission Yeast
    • Dlc1 belongs to the Tctex family of dynein light chains.
    • Miki F., Okazaki K., Shimanuki M., Yamamoto A., Hiraoka Y., Niwa O. The 14-kDa dynein light chain-family protein Dlc1 is required for regular oscillatory nuclear movement and efficient recombination during meiotic prophase in Fission Yeast. Mol Biol Cell. 13:2002;930-946 Dlc1 belongs to the Tctex family of dynein light chains.
    • (2002) Mol Biol Cell , vol.13 , pp. 930-946
    • Miki, F.1    Okazaki, K.2    Shimanuki, M.3    Yamamoto, A.4    Hiraoka, Y.5    Niwa, O.6
  • 11
    • 0342265157 scopus 로고    scopus 로고
    • Cytoplasmic dynein is required for distinct aspects of MTOC positioning, including centrosome separation, in the one cell stage Caenorhabditis elegans embryo
    • Gonczy P., Pichler S., Kirkham M., Hyman A.A. Cytoplasmic dynein is required for distinct aspects of MTOC positioning, including centrosome separation, in the one cell stage Caenorhabditis elegans embryo. J Cell Biol. 147:1999;135-150.
    • (1999) J Cell Biol , vol.147 , pp. 135-150
    • Gonczy, P.1    Pichler, S.2    Kirkham, M.3    Hyman, A.A.4
  • 12
    • 0035166346 scopus 로고    scopus 로고
    • Cytoplasmic dynein light intermediate chain is required for discrete aspects of mitosis in Caenorhabditis elegans
    • Yoder J.H., Han M. Cytoplasmic dynein light intermediate chain is required for discrete aspects of mitosis in Caenorhabditis elegans. Mol Biol Cell. 12:2001;2921-2933.
    • (2001) Mol Biol Cell , vol.12 , pp. 2921-2933
    • Yoder, J.H.1    Han, M.2
  • 13
    • 0035694702 scopus 로고    scopus 로고
    • Unc-83 encodes a novel component of the nuclear envelope and is essential for proper nuclear migration
    • Starr D.A., Hermann G.J., Malone C.J., Fixsen W., Priess J.R., Horvitz H.R., Han M. unc-83 encodes a novel component of the nuclear envelope and is essential for proper nuclear migration. Development. 128:2001;5039-5050.
    • (2001) Development , vol.128 , pp. 5039-5050
    • Starr, D.A.1    Hermann, G.J.2    Malone, C.J.3    Fixsen, W.4    Priess, J.R.5    Horvitz, H.R.6    Han, M.7
  • 14
    • 0036193442 scopus 로고    scopus 로고
    • Lamin-dependent localization of UNC-84, a protein required for nuclear migration in Caenorhabditis elegans
    • This interesting paper establishes a physical basis for the nuclear envelope localization of UNC-84.
    • Lee K.K., Starr D., Cohen M., Liu J., Han M., Wilson K.L., Gruenbaum Y. Lamin-dependent localization of UNC-84, a protein required for nuclear migration in Caenorhabditis elegans. Mol Biol Cell. 13:2002;892-901 This interesting paper establishes a physical basis for the nuclear envelope localization of UNC-84.
    • (2002) Mol Biol Cell , vol.13 , pp. 892-901
    • Lee, K.K.1    Starr, D.2    Cohen, M.3    Liu, J.4    Han, M.5    Wilson, K.L.6    Gruenbaum, Y.7
  • 16
    • 0033224241 scopus 로고    scopus 로고
    • Drosophila Lissencephaly-1 functions with Bic-D and dynein in oocyte determination and nuclear positioning
    • Swan A., Nguyen T., Suter B. Drosophila Lissencephaly-1 functions with Bic-D and dynein in oocyte determination and nuclear positioning. Nat Cell Biol. 1:1999;444-449.
    • (1999) Nat Cell Biol , vol.1 , pp. 444-449
    • Swan, A.1    Nguyen, T.2    Suter, B.3
  • 17
    • 0034287451 scopus 로고    scopus 로고
    • The Drosophila lissencephaly1 (DLis1) gene is required for nuclear migration
    • Lei Y., Warrior R. The Drosophila lissencephaly1 (DLis1) gene is required for nuclear migration. Dev Biol. 226:2000;57-72.
    • (2000) Dev Biol , vol.226 , pp. 57-72
    • Lei, Y.1    Warrior, R.2
  • 18
    • 0033523985 scopus 로고    scopus 로고
    • Molecular analysis of the Klarsicht gene and its role in nuclear migration within differentiating cells of the Drosophila eye
    • Mosley-Bishop K.L., Li Q., Patterson L., Fischer J.A. Molecular analysis of the Klarsicht gene and its role in nuclear migration within differentiating cells of the Drosophila eye. Curr Biol. 9:1999;1211-1220.
    • (1999) Curr Biol , vol.9 , pp. 1211-1220
    • Mosley-Bishop, K.L.1    Li, Q.2    Patterson, L.3    Fischer, J.A.4
  • 19
    • 0034194602 scopus 로고    scopus 로고
    • Dynamics of cytoplasmic dynein in living cells and the effect of a mutation in the dynactin complex actin-related protein Arp1
    • Xiang X., Han G., Winkelmann D.A., Zuo W., Morris N.R. Dynamics of cytoplasmic dynein in living cells and the effect of a mutation in the dynactin complex actin-related protein Arp1. Curr Biol. 10:2000;603-606.
    • (2000) Curr Biol , vol.10 , pp. 603-606
    • Xiang, X.1    Han, G.2    Winkelmann, D.A.3    Zuo, W.4    Morris, N.R.5
  • 20
    • 0035336825 scopus 로고    scopus 로고
    • The Aspergillus cytoplasmic dynein heavy chain and NUDF localize to microtubule ends and affect microtubule dynamics
    • In addition to reporting that Aspergillus cytoplasmic dynein heavy chain and NUDF localize to microtubule ends and affect microtubule dynamics, this paper also contains useful references to earlier papers demonstrating that NUDF is required for dynein function.
    • Han G., Liu B., Zhang J., Zuo W., Morris N.R., Xiang X. The Aspergillus cytoplasmic dynein heavy chain and NUDF localize to microtubule ends and affect microtubule dynamics. Curr Biol. 11:2001;719-724 In addition to reporting that Aspergillus cytoplasmic dynein heavy chain and NUDF localize to microtubule ends and affect microtubule dynamics, this paper also contains useful references to earlier papers demonstrating that NUDF is required for dynein function.
    • (2001) Curr Biol , vol.11 , pp. 719-724
    • Han, G.1    Liu, B.2    Zhang, J.3    Zuo, W.4    Morris, N.R.5    Xiang, X.6
  • 21
    • 0036231905 scopus 로고    scopus 로고
    • Cytoplasmic dynein intermediate chain and heavy chain are dependent upon each other for microtubule end localization in Aspergillus nidulans
    • The authors use mutations and GFP-labeled proteins to show that localization of the dynein intermediate and heavy chains to MT plus ends in A. nidulans requires both dynein subunits. They also demonstrate that heavy chain localization to MT plus ends requires NUDF, the A. nidulans homolog of mammalian Lis1.
    • Zhang J., Han G., Xiang X. Cytoplasmic dynein intermediate chain and heavy chain are dependent upon each other for microtubule end localization in Aspergillus nidulans. Mol Microbiol. 44:2002;381-392 The authors use mutations and GFP-labeled proteins to show that localization of the dynein intermediate and heavy chains to MT plus ends in A. nidulans requires both dynein subunits. They also demonstrate that heavy chain localization to MT plus ends requires NUDF, the A. nidulans homolog of mammalian Lis1.
    • (2002) Mol Microbiol , vol.44 , pp. 381-392
    • Zhang, J.1    Han, G.2    Xiang, X.3
  • 22
    • 0035723385 scopus 로고    scopus 로고
    • Genetic evidence for a microtubule-destabilizing effect of conventional kinesin and analysis of its consequences for the control of nuclear distribution in Aspergillus nidulans
    • Requena N., Alberti-Segui C., Winzenburg E., Horn C., Schliwa M., Philippsen P., Liese R., Fischer R. Genetic evidence for a microtubule-destabilizing effect of conventional kinesin and analysis of its consequences for the control of nuclear distribution in Aspergillus nidulans. Mol Microbiol. 42:2001;121-132.
    • (2001) Mol Microbiol , vol.42 , pp. 121-132
    • Requena, N.1    Alberti-Segui, C.2    Winzenburg, E.3    Horn, C.4    Schliwa, M.5    Philippsen, P.6    Liese, R.7    Fischer, R.8
  • 23
    • 0035166330 scopus 로고    scopus 로고
    • Null mutants of the Neurospora actin-related protein 1 pointed-end complex show distinct phenotypes
    • This paper demonstrates that the abnormal hyphal morphology of ropy mutants is not a necessary consequence of the nuclear migration defect seen in most of these mutants. Although mutations in the RO2 (p65), RO7 (Arp11), and RO12 (p25) subunits of the dynactin pointed end complex have abnormal curled hyphae, as do all the other Neurospora crassa ropy mutants, nuclear distribution is normal in RO12.
    • Lee I.H., Kumar S., Plamann M. Null mutants of the Neurospora actin-related protein 1 pointed-end complex show distinct phenotypes. Mol Biol Cell. 12:2001;2195-2206 This paper demonstrates that the abnormal hyphal morphology of ropy mutants is not a necessary consequence of the nuclear migration defect seen in most of these mutants. Although mutations in the RO2 (p65), RO7 (Arp11), and RO12 (p25) subunits of the dynactin pointed end complex have abnormal curled hyphae, as do all the other Neurospora crassa ropy mutants, nuclear distribution is normal in RO12.
    • (2001) Mol Biol Cell , vol.12 , pp. 2195-2206
    • Lee, I.H.1    Kumar, S.2    Plamann, M.3
  • 24
    • 0034044840 scopus 로고    scopus 로고
    • Ami1, an orthologue of the Aspergillus nidulans apsA gene, is involved in nuclear migration events throughout the life cycle of Podospora anserina
    • Graia F., Berteaux-Lecellier V., Zickler D., Picard M. ami1, an orthologue of the Aspergillus nidulans apsA gene, is involved in nuclear migration events throughout the life cycle of Podospora anserina. Genetics. 155:2000;633-646.
    • (2000) Genetics , vol.155 , pp. 633-646
    • Graia, F.1    Berteaux-Lecellier, V.2    Zickler, D.3    Picard, M.4
  • 25
    • 0035057843 scopus 로고    scopus 로고
    • Cytoplasmic dynein is required to oppose the force that moves nuclei towards the hyphal tip in the filamentous ascomycete Ashbya gossypii
    • In contrast to other fungi in which dynein ablation causes nuclei to be clustered at the spore end of the hyphae, dynein ablation in Ashbyacauses nuclei to be clustered at the hyphal tips.
    • Alberti-Segui C., Dietrich F., Altmann-Johl R., Hoepfner D., Philippsen P. Cytoplasmic dynein is required to oppose the force that moves nuclei towards the hyphal tip in the filamentous ascomycete Ashbya gossypii. J Cell Sci. 114:2001;975-986 In contrast to other fungi in which dynein ablation causes nuclei to be clustered at the spore end of the hyphae, dynein ablation in Ashbyacauses nuclei to be clustered at the hyphal tips.
    • (2001) J Cell Sci , vol.114 , pp. 975-986
    • Alberti-Segui, C.1    Dietrich, F.2    Altmann-Johl, R.3    Hoepfner, D.4    Philippsen, P.5
  • 28
    • 0033535340 scopus 로고    scopus 로고
    • Microtubule dynamics from mating through the first zygotic division in the budding yeast Saccharomyces cerevisiae
    • Maddox P., Chin E., Mallavarapu A., Yeh E., Salmon E.D., Bloom K. Microtubule dynamics from mating through the first zygotic division in the budding yeast Saccharomyces cerevisiae. J Cell Biol. 144:1999;977-987.
    • (1999) J Cell Biol , vol.144 , pp. 977-987
    • Maddox, P.1    Chin, E.2    Mallavarapu, A.3    Yeh, E.4    Salmon, E.D.5    Bloom, K.6
  • 29
    • 0035897404 scopus 로고    scopus 로고
    • A mechanism for nuclear positioning in fission yeast based on microtubule pushing
    • Using GFP-tubulin to visualize microtubules (MTs), the authors demonstrate that cytoplasmic MTs emanating from the nucleus dynamically sense the positions of the ends of the cell and maintain the nucleus in the center of the cell by pushing against the ends.
    • Tran P.T., Marsh L., Doye V., Inoue S., Chang F. A mechanism for nuclear positioning in fission yeast based on microtubule pushing. J Cell Biol. 153:2001;397-411 Using GFP-tubulin to visualize microtubules (MTs), the authors demonstrate that cytoplasmic MTs emanating from the nucleus dynamically sense the positions of the ends of the cell and maintain the nucleus in the center of the cell by pushing against the ends.
    • (2001) J Cell Biol , vol.153 , pp. 397-411
    • Tran, P.T.1    Marsh, L.2    Doye, V.3    Inoue, S.4    Chang, F.5
  • 30
    • 0035166773 scopus 로고    scopus 로고
    • Single site alpha-tubulin mutation affects astral microtubules and nuclear positioning during anaphase in Saccharomyces cerevisiae: Possible role for palmitoylation of alpha-tubulin
    • Caron J.M., Vega L.R., Fleming J., Bishop R., Solomon F. Single site alpha-tubulin mutation affects astral microtubules and nuclear positioning during anaphase in Saccharomyces cerevisiae: possible role for palmitoylation of alpha-tubulin. Mol Biol Cell. 12:2001;2672-2687.
    • (2001) Mol Biol Cell , vol.12 , pp. 2672-2687
    • Caron, J.M.1    Vega, L.R.2    Fleming, J.3    Bishop, R.4    Solomon, F.5
  • 31
    • 0035951060 scopus 로고    scopus 로고
    • Mutation in the beta-tubulin signature motif suppresses microtubule GTPase activity and dynamics, and slows mitosis
    • ••] affects nuclear positioning. The import of these two papers for dynein-mediated nuclear positioning is that because microtubule dynamics affect nuclear positioning, the effect of dynein on positioning could just as well be mediated via an effect of dynein on microtubule dynamics as by dynein motor activity per se.
    • ••] affects nuclear positioning. The import of these two papers for dynein-mediated nuclear positioning is that because microtubule dynamics affect nuclear positioning, the effect of dynein on positioning could just as well be mediated via an effect of dynein on microtubule dynamics as by dynein motor activity per se.
    • (2001) Biochemistry , vol.40 , pp. 15725-15732
    • Dougherty, C.A.1    Sage, C.R.2    Davis, A.3    Farrell, K.W.4
  • 32
    • 0034618076 scopus 로고    scopus 로고
    • The Lis1-related NUDF protein of Aspergillus nidulans interacts with the coiled-coil domain of the NUDE/RO11 protein
    • Efimov V.P., Morris N.R. The Lis1-related NUDF protein of Aspergillus nidulans interacts with the coiled-coil domain of the NUDE/RO11 protein. J Cell Biol. 150:2000;681-688.
    • (2000) J Cell Biol , vol.150 , pp. 681-688
    • Efimov, V.P.1    Morris, N.R.2
  • 33
    • 0036235403 scopus 로고    scopus 로고
    • Lis1, CLIP-170's key to the dynein/dynactin pathway
    • This paper provides evidence that Lis1 acts as an adaptor between CLIP-170 and cytoplasmic dynein by demonstrating that they colocalize and interact physically.
    • Coquelle F.M., Caspi M., Cordelieres F.P., Dompierre J.P., Dujardin D.L., Koifman C., Martin P., Hoogenraad C.C., Akhmanova A., Galjart N.et al. Lis1, CLIP-170's key to the dynein/dynactin pathway. Mol Cell Biol. 22:2002;3089-3102 This paper provides evidence that Lis1 acts as an adaptor between CLIP-170 and cytoplasmic dynein by demonstrating that they colocalize and interact physically.
    • (2002) Mol Cell Biol , vol.22 , pp. 3089-3102
    • Coquelle, F.M.1    Caspi, M.2    Cordelieres, F.P.3    Dompierre, J.P.4    Dujardin, D.L.5    Koifman, C.6    Martin, P.7    Hoogenraad, C.C.8    Akhmanova, A.9    Galjart, N.10
  • 34
    • 0033051741 scopus 로고    scopus 로고
    • Colocalization of cytoplasmic dynein with dynactin and CLIP-170 at microtubule distal ends
    • 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.
    • (1999) J Cell Sci , vol.112 , pp. 1437-1447
    • Vaughan, K.T.1    Tynan, S.H.2    Faulkner, N.E.3    Echeverri, C.J.4    Vallee, R.B.5
  • 35
    • 0032756658 scopus 로고    scopus 로고
    • Role of dynactin in endocytic traffic: Effects of dynamitin overexpression and colocalization with CLIP-170A
    • 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-170A. Mol Biol Cell. 10:1999;4107-4120.
    • (1999) Mol Biol Cell , vol.10 , pp. 4107-4120
    • 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
  • 36
    • 0037157845 scopus 로고    scopus 로고
    • A role for regulated binding of p150(Glued) to microtubule plus ends in organelle transport
    • glued to microtubule plus ends is modulated by phosphorylation. Of particular interest is a demonstration that interactions between microtubule plus ends and Golgi membranes precede centripetal, dynein-mediated membrane transport.
    • glued to microtubule plus ends is modulated by phosphorylation. Of particular interest is a demonstration that interactions between microtubule plus ends and Golgi membranes precede centripetal, dynein-mediated membrane transport.
    • (2002) J Cell Biol , vol.158 , pp. 305-319
    • Vaughan, P.S.1    Miura, P.2    Henderson, M.3    Byrne, B.4    Vaughan, K.T.5
  • 38
    • 17744372880 scopus 로고    scopus 로고
    • Clasps are CLIP-115 and -170 associating proteins involved in the regional regulation of microtubule dynamics in motile fibroblasts
    • The CLASP proteins are found on distal segments of microtubules oriented toward the leading edge of migrating cells. The authors provide evidence that CLASPs regulate MT dynamics in response to positional clues.
    • 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 The CLASP proteins are found on distal segments of microtubules oriented toward the leading edge of migrating cells. The authors provide evidence that CLASPs regulate MT dynamics in response to positional clues.
    • (2001) Cell , vol.104 , pp. 923-935
    • Akhmanova, A.1    Hoogenraad, C.C.2    Drabek, K.3    Stepanova, T.4    Dortland, B.5    Verkerk, T.6    Vermeulen, W.7    Burgering, B.M.8    De Zeeuw, C.I.9    Grosveld, F.10    Galjart, N.11
  • 39
    • 0037054547 scopus 로고    scopus 로고
    • The adenomatous polyposis coli protein unambiguously localizes to microtubule plus ends and is involved in establishing parallel arrays of microtubule bundles in highly polarized epithelial cells
    • It had previously been shown (see Mimori-Kiyosue et al. [2000] [41]) that EB1, a protein associated with the adenomatous polyposis coli (APC) protein, is found at the plus ends of microtubules. This paper rounds out the picture by showing that APC co-locates with EB1 at microtubule plus ends in polarized epithelial cells in which microtubule polarity has been definitively established by hook decoration. The authors show that in mice heterozygous for APC, there are fewer microtubule bundles, suggesting that the presence of APC stabilizes microtubules.
    • Mogensen M.M., Tucker J.B., Mackie J.B., Prescott A.R., Nathke I.S. The adenomatous polyposis coli protein unambiguously localizes to microtubule plus ends and is involved in establishing parallel arrays of microtubule bundles in highly polarized epithelial cells. J Cell Biol. 157:2002;1041-1048 It had previously been shown (see Mimori-Kiyosue et al. [2000] [41]) that EB1, a protein associated with the adenomatous polyposis coli (APC) protein, is found at the plus ends of microtubules. This paper rounds out the picture by showing that APC co-locates with EB1 at microtubule plus ends in polarized epithelial cells in which microtubule polarity has been definitively established by hook decoration. The authors show that in mice heterozygous for APC, there are fewer microtubule bundles, suggesting that the presence of APC stabilizes microtubules.
    • (2002) J Cell Biol , vol.157 , pp. 1041-1048
    • Mogensen, M.M.1    Tucker, J.B.2    Mackie, J.B.3    Prescott, A.R.4    Nathke, I.S.5
  • 40
    • 0035176077 scopus 로고    scopus 로고
    • Binding of the adenomatous polyposis coli protein to microtubules increases microtubule stability and is regulated by GSK3 beta phosphorylation
    • Zumbrunn J., Kinoshita K., Hyman A.A., Nathke I.S. Binding of the adenomatous polyposis coli protein to microtubules increases microtubule stability and is regulated by GSK3 beta phosphorylation. Curr Biol. 11:2001;44-49.
    • (2001) Curr Biol , vol.11 , pp. 44-49
    • Zumbrunn, J.1    Kinoshita, K.2    Hyman, A.A.3    Nathke, I.S.4
  • 41
    • 0034644119 scopus 로고    scopus 로고
    • The dynamic behavior of the APC-binding protein EB1 on the distal ends of microtubules
    • Mimori-Kiyosue Y., Shiina N., Tsukita S. The dynamic behavior of the APC-binding protein EB1 on the distal ends of microtubules. Curr Biol. 10:2000;865-868.
    • (2000) Curr Biol , vol.10 , pp. 865-868
    • Mimori-Kiyosue, Y.1    Shiina, N.2    Tsukita, S.3
  • 42
    • 0036469076 scopus 로고    scopus 로고
    • Dynein at the cortex
    • This review summarizes the evidence for cortical dynein.
    • Dujardin D., Vallee R.B. Dynein at the cortex. Curr Opin Cell Biol. 14:2002;44-49 This review summarizes the evidence for cortical dynein.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 44-49
    • Dujardin, D.1    Vallee, R.B.2
  • 44
    • 0035502933 scopus 로고    scopus 로고
    • Actin-dependent membrane association of the APC tumour suppressor in polarized mammalian epithelial cells
    • Rosin-Arbesfeld R., Ihrke G., Bienz M. Actin-dependent membrane association of the APC tumour suppressor in polarized mammalian epithelial cells. EMBO J. 20:2001;5929-5939.
    • (2001) EMBO J , vol.20 , pp. 5929-5939
    • Rosin-Arbesfeld, R.1    Ihrke, G.2    Bienz, M.3
  • 45
    • 18444369936 scopus 로고    scopus 로고
    • Rac1 and Cdc42 capture microtubules through IQGAP1 and CLIP-170
    • This beautiful paper demonstrates that IQGAP1, an effector of the Rac1 and Cdc42 GTPases, interact with the microtubule plus-end protein CLIP-170 to target the plus ends of cytoplasmic microtubules to the polarized cell cortex.
    • 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 beautiful paper demonstrates that IQGAP1, an effector of the Rac1 and Cdc42 GTPases, interact with the microtubule plus-end protein CLIP-170 to target the plus ends of cytoplasmic microtubules to the polarized cell cortex.
    • (2002) Cell , vol.109 , pp. 873-885
    • Fukata, M.1    Watanabe, T.2    Noritake, J.3    Nakagawa, M.4    Yamaga, M.5    Kuroda, S.6    Matsuura, Y.7    Iwamatsu, A.8    Perez, F.9    Kaibuchi, K.10
  • 46
    • 0036000019 scopus 로고    scopus 로고
    • PLAC-24 is a cytoplasmic dynein-binding protein that is recruited to sites of cell-cell contact
    • Karki S., Ligon L.A., DeSantis J., Tokito M., Holzbaur E.L. PLAC-24 is a cytoplasmic dynein-binding protein that is recruited to sites of cell-cell contact. Mol Biol Cell. 13:2002;1722-1734.
    • (2002) Mol Biol Cell , vol.13 , pp. 1722-1734
    • Karki, S.1    Ligon, L.A.2    DeSantis, J.3    Tokito, M.4    Holzbaur, E.L.5
  • 47
    • 0033538842 scopus 로고    scopus 로고
    • Cytoplasmic dynein is required for the nuclear attachment and migration of centrosomes during mitosis in Drosophila
    • Robinson J.T., Wojcik E.J., Sanders M.A., McGrail M., Hays T.S. Cytoplasmic dynein is required for the nuclear attachment and migration of centrosomes during mitosis in Drosophila. J Cell Biol. 146:1999;597-608.
    • (1999) J Cell Biol , vol.146 , pp. 597-608
    • Robinson, J.T.1    Wojcik, E.J.2    Sanders, M.A.3    McGrail, M.4    Hays, T.S.5
  • 48
    • 0035943401 scopus 로고    scopus 로고
    • Integrin-mediated activation of Cdc42 controls cell polarity in migrating astrocytes through PKCzeta
    • Cells migrating into a wound re-orient their microtubule organizing center and microtubules by a dynein-requiring process initiated by the interaction of integrins with the extracellular matrix.
    • Etienne-Manneville S., Hall A. Integrin-mediated activation of Cdc42 controls cell polarity in migrating astrocytes through PKCzeta. Cell. 106:2001;489-498 Cells migrating into a wound re-orient their microtubule organizing center and microtubules by a dynein-requiring process initiated by the interaction of integrins with the extracellular matrix.
    • (2001) Cell , vol.106 , pp. 489-498
    • Etienne-Manneville, S.1    Hall, A.2
  • 49
    • 0034907213 scopus 로고    scopus 로고
    • MDia mediates Rho-regulated formation and orientation of stable microtubules
    • Palazzo A.F., Cook T.A., Alberts A.S., Gundersen G.G. mDia mediates Rho-regulated formation and orientation of stable microtubules. Nat Cell Biol. 3:2001;723-729.
    • (2001) Nat Cell Biol , vol.3 , pp. 723-729
    • Palazzo, A.F.1    Cook, T.A.2    Alberts, A.S.3    Gundersen, G.G.4
  • 52
    • 0035893238 scopus 로고    scopus 로고
    • NUDC associates with Lis1 and the dynein motor at the leading pole of neurons
    • NUDC co-localizes with Lis1 and the cytoplasmic dynein intermediate chain in a polarized manner at the microtubule organizing center in migrating cerebellar granule cells. It also co-immunoprecipitates with CDIC and cytoplasmic dynein. These data suggest that a functional interaction of NUDC with Lis1 and dynein underlies neuronal migration.
    • Aumais J.P., Tunstead J.R., McNeil R.S., Schaar B.T., McConnell S.K., Lin S.H., Clark G.D., Yu-Lee L.Y. NUDC associates with Lis1 and the dynein motor at the leading pole of neurons. J Neurosci. 21:2001;RC187 NUDC co-localizes with Lis1 and the cytoplasmic dynein intermediate chain in a polarized manner at the microtubule organizing center in migrating cerebellar granule cells. It also co-immunoprecipitates with CDIC and cytoplasmic dynein. These data suggest that a functional interaction of NUDC with Lis1 and dynein underlies neuronal migration.
    • (2001) J Neurosci , vol.21 , pp. 187
    • Aumais, J.P.1    Tunstead, J.R.2    McNeil, R.S.3    Schaar, B.T.4    McConnell, S.K.5    Lin, S.H.6    Clark, G.D.7    Yu-Lee, L.Y.8
  • 53
    • 0034637504 scopus 로고    scopus 로고
    • Direct association of Lis1, the lissencephaly gene product, with a mammalian homologue of a fungal nuclear distribution protein, rNUDE
    • Kitagawa M., Umezu M., Aoki J., Koizumi H., Arai H., Inoue K. Direct association of Lis1, the lissencephaly gene product, with a mammalian homologue of a fungal nuclear distribution protein, rNUDE. FEBS Lett. 479:2000;57-62.
    • (2000) FEBS Lett. , vol.479 , pp. 57-62
    • Kitagawa, M.1    Umezu, M.2    Aoki, J.3    Koizumi, H.4    Arai, H.5    Inoue, K.6
  • 54
    • 0037128930 scopus 로고    scopus 로고
    • Role of dynein, dynactin, and CLIP-170 interactions in Lis1 kinetochore function
    • Tai C.Y., Dujardin D.L., Faulkner N.E., Vallee R.B. Role of dynein, dynactin, and CLIP-170 interactions in Lis1 kinetochore function. J Cell Biol. 156:2002;959-968.
    • (2002) J Cell Biol , vol.156 , pp. 959-968
    • Tai, C.Y.1    Dujardin, D.L.2    Faulkner, N.E.3    Vallee, R.B.4
  • 56
    • 0035914441 scopus 로고    scopus 로고
    • The Lis1-related protein NUDF of Aspergillus nidulans and its interaction partner NUDE bind directly to specific subunits of dynein and dynactin and to alpha- and gamma-tubulin
    • Although this paper deals only with Aspergillus proteins, their interactions are similar to those described for Lis1 and mammalian NUDE.
    • Hoffmann B., Zuo W., Liu A., Morris N.R. The Lis1-related protein NUDF of Aspergillus nidulans and its interaction partner NUDE bind directly to specific subunits of dynein and dynactin and to alpha- and gamma-tubulin. J Biol Chem. 276:2001;38877-38884 Although this paper deals only with Aspergillus proteins, their interactions are similar to those described for Lis1 and mammalian NUDE.
    • (2001) J Biol Chem , vol.276 , pp. 38877-38884
    • Hoffmann, B.1    Zuo, W.2    Liu, A.3    Morris, N.R.4
  • 57
    • 0035834037 scopus 로고    scopus 로고
    • Nuclear envelope proteomics: Novel integral membrane proteins of the inner nuclear membrane
    • Dreger M., Bengtsson L., Schoneberg T., Otto H., Hucho F. Nuclear envelope proteomics: novel integral membrane proteins of the inner nuclear membrane. Proc Natl Acad Sci USA. 98:2001;11943-11948.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 11943-11948
    • Dreger, M.1    Bengtsson, L.2    Schoneberg, T.3    Otto, H.4    Hucho, F.5
  • 58
    • 0034644646 scopus 로고    scopus 로고
    • Syne-1, a dystrophin- and Klarsicht-related protein associated with synaptic nuclei at the neuromuscular junction
    • Apel E.D., Lewis R.M., Grady R.M., Sanes J.R. Syne-1, a dystrophin- and Klarsicht-related protein associated with synaptic nuclei at the neuromuscular junction. J Biol Chem. 275:2000;31986-31995.
    • (2000) J Biol Chem , vol.275 , pp. 31986-31995
    • Apel, E.D.1    Lewis, R.M.2    Grady, R.M.3    Sanes, J.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.