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Volumn 773, Issue , 2014, Pages 505-520

Connecting the nucleus to the cytoskeleton for nuclear positioning and cell migration

Author keywords

Actin cytoskeleton; Cell migration; Centrosome reorientation; LINC complex; Nuclear envelope; Nuclear positioning; Nucleo cytoskeletal connections

Indexed keywords

CELL MEMBRANE PROTEIN; MYOSIN ADENOSINE TRIPHOSPHATASE; PROTEIN NESPRIN; PROTEIN SAMP1; PROTEIN SUN; UNCLASSIFIED DRUG;

EID: 84934443069     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4899-8032-8_23     Document Type: Article
Times cited : (17)

References (58)
  • 1
    • 71549123700 scopus 로고    scopus 로고
    • Nuclei take a position: Managing nuclear location
    • doi: 10.1016/j.devcel.2009.10.018
    • Burke B, Roux KJ (2009) Nuclei take a position: managing nuclear location. Dev Cell 17: 587-597. doi: 10.1016/j.devcel.2009.10.018
    • (2009) Dev Cell , vol.17 , pp. 587-597
    • Burke, B.1    Roux, K.J.2
  • 2
    • 0037439661 scopus 로고    scopus 로고
    • ANChors away: An actin based mechanism of nuclear positioning
    • Starr DA, Han M (2003) ANChors away: an actin based mechanism of nuclear positioning. J Cell Sci 116:211-216
    • (2003) J Cell Sci , vol.116 , pp. 211-216
    • Starr, D.A.1    Han, M.2
  • 3
    • 71549117899 scopus 로고    scopus 로고
    • The nuclear envelope as a signaling node in development and disease
    • doi: 10.1016/j.devcel.2009.10.016
    • Dauer WT, Worman HJ (2009) The nuclear envelope as a signaling node in development and disease. Dev Cell 17:626-638. doi: 10.1016/j.devcel.2009.10.016
    • (2009) Dev Cell , vol.17 , pp. 626-638
    • Dauer, W.T.1    Worman, H.J.2
  • 4
    • 0034708375 scopus 로고    scopus 로고
    • Viscoelastic properties of the cell nucleus
    • doi: 10.1006/bbrc.2000.2360
    • Guilak F, Tedrow JR, Burgkart R (2000) Viscoelastic properties of the cell nucleus. Biochem Biophys Res Commun 269:781-786. doi: 10.1006/bbrc.2000. 2360
    • (2000) Biochem Biophys Res Commun , vol.269 , pp. 781-786
    • Guilak, F.1    Tedrow, J.R.2    Burgkart, R.3
  • 7
    • 0037220989 scopus 로고    scopus 로고
    • Nuclear positioning: The means is at the ends
    • Morris NR (2003) Nuclear positioning: the means is at the ends. Curr Opin Cell Biol 15:54-59
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 54-59
    • Morris, N.R.1
  • 8
    • 0032772929 scopus 로고    scopus 로고
    • UNC-84 localizes to the nuclear envelope and is required for nuclear migration and anchoring during C. Elegans development
    • Malone CJ, Fixsen WD, Horvitz HR, Han M (1999) UNC-84 localizes to the nuclear envelope and is required for nuclear migration and anchoring during C. Elegans development. Development 126:3171-3181
    • (1999) Development , vol.126 , pp. 3171-3181
    • Malone, C.J.1    Fixsen, W.D.2    Horvitz, H.R.3    Han, M.4
  • 9
    • 0031716602 scopus 로고    scopus 로고
    • Mechanisms of nuclear positioning
    • Reinsch S, Gönczy P (1998) Mechanisms of nuclear positioning. J Cell Sci 111:2283-2295
    • (1998) J Cell Sci , vol.111 , pp. 2283-2295
    • Reinsch, S.1    Gönczy, P.2
  • 10
    • 0034657914 scopus 로고    scopus 로고
    • Microtubule interactions with the cell cortex causing nuclear movements in Saccharomyces cerevisiae
    • Adames NR, Cooper JA (2000) Microtubule interactions with the cell cortex causing nuclear movements in Saccharomyces cerevisiae. J Cell Biol 149:863-874
    • (2000) J Cell Biol , vol.149 , pp. 863-874
    • Adames, N.R.1    Cooper, J.A.2
  • 11
    • 84873510729 scopus 로고    scopus 로고
    • Spindle pole body-anchored Kar3 drives the nucleus along microtubules from another nucleus in preparation for nuclear fusion during yeast karyogamy
    • doi: 10.1101/gad.206318.112
    • Gibeaux R, Politi AZ, Nédélec F, Antony C, Knop M (2013) Spindle pole body-anchored Kar3 drives the nucleus along microtubules from another nucleus in preparation for nuclear fusion during yeast karyogamy. Genes Dev 27:335-349. doi: 10.1101/gad.206318.112
    • (2013) Genes Dev , vol.27 , pp. 335-349
    • Gibeaux, R.1    Politi, A.Z.2    Nédélec, F.3    Antony, C.4    Knop, M.5
  • 12
    • 30044442419 scopus 로고    scopus 로고
    • The KASH domain protein MSP-300 plays an essential role in nuclear anchoring during Drosophila oogenesis
    • Yu J, Starr DA, Wu X, Parkhurst SM, Zhuang Y, Xu T, Xu R, Han M (2006) The KASH domain protein MSP-300 plays an essential role in nuclear anchoring during Drosophila oogenesis. Dev Biol 289:336-345
    • (2006) Dev Biol , vol.289 , pp. 336-345
    • Yu, J.1    Starr, D.A.2    Wu, X.3    Parkhurst, S.M.4    Zhuang, Y.5    Xu, T.6    Xu, R.7    Han, M.8
  • 13
    • 0346094458 scopus 로고    scopus 로고
    • The C. Elegans hook protein, ZYG-12, mediates the essential attachment between the centrosome and nucleus
    • doi: 10.1016/S0092-8674(03)00985-1
    • Malone CJ, Misner L, Le Bot N, Tsai M-C, Campbell JM, Ahringer J, White JG (2003) The C. Elegans hook protein, ZYG-12, mediates the essential attachment between the centrosome and nucleus. Cell 115:825-836. doi: 10.1016/S0092- 8674(03)00985-1
    • (2003) Cell , vol.115 , pp. 825-836
    • Malone, C.J.1    Misner, L.2    Le Bot, N.3    Tsai, M.-C.4    Campbell, J.M.5    Ahringer, J.6    White, J.G.7
  • 14
    • 0031105358 scopus 로고    scopus 로고
    • Movement of nuclei along microtubules in Xenopus egg extracts
    • Reinsch S, Karsenti E (1997) Movement of nuclei along microtubules in Xenopus egg extracts. Curr Biol 7:211-214
    • (1997) Curr Biol , vol.7 , pp. 211-214
    • Reinsch, S.1    Karsenti, E.2
  • 15
    • 84864865667 scopus 로고    scopus 로고
    • Nuclear movement during myotube formation is microtubule and dynein dependent and is regulated by Cdc42, Par6 and Par3
    • doi: 10.1038/embor.2012.89
    • Cadot B, Gache V, Vasyutina E, Falcone S, Birchmeier C, Gomes ER (2012) Nuclear movement during myotube formation is microtubule and dynein dependent and is regulated by Cdc42, Par6 and Par3. EMBO Rep 13:741-749. doi: 10.1038/embor.2012.89
    • (2012) EMBO Rep , vol.13 , pp. 741-749
    • Cadot, B.1    Gache, V.2    Vasyutina, E.3    Falcone, S.4    Birchmeier, C.5    Gomes, E.R.6
  • 16
    • 84867376512 scopus 로고    scopus 로고
    • Coordination of satellite cell activation and self-renewal by Par-complex-dependent asymmetric activation of p38α/β MAPK
    • doi: 10.1016/j.stem.2012.05.025
    • Troy A, Cadwallader AB, Fedorov Y, Tyner K, Tanaka KK, Olwin BB (2012) Coordination of satellite cell activation and self-renewal by Par-complex-dependent asymmetric activation of p38α/β MAPK. Cell Stem Cell 11:541-553. doi: 10.1016/j.stem.2012.05.025
    • (2012) Cell Stem Cell , vol.11 , pp. 541-553
    • Troy, A.1    Cadwallader, A.B.2    Fedorov, Y.3    Tyner, K.4    Tanaka, K.K.5    Olwin, B.B.6
  • 18
    • 77955901384 scopus 로고    scopus 로고
    • Linear arrays of nuclear envelope proteins harness retrograde actin fl ow for nuclear movement
    • doi: 10.1126/science.1189072
    • Luxton GWG, Gomes ER, Folker ES, Vintinner E, Gundersen GG (2010) Linear arrays of nuclear envelope proteins harness retrograde actin fl ow for nuclear movement. Science 329:956-959. doi: 10.1126/science.1189072
    • (2010) Science , vol.329 , pp. 956-959
    • Luxton, G.W.G.1    Gomes, E.R.2    Folker, E.S.3    Vintinner, E.4    Gundersen, G.G.5
  • 19
    • 79960234802 scopus 로고    scopus 로고
    • TAN lines: A novel nuclear envelope structure involved in nuclear positioning
    • doi: 10.4161/nucl.2.3.16243
    • Luxton GWG, Gomes ER, Folker ES, Worman H, Gundersen GG (2011) TAN lines: a novel nuclear envelope structure involved in nuclear positioning. Nucleus 2:173-181. doi: 10.4161/nucl.2.3.16243
    • (2011) Nucleus , vol.2 , pp. 173-181
    • Luxton, G.W.G.1    Gomes, E.R.2    Folker, E.S.3    Worman, H.4    Gundersen, G.G.5
  • 21
    • 0020316410 scopus 로고
    • Polarization of the Golgi apparatus and the microtubuleorganizing center in cultured fi broblasts at the edge of an experimental wound
    • Kupfer A, Louvard D, Singer SJ (1982) Polarization of the Golgi apparatus and the microtubuleorganizing center in cultured fi broblasts at the edge of an experimental wound. Proc Natl Acad Sci USA 79:2603-2607
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 2603-2607
    • Kupfer, A.1    Louvard, D.2    Singer, S.J.3
  • 22
    • 0023794840 scopus 로고
    • Selective stabilization of microtubules oriented toward the direction of cell migration
    • Gundersen GG, Bulinski JC (1988) Selective stabilization of microtubules oriented toward the direction of cell migration. Proc Natl Acad Sci USA 85:5946-5950
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 5946-5950
    • Gundersen, G.G.1    Bulinski, J.C.2
  • 23
    • 0033594123 scopus 로고    scopus 로고
    • Rho GTPases control polarity, protrusion, and adhesion during cell movement
    • doi: 10.1083/jcb.144.6.1235
    • Nobes CD, Hall A (1999) Rho GTPases control polarity, protrusion, and adhesion during cell movement. J Cell Biol 144:1235-1244. doi: 10.1083/jcb.144.6.1235
    • (1999) J Cell Biol , vol.144 , pp. 1235-1244
    • Nobes, C.D.1    Hall, A.2
  • 24
    • 0020725023 scopus 로고
    • Membrane insertion at the leading edge of motile fi broblasts
    • Bergmann JE, Kupfer A, Singer SJ (1983) Membrane insertion at the leading edge of motile fi broblasts. Proc Natl Acad Sci USA 80:1367-1371
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 1367-1371
    • Bergmann, J.E.1    Kupfer, A.2    Singer, S.J.3
  • 25
    • 0344034726 scopus 로고    scopus 로고
    • Migrating fi broblasts perform polarized, microtubule-dependent exocytosis towards the leading edge
    • Schmoranzer J, Kreitzer G, Simon SM (2003) Migrating fi broblasts perform polarized, microtubule-dependent exocytosis towards the leading edge. J Cell Sci 116:4513-4519
    • (2003) J Cell Sci , vol.116 , pp. 4513-4519
    • Schmoranzer, J.1    Kreitzer, G.2    Simon, S.M.3
  • 26
    • 0032489802 scopus 로고    scopus 로고
    • Rho guanosine triphosphatase mediates the selective stabilization of microtubules induced by lysophosphatidic acid
    • doi: 10.1083/jcb.141.1.175
    • Cook TA, Nagasaki T, Gundersen GG (1998) Rho guanosine triphosphatase mediates the selective stabilization of microtubules induced by lysophosphatidic acid. J Cell Biol 141: 175-185. doi: 10.1083/jcb.141.1.175
    • (1998) J Cell Biol , vol.141 , pp. 175-185
    • Cook, T.A.1    Nagasaki, T.2    Gundersen, G.G.3
  • 27
    • 17844379382 scopus 로고    scopus 로고
    • Nuclear movement regulated by Cdc42, MRCK, myosin, and actin fl ow establishes MTOC polarization in migrating cells
    • Gomes ER, Jani S, Gundersen GG (2005) Nuclear movement regulated by Cdc42, MRCK, myosin, and actin fl ow establishes MTOC polarization in migrating cells. Cell 121:451-463
    • (2005) Cell , vol.121 , pp. 451-463
    • Gomes, E.R.1    Jani, S.2    Gundersen, G.G.3
  • 28
    • 0035943401 scopus 로고    scopus 로고
    • Integrin-mediated activation of Cdc42 controls cell polarity in migrating astrocytes through PKCzeta
    • Etienne-Manneville S, Hall A (2001) Integrin-mediated activation of Cdc42 controls cell polarity in migrating astrocytes through PKCzeta. Cell 106:489-498
    • (2001) Cell , vol.106 , pp. 489-498
    • Etienne-Manneville, S.1    Hall, A.2
  • 31
    • 67649859266 scopus 로고    scopus 로고
    • Par3 and dynein associate to regulate local microtubule dynamics and centrosome orientation during migration
    • doi: 10.1016/j.cub.2009.05.065
    • Schmoranzer J, Fawcett JP, Segura M, Tan S, Vallee RB, Pawson T, Gundersen GG (2009) Par3 and dynein associate to regulate local microtubule dynamics and centrosome orientation during migration. Curr Biol 19:1065-1074. doi: 10.1016/j.cub.2009.05.065
    • (2009) Curr Biol , vol.19 , pp. 1065-1074
    • Schmoranzer, J.1    Fawcett, J.P.2    Segura, M.3    Tan, S.4    Vallee, R.B.5    Pawson, T.6    Gundersen, G.G.7
  • 32
    • 79951553475 scopus 로고    scopus 로고
    • Nuclear mechanics during cell migration
    • doi: 10.1016/j.ceb.2010.10.015
    • Friedl P, Wolf K, Lammerding J (2011) Nuclear mechanics during cell migration. Curr Opin Cell Biol 23:55-64. doi: 10.1016/j.ceb.2010.10.015
    • (2011) Curr Opin Cell Biol , vol.23 , pp. 55-64
    • Friedl, P.1    Wolf, K.2    Lammerding, J.3
  • 33
    • 78651103909 scopus 로고    scopus 로고
    • Lamin A variants that cause striated muscle disease are defective in anchoring transmembrane actin-associated nuclear lines for nuclear movement
    • doi: 10.1073/pnas.1000824108
    • Folker ES, Östlund C, Luxton GWG, Worman HJ, Gundersen GG (2011) Lamin A variants that cause striated muscle disease are defective in anchoring transmembrane actin-associated nuclear lines for nuclear movement. Proc Natl Acad Sci USA 108:131-136. doi: 10.1073/pnas.1000824108
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 131-136
    • Folker, E.S.1    Östlund, C.2    Luxton, G.W.G.3    Worman, H.J.4    Gundersen, G.G.5
  • 36
    • 42649137624 scopus 로고    scopus 로고
    • Structural requirements for the assembly of LINC complexes and their function in cellular mechanical stiffness
    • doi: 10.1016/j.yexcr.2008.02.022
    • Stewart-Hutchinson PJ, Hale CM, Wirtz D, Hodzic D (2008) Structural requirements for the assembly of LINC complexes and their function in cellular mechanical stiffness. Exp Cell Res 314:1892-1905. doi: 10.1016/j.yexcr.2008.02. 022
    • (2008) Exp Cell Res , vol.314 , pp. 1892-1905
    • Stewart-Hutchinson, P.J.1    Hale, C.M.2    Wirtz, D.3    Hodzic, D.4
  • 38
    • 0042691509 scopus 로고    scopus 로고
    • Nuclear membrane proteins with potential disease links found by subtractive proteomics
    • Schirmer EC, Florens L, Guan T, Yates JR, Gerace L (2003) Nuclear membrane proteins with potential disease links found by subtractive proteomics. Science 301:1380-1382
    • (2003) Science , vol.301 , pp. 1380-1382
    • Schirmer, E.C.1    Florens, L.2    Guan, T.3    Yates, J.R.4    Gerace, L.5
  • 39
    • 68949170696 scopus 로고    scopus 로고
    • An integral protein of the inner nuclear membrane localizes to the mitotic spindle in mammalian cells
    • doi: 10.1242/jcs.047373
    • Buch C, Lindberg R, Figueroa R, Gudise S, Onischenko E, Hallberg E (2009) An integral protein of the inner nuclear membrane localizes to the mitotic spindle in mammalian cells. J Cell Sci 122:2100-2107. doi: 10.1242/jcs.047373
    • (2009) J Cell Sci , vol.122 , pp. 2100-2107
    • Buch, C.1    Lindberg, R.2    Figueroa, R.3    Gudise, S.4    Onischenko, E.5    Hallberg, E.6
  • 40
    • 77957681891 scopus 로고    scopus 로고
    • A transmembrane inner nuclear membrane protein in the mitotic spindle
    • doi: 10.4161/nucl.1.3.11740
    • Figueroa R, Gudise S, Larsson V, Hallberg E (2010) A transmembrane inner nuclear membrane protein in the mitotic spindle. Nucleus 1:249-253. doi: 10.4161/nucl.1.3.11740
    • (2010) Nucleus , vol.1 , pp. 249-253
    • Figueroa, R.1    Gudise, S.2    Larsson, V.3    Hallberg, E.4
  • 42
    • 79958115156 scopus 로고    scopus 로고
    • Samp1 is functionally associated with the LINC complex and A-type lamina networks
    • Gudise S, Figueroa RA, Lindberg R, Larsson V, Hallberg E (2011) Samp1 is functionally associated with the LINC complex and A-type lamina networks. J Cell Sci 124:2077-2085
    • (2011) J Cell Sci , vol.124 , pp. 2077-2085
    • Gudise, S.1    Figueroa, R.A.2    Lindberg, R.3    Larsson, V.4    Hallberg, E.5
  • 43
    • 77953890070 scopus 로고    scopus 로고
    • A membranous spindle matrix orchestrates cell division
    • doi: 10.1038/nrm2919
    • Zheng Y (2010) A membranous spindle matrix orchestrates cell division. Nat Rev Mol Cell Biol 11:529-535. doi: 10.1038/nrm2919
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 529-535
    • Zheng, Y.1
  • 44
    • 84860270506 scopus 로고    scopus 로고
    • A promiscuous biotin ligase fusion protein identifi es proximal and interacting proteins in mammalian cells
    • doi: 10.1083/jcb.201112098
    • Roux KJ, Kim DI, Raida M, Burke B (2012) A promiscuous biotin ligase fusion protein identifi es proximal and interacting proteins in mammalian cells. J Cell Biol 196:801-810. doi: 10.1083/jcb.201112098
    • (2012) J Cell Biol , vol.196 , pp. 801-810
    • Roux, K.J.1    Kim, D.I.2    Raida, M.3    Burke, B.4
  • 45
    • 48449102095 scopus 로고    scopus 로고
    • A network of nuclear envelope membrane proteins linking centromeres to microtubules
    • doi: 10.1016/j.cell.2008.06.022
    • King MC, Drivas TG, Blobel G (2008) A network of nuclear envelope membrane proteins linking centromeres to microtubules. Cell 134:427-438. doi: 10.1016/j.cell.2008.06.022
    • (2008) Cell , vol.134 , pp. 427-438
    • King, M.C.1    Drivas, T.G.2    Blobel, G.3
  • 46
    • 80053130289 scopus 로고    scopus 로고
    • Inner nuclear membrane protein Ima1 is dispensable for intranuclear positioning of centromeres
    • doi: 10.1111/j.1365-2443.2011.01544.x
    • Hiraoka Y, Maekawa H, Asakawa H, Chikashige Y, Kojidani T, Osakada H, Matsuda A, Haraguchi T (2011) Inner nuclear membrane protein Ima1 is dispensable for intranuclear positioning of centromeres. Genes Cells 16:1000-1011. doi: 10.1111/j.1365-2443.2011.01544.x
    • (2011) Genes Cells , vol.16 , pp. 1000-1011
    • Hiraoka, Y.1    Maekawa, H.2    Asakawa, H.3    Chikashige, Y.4    Kojidani, T.5    Osakada, H.6    Matsuda, A.7    Haraguchi, T.8
  • 50
    • 33744827404 scopus 로고    scopus 로고
    • The cellular roles of the lissencephaly gene LIS1, and what they tell us about brain development
    • doi: 10.1101/gad.1417206
    • Vallee RB, Tsai J-W (2006) The cellular roles of the lissencephaly gene LIS1, and what they tell us about brain development. Genes Dev 20:1384-1393. doi: 10.1101/gad.1417206
    • (2006) Genes Dev , vol.20 , pp. 1384-1393
    • Vallee, R.B.1    Tsai, J.-W.2
  • 51
    • 69449090498 scopus 로고    scopus 로고
    • Mutation of SYNE-1, encoding an essential component of the nuclear lamina, is responsible for autosomal recessive arthrogryposis
    • doi: 10.1093/hmg/ddp290
    • Attali R, Warwar N, Israel A, Gurt I, McNally E, Puckelwartz M, Glick B, Nevo Y, Ben-Neriah Z, Melki J (2009) Mutation of SYNE-1, encoding an essential component of the nuclear lamina, is responsible for autosomal recessive arthrogryposis. Hum Mol Genet 18:3462-3469. doi: 10.1093/hmg/ddp290
    • (2009) Hum Mol Genet , vol.18 , pp. 3462-3469
    • Attali, R.1    Warwar, N.2    Israel, A.3    Gurt, I.4    McNally, E.5    Puckelwartz, M.6    Glick, B.7    Nevo, Y.8    Ben-Neriah, Z.9    Melki, J.10
  • 55
    • 66349137319 scopus 로고    scopus 로고
    • LULL1 Retargets TorsinA to the nuclear envelope revealing an activity that is impaired by the DYT1 dystonia mutation
    • doi: 10.1091/mbc.E09-01-0094
    • Vander Heyden AB, Naismith TV, Snapp EL, Hodzic D, Hanson PI (2009) LULL1 Retargets TorsinA to the nuclear envelope revealing an activity that is impaired by the DYT1 dystonia mutation. Mol Biol Cell 20(11):2661-2672. doi: 10.1091/mbc.E09-01-0094
    • (2009) Mol Biol Cell , vol.20 , Issue.11 , pp. 2661-2672
    • Vander Heyden, A.B.1    Naismith, T.V.2    Snapp, E.L.3    Hodzic, D.4    Hanson, P.I.5
  • 56
  • 57
    • 84859465143 scopus 로고    scopus 로고
    • MAP and kinesin-dependent nuclear positioning is required for skeletal muscle function
    • doi: 10.1038/nature10914
    • Metzger T, Gache V, Xu M, Cadot B, Folker ES, Richardson BE, Gomes ER, Baylies MK (2012) MAP and kinesin-dependent nuclear positioning is required for skeletal muscle function. Nature 484:120-124. doi: 10.1038/nature10914
    • (2012) Nature , vol.484 , pp. 120-124
    • Metzger, T.1    Gache, V.2    Xu, M.3    Cadot, B.4    Folker, E.S.5    Richardson, B.E.6    Gomes, E.R.7    Baylies, M.K.8


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