메뉴 건너뛰기




Volumn 126, Issue , 2014, Pages 205-215

Nuclear forces and cell mechanosensing

Author keywords

Cytoskeleton; KASH domain proteins; Lamin A C; LINC complex; Mechanotransduction; Nesprin proteins; Nuclear envelope; Nucleus; SUN domain proteins

Indexed keywords

MEMBRANE RECEPTOR; MULTIPROTEIN COMPLEX;

EID: 84905157800     PISSN: 18771173     EISSN: 18780814     Source Type: Book Series    
DOI: 10.1016/B978-0-12-394624-9.00008-7     Document Type: Chapter
Times cited : (58)

References (80)
  • 2
    • 0025186789 scopus 로고
    • Mechanosensitive ion channels
    • C.E. Morris Mechanosensitive ion channels J Membr Biol 113 2 1990 93 107 (Pubitemid 20053115)
    • (1990) Journal of Membrane Biology , vol.113 , Issue.2 , pp. 93-107
    • Morris, C.E.1
  • 3
    • 33644901594 scopus 로고    scopus 로고
    • Mechanical forces alter zyxin unbinding kinetics within focal adhesions of living cells
    • T.P. Lele, J. Pendse, S. Kumar, M. Salanga, J. Karavitis, and D.E. Ingber Mechanical forces alter zyxin unbinding kinetics within focal adhesions of living cells J Cell Physiol 207 1 2006 187 194
    • (2006) J Cell Physiol , vol.207 , Issue.1 , pp. 187-194
    • Lele, T.P.1    Pendse, J.2    Kumar, S.3    Salanga, M.4    Karavitis, J.5    Ingber, D.E.6
  • 5
    • 33744488545 scopus 로고    scopus 로고
    • Cellular mechanotransduction: Putting all the pieces together again
    • DOI 10.1096/fj.05-5424rev
    • D. Ingber Cellular mechanotransduction: putting all the pieces together again FASEB J 20 7 2006 811 827 (Pubitemid 44943939)
    • (2006) FASEB Journal , vol.20 , Issue.7 , pp. 811-827
    • Ingber, D.E.1
  • 6
    • 58049211966 scopus 로고    scopus 로고
    • Mechanotransduction at a distance: Mechanically coupling the extracellular matrix with the nucleus
    • N. Wang, J.D. Tytell, and D.E. Ingber Mechanotransduction at a distance: mechanically coupling the extracellular matrix with the nucleus Nat Rev Mol Cell Biol 10 1 2009 75 82
    • (2009) Nat Rev Mol Cell Biol , vol.10 , Issue.1 , pp. 75-82
    • Wang, N.1    Tytell, J.D.2    Ingber, D.E.3
  • 7
    • 0027090097 scopus 로고
    • Altering the cellular mechanical force balance results in integrated changes in cell, cytoskeletal and nuclear shape
    • J.R. Sims, S. Karp, and D.E. Ingber Altering the cellular mechanical force balance results in integrated changes in cell, cytoskeletal and nuclear shape J Cell Sci 103 Pt. 4 1992 1215 1222 (Pubitemid 23042264)
    • (1992) Journal of Cell Science , vol.103 , Issue.4 , pp. 1215-1222
    • Sims, J.R.1    Karp, S.2    Ingber, D.E.3
  • 9
    • 0030899760 scopus 로고    scopus 로고
    • Tensegrity: The architectural basis of cellular mechanotransduction
    • DOI 10.1146/annurev.physiol.59.1.575
    • D.E. Ingber Tensegrity: the architectural basis of cellular mechanotransduction Annu Rev Physiol 59 1997 575 599 (Pubitemid 27142456)
    • (1997) Annual Review of Physiology , vol.59 , pp. 575-599
    • Ingber, D.E.1
  • 10
    • 0033036061 scopus 로고    scopus 로고
    • Tensegrity and mechanoregulation: From skeleton to cytoskeleton
    • DOI 10.1053/joca.1998.0164
    • C.S. Chen, and D.E. Ingber Tensegrity and mechanoregulation: from skeleton to cytoskeleton Osteoarthr Cartil 7 1 1999 81 94 (Pubitemid 29112962)
    • (1999) Osteoarthritis and Cartilage , vol.7 , Issue.1 , pp. 81-94
    • Chen, C.S.1    Ingber, D.E.2
  • 11
    • 0037383404 scopus 로고    scopus 로고
    • Tensegrity I. Cell structure and hierarchical systems biology
    • DOI 10.1242/jcs.00359
    • D.E. Ingber, and I. Tensegrity Cell structure and hierarchical systems biology J Cell Sci 116 Pt 7 2003 1157 1173 (Pubitemid 36410656)
    • (2003) Journal of Cell Science , vol.116 , Issue.7 , pp. 1157-1173
    • Ingber, D.E.1
  • 14
    • 0036084083 scopus 로고    scopus 로고
    • Cell prestress. I. Stiffness and prestress are closely associated in adherent contractile cells
    • N. Wang, I.M. Tolic-Norrelykke, and J. Chen et al. Cell prestress. I. Stiffness and prestress are closely associated in adherent contractile cells Am J Physiol Cell Physiol 282 3 2002 C606 C616
    • (2002) Am J Physiol Cell Physiol , vol.282 , Issue.3
    • Wang, N.1    Tolic-Norrelykke, I.M.2    Chen, J.3
  • 16
    • 0029584101 scopus 로고
    • Compression-induced changes in the shape and volume of the chondrocyte nucleus
    • DOI 10.1016/0021-9290(95)00100-X
    • F. Guilak Compression-induced changes in the shape and volume of the chondrocyte nucleus J Biomech 28 12 1995 1529 1541 (Pubitemid 26004298)
    • (1995) Journal of Biomechanics , vol.28 , Issue.12 , pp. 1529-1541
    • Guilak, F.1
  • 17
    • 79960685238 scopus 로고    scopus 로고
    • The interaction between nesprins and sun proteins at the nuclear envelope is critical for force transmission between the nucleus and cytoskeleton
    • M.L. Lombardi, D.E. Jaalouk, C.M. Shanahan, B. Burke, K.J. Roux, and J. Lammerding The interaction between nesprins and sun proteins at the nuclear envelope is critical for force transmission between the nucleus and cytoskeleton J Biol Chem 286 30 2011 26743 26753
    • (2011) J Biol Chem , vol.286 , Issue.30 , pp. 26743-26753
    • Lombardi, M.L.1    Jaalouk, D.E.2    Shanahan, C.M.3    Burke, B.4    Roux, K.J.5    Lammerding, J.6
  • 18
    • 84934435247 scopus 로고    scopus 로고
    • Mechanical properties of interphase nuclei probed by cellular strain application
    • J. Lammerding, and R.T. Lee Mechanical properties of interphase nuclei probed by cellular strain application Methods Mol Biol 464 2009 13 26
    • (2009) Methods Mol Biol , vol.464 , pp. 13-26
    • Lammerding, J.1    Lee, R.T.2
  • 22
    • 84866424053 scopus 로고    scopus 로고
    • Dynamic force-induced direct dissociation of protein complexes in a nuclear body in living cells
    • Y.C. Poh, S.P. Shevtsov, and F. Chowdhury et al. Dynamic force-induced direct dissociation of protein complexes in a nuclear body in living cells Nat Commun 3 2012 866
    • (2012) Nat Commun , vol.3 , pp. 866
    • Poh, Y.C.1    Shevtsov, S.P.2    Chowdhury, F.3
  • 23
    • 71549123700 scopus 로고    scopus 로고
    • Nuclei take a position: Managing nuclear location
    • B. Burke, and K.J. Roux Nuclei take a position: managing nuclear location Dev Cell 17 5 2009 587 597
    • (2009) Dev Cell , vol.17 , Issue.5 , pp. 587-597
    • Burke, B.1    Roux, K.J.2
  • 25
    • 78049394356 scopus 로고    scopus 로고
    • Interactions between nuclei and the cytoskeleton are mediated by SUN-KASH nuclear-envelope bridges
    • D.A. Starr, and H.N. Fridolfsson Interactions between nuclei and the cytoskeleton are mediated by SUN-KASH nuclear-envelope bridges Annu Rev Cell Dev Biol 26 2010 421 444
    • (2010) Annu Rev Cell Dev Biol , vol.26 , pp. 421-444
    • Starr, D.A.1    Fridolfsson, H.N.2
  • 26
    • 80054902318 scopus 로고    scopus 로고
    • The nucleoskeleton as a genome-associated dynamic 'network of networks'
    • D.N. Simon, and K.L. Wilson The nucleoskeleton as a genome-associated dynamic 'network of networks' Nat Rev Mol Cell Biol 12 11 2011 695 708
    • (2011) Nat Rev Mol Cell Biol , vol.12 , Issue.11 , pp. 695-708
    • Simon, D.N.1    Wilson, K.L.2
  • 27
    • 84867055836 scopus 로고    scopus 로고
    • Structural insights into SUN-KASH complexes across the nuclear envelope
    • W. Wang, Z. Shi, and S. Jiao et al. Structural insights into SUN-KASH complexes across the nuclear envelope Cell Res 22 10 2012 1440 1452
    • (2012) Cell Res , vol.22 , Issue.10 , pp. 1440-1452
    • Wang, W.1    Shi, Z.2    Jiao, S.3
  • 28
    • 84861543038 scopus 로고    scopus 로고
    • LINC complexes form by binding of three KASH peptides to domain interfaces of trimeric SUN proteins
    • B.A. Sosa, A. Rothballer, U. Kutay, and T.U. Schwartz LINC complexes form by binding of three KASH peptides to domain interfaces of trimeric SUN proteins Cell 149 5 2012 1035 1047
    • (2012) Cell , vol.149 , Issue.5 , pp. 1035-1047
    • Sosa, B.A.1    Rothballer, A.2    Kutay, U.3    Schwartz, T.U.4
  • 29
    • 79952031707 scopus 로고    scopus 로고
    • KASH protein Syne-2/Nesprin-2 and SUN proteins SUN1/2 mediate nuclear migration during mammalian retinal development
    • J. Yu, K. Lei, and M. Zhou et al. KASH protein Syne-2/Nesprin-2 and SUN proteins SUN1/2 mediate nuclear migration during mammalian retinal development Hum Mol Genet 20 6 2011 1061 1073
    • (2011) Hum Mol Genet , vol.20 , Issue.6 , pp. 1061-1073
    • Yu, J.1    Lei, K.2    Zhou, M.3
  • 30
    • 70350211470 scopus 로고    scopus 로고
    • SUN1/2 and Syne/Nesprin-1/2 complexes connect centrosome to the nucleus during neurogenesis and neuronal migration in mice
    • X. Zhang, K. Lei, and X. Yuan et al. SUN1/2 and Syne/Nesprin-1/2 complexes connect centrosome to the nucleus during neurogenesis and neuronal migration in mice Neuron 64 2 2009 173 187
    • (2009) Neuron , vol.64 , Issue.2 , pp. 173-187
    • Zhang, X.1    Lei, K.2    Yuan, X.3
  • 31
    • 84873329892 scopus 로고    scopus 로고
    • The LINC complex is essential for hearing
    • H.F. Horn, Z. Brownstein, and D.R. Lenz et al. The LINC complex is essential for hearing J Clin Invest 123 2 2013 740 750
    • (2013) J Clin Invest , vol.123 , Issue.2 , pp. 740-750
    • Horn, H.F.1    Brownstein, Z.2    Lenz, D.R.3
  • 32
    • 60549099949 scopus 로고    scopus 로고
    • Nesprin 4 is an outer nuclear membrane protein that can induce kinesin-mediated cell polarization
    • K.J. Roux, M.L. Crisp, and Q. Liu et al. Nesprin 4 is an outer nuclear membrane protein that can induce kinesin-mediated cell polarization Proc Natl Acad Sci USA 106 7 2009 2194 2199
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.7 , pp. 2194-2199
    • Roux, K.J.1    Crisp, M.L.2    Liu, Q.3
  • 33
    • 84886934835 scopus 로고    scopus 로고
    • A mammalian KASH domain protein coupling meiotic chromosomes to the cytoskeleton
    • H.F. Horn, D.I. Kim, and G.D. Wright et al. A mammalian KASH domain protein coupling meiotic chromosomes to the cytoskeleton J Cell Biol 202 7 2013 1023 1039
    • (2013) J Cell Biol , vol.202 , Issue.7 , pp. 1023-1039
    • Horn, H.F.1    Kim, D.I.2    Wright, G.D.3
  • 34
    • 84865018091 scopus 로고    scopus 로고
    • A conserved KASH domain protein associates with telomeres, SUN1, and dynactin during mammalian meiosis
    • A. Morimoto, H. Shibuya, and X. Zhu et al. A conserved KASH domain protein associates with telomeres, SUN1, and dynactin during mammalian meiosis J Cell Biol 198 2 2012 165 172
    • (2012) J Cell Biol , vol.198 , Issue.2 , pp. 165-172
    • Morimoto, A.1    Shibuya, H.2    Zhu, X.3
  • 35
    • 77950354284 scopus 로고    scopus 로고
    • Lrmp/Jaw1 is expressed in sweet, bitter, and umami receptor-expressing cells
    • Y. Shindo, M.R. Kim, and H. Miura et al. Lrmp/Jaw1 is expressed in sweet, bitter, and umami receptor-expressing cells Chem Senses 35 2 2010 171 177
    • (2010) Chem Senses , vol.35 , Issue.2 , pp. 171-177
    • Shindo, Y.1    Kim, M.R.2    Miura, H.3
  • 36
    • 33747883668 scopus 로고    scopus 로고
    • Identification and characterization of GSRP-56, a novel Golgi-localized spectrin repeat-containing protein
    • DOI 10.1016/j.yexcr.2006.06.026, PII S0014482706002278
    • Y. Kobayashi, Y. Katanosaka, Y. Iwata, M. Matsuoka, M. Shigekawa, and S. Wakabayashi Identification and characterization of GSRP-56, a novel Golgi-localized spectrin repeat-containing protein Exp Cell Res 312 16 2006 3152 3164 (Pubitemid 44292665)
    • (2006) Experimental Cell Research , vol.312 , Issue.16 , pp. 3152-3164
    • Kobayashi, Y.1    Katanosaka, Y.2    Iwata, Y.3    Matsuoka, M.4    Shigekawa, M.5    Wakabayashi, S.6
  • 37
    • 84863613755 scopus 로고    scopus 로고
    • Multiple novel nesprin-1 and nesprin-2 variants act as versatile tissue-specific intracellular scaffolds
    • D. Rajgor, J.A. Mellad, F. Autore, Q. Zhang, and C.M. Shanahan Multiple novel nesprin-1 and nesprin-2 variants act as versatile tissue-specific intracellular scaffolds PLoS One 7 7 2012 e40098
    • (2012) PLoS One , vol.7 , Issue.7 , pp. 40098
    • Rajgor, D.1    Mellad, J.A.2    Autore, F.3    Zhang, Q.4    Shanahan, C.M.5
  • 38
    • 8844247986 scopus 로고    scopus 로고
    • CPG2: A brain- and synapse-specific protein that regulates the endocytosis of glutamate receptors
    • DOI 10.1016/j.neuron.2004.10.025, PII S0896627304006889
    • J.R. Cottrell, E. Borok, T.L. Horvath, and E. Nedivi CPG2: a brain- and synapse-specific protein that regulates the endocytosis of glutamate receptors Neuron 44 4 2004 677 690 (Pubitemid 39531231)
    • (2004) Neuron , vol.44 , Issue.4 , pp. 677-690
    • Cottrell, J.R.1    Borok, E.2    Horvath, T.L.3    Nedivi, E.4
  • 39
    • 51649107126 scopus 로고    scopus 로고
    • Loss of Drop1 expression already at early tumor stages in a wide range of human carcinomas
    • A. Marme, H.P. Zimmermann, and G. Moldenhauer et al. Loss of Drop1 expression already at early tumor stages in a wide range of human carcinomas Int J Cancer 123 9 2008 2048 2056
    • (2008) Int J Cancer , vol.123 , Issue.9 , pp. 2048-2056
    • Marme, A.1    Zimmermann, H.P.2    Moldenhauer, G.3
  • 40
    • 74049100497 scopus 로고    scopus 로고
    • Novel nuclear nesprin-2 variants tether active extracellular signal-regulated MAPK1 and MAPK2 at promyelocytic leukemia protein nuclear bodies and act to regulate smooth muscle cell proliferation
    • D.T. Warren, T. Tajsic, J.A. Mellad, R. Searles, Q. Zhang, and C.M. Shanahan Novel nuclear nesprin-2 variants tether active extracellular signal-regulated MAPK1 and MAPK2 at promyelocytic leukemia protein nuclear bodies and act to regulate smooth muscle cell proliferation J Biol Chem 285 2 2010 1311 1320
    • (2010) J Biol Chem , vol.285 , Issue.2 , pp. 1311-1320
    • Warren, D.T.1    Tajsic, T.2    Mellad, J.A.3    Searles, R.4    Zhang, Q.5    Shanahan, C.M.6
  • 41
    • 0024150623 scopus 로고
    • Focal adhesions: Transmembrane junctions between the extracellular matrix and the cytoskeleton
    • K. Burridge, K. Fath, T. Kelly, G. Nuckolls, and C. Turner Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton Annu Rev Cell Biol 4 1988 487 525 (Pubitemid 19139264)
    • (1988) Annual Review of Cell Biology , vol.4 , pp. 487-525
    • Burridge, K.1    Fath, K.2    Kelly, T.3    Nuckolls, G.4    Turner, C.5
  • 42
    • 0027172919 scopus 로고
    • Mechanotransduction across the cell surface and through the cytoskeleton
    • N. Wang, J.P. Butler, and D.E. Ingber Mechanotransduction across the cell surface and through the cytoskeleton Science 260 5111 1993 1124 1127 (Pubitemid 23186787)
    • (1993) Science , vol.260 , Issue.5111 , pp. 1124-1127
    • Wang, N.1    Butler, J.P.2    Ingber, D.E.3
  • 44
    • 0023080985 scopus 로고
    • Dynamic reciprocity: How do extracellular matrix and hormones direct gene expression?
    • M.J. Bissell, and J. Aggeler Dynamic reciprocity: how do extracellular matrix and hormones direct gene expression? Prog Clin Biol Res 249 1987 251 262
    • (1987) Prog Clin Biol Res , vol.249 , pp. 251-262
    • Bissell, M.J.1    Aggeler, J.2
  • 45
    • 0023613106 scopus 로고
    • The influence of extracellular matrix on gene expression: Is structure the message?
    • M.J. Bissell, and M.H. Barcellos-Hoff The influence of extracellular matrix on gene expression: is structure the message? J Cell Sci Suppl 8 1987 327 343 (Pubitemid 18041168)
    • (1987) Journal of Cell Science , Issue.SUPPL. 8 , pp. 327-343
    • Bissell, M.J.1    Barcellos-Hoff, M.H.2
  • 46
    • 0020456385 scopus 로고
    • How does the extracellular matrix direct gene expression?
    • DOI 10.1016/0022-5193(82)90388-5
    • M.J. Bissell, H.G. Hall, and G. Parry How does the extracellular matrix direct gene expression? J Theor Biol 99 1 1982 31 68 (Pubitemid 13209096)
    • (1982) Journal of Theoretical Biology , vol.99 , Issue.1 , pp. 31-68
    • Bissell, M.J.1    Hall, H.G.2    Parry, G.3
  • 47
    • 77955901384 scopus 로고    scopus 로고
    • Linear arrays of nuclear envelope proteins harness retrograde actin flow for nuclear movement
    • G.W. Luxton, E.R. Gomes, E.S. Folker, E. Vintinner, and G.G. Gundersen Linear arrays of nuclear envelope proteins harness retrograde actin flow for nuclear movement Science 329 5994 2010 956 959
    • (2010) Science , vol.329 , Issue.5994 , pp. 956-959
    • Luxton, G.W.1    Gomes, E.R.2    Folker, E.S.3    Vintinner, E.4    Gundersen, G.G.5
  • 48
    • 81855212456 scopus 로고    scopus 로고
    • Keeping the LINC: The importance of nucleocytoskeletal coupling in intracellular force transmission and cellular function
    • M.L. Lombardi, and J. Lammerding Keeping the LINC: the importance of nucleocytoskeletal coupling in intracellular force transmission and cellular function Biochem Soc Trans 39 6 2011 1729 1734
    • (2011) Biochem Soc Trans , vol.39 , Issue.6 , pp. 1729-1734
    • Lombardi, M.L.1    Lammerding, J.2
  • 49
    • 42649137624 scopus 로고    scopus 로고
    • Structural requirements for the assembly of LINC complexes and their function in cellular mechanical stiffness
    • P.J. Stewart-Hutchinson, C.M. Hale, D. Wirtz, and D. Hodzic Structural requirements for the assembly of LINC complexes and their function in cellular mechanical stiffness Exp Cell Res 314 8 2008 1892 1905
    • (2008) Exp Cell Res , vol.314 , Issue.8 , pp. 1892-1905
    • Stewart-Hutchinson, P.J.1    Hale, C.M.2    Wirtz, D.3    Hodzic, D.4
  • 50
    • 0028001366 scopus 로고
    • Marbles mutants: Uncoupling cell determination and nuclear migration in the developing Drosophila eye
    • J.A. Fischer-Vize, and K.L. Mosley Marbles mutants: uncoupling cell determination and nuclear migration in the developing Drosophila eye Development 120 9 1994 2609 2618 (Pubitemid 24268834)
    • (1994) Development , vol.120 , Issue.9 , pp. 2609-2618
    • Fischer-Vize, J.A.1    Mosley, K.L.2
  • 51
    • 0032772929 scopus 로고    scopus 로고
    • UNC-84 localizes to the nuclear envelope and is required for nuclear migration and anchoring during C. Elegans development
    • C.J. Malone, W.D. Fixsen, H.R. Horvitz, and M. Han UNC-84 localizes to the nuclear envelope and is required for nuclear migration and anchoring during C. elegans development Development 126 14 1999 3171 3181 (Pubitemid 29378180)
    • (1999) Development , vol.126 , Issue.14 , pp. 3171-3181
    • Malone, C.J.1    Fixsen, W.D.2    Horvitz, H.R.3    Han, M.4
  • 52
    • 0033523985 scopus 로고    scopus 로고
    • Molecular analysis of the klarsicht gene and its role in nuclear migration within differentiating cells of the Drosophila eye
    • K.L. Mosley-Bishop, Q. Li, L. Patterson, and J.A. Fischer Molecular analysis of the klarsicht gene and its role in nuclear migration within differentiating cells of the Drosophila eye Curr Biol 9 21 1999 1211 1220 (Pubitemid 29527146)
    • (1999) Current Biology , vol.9 , Issue.21 , pp. 1211-1220
    • Mosley-Bishop, K.L.1    Li, Q.2    Patterson, K.3    Fischer, J.A.4
  • 54
    • 77954333003 scopus 로고    scopus 로고
    • Actomyosin tension exerted on the nucleus through nesprin-1 connections influences endothelial cell adhesion, migration, and cyclic strain-induced reorientation
    • T.J. Chancellor, J. Lee, C.K. Thodeti, and T. Lele Actomyosin tension exerted on the nucleus through nesprin-1 connections influences endothelial cell adhesion, migration, and cyclic strain-induced reorientation Biophys J 99 1 2010 115 123
    • (2010) Biophys J , vol.99 , Issue.1 , pp. 115-123
    • Chancellor, T.J.1    Lee, J.2    Thodeti, C.K.3    Lele, T.4
  • 55
    • 24144481867 scopus 로고    scopus 로고
    • Abnormal nuclear shape and impaired mechanotransduction in emerin-deficient cells
    • DOI 10.1083/jcb.200502148
    • J. Lammerding, J. Hsiao, P.C. Schulze, S. Kozlov, C.L. Stewart, and R.T. Lee Abnormal nuclear shape and impaired mechanotransduction in emerin-deficient cells J Cell Biol 170 5 2005 781 791 (Pubitemid 41242110)
    • (2005) Journal of Cell Biology , vol.170 , Issue.5 , pp. 781-791
    • Lammerding, J.1    Hsiao, J.2    Schulze, P.C.3    Kozlov, S.4    Stewart, C.L.5    Lee, R.T.6
  • 56
    • 84875190548 scopus 로고    scopus 로고
    • Nuclear positioning
    • G.G. Gundersen, and H.J. Worman Nuclear positioning Cell 152 6 2013 1376 1389
    • (2013) Cell , vol.152 , Issue.6 , pp. 1376-1389
    • Gundersen, G.G.1    Worman, H.J.2
  • 57
    • 79960234802 scopus 로고    scopus 로고
    • TAN lines: A novel nuclear envelope structure involved in nuclear positioning
    • G.W. Luxton, E.R. Gomes, E.S. Folker, H.J. Worman, and G.G. Gundersen TAN lines: a novel nuclear envelope structure involved in nuclear positioning Nucleus 2 3 2011 173 181
    • (2011) Nucleus , vol.2 , Issue.3 , pp. 173-181
    • Luxton, G.W.1    Gomes, E.R.2    Folker, E.S.3    Worman, H.J.4    Gundersen, G.G.5
  • 58
    • 84890533531 scopus 로고    scopus 로고
    • Emerin organizes actin flow for nuclear movement and centrosome orientation in migrating fibroblasts
    • W. Chang, E.S. Folker, H.J. Worman, and G.G. Gundersen Emerin organizes actin flow for nuclear movement and centrosome orientation in migrating fibroblasts Mol Biol Cell 24 24 2013 3869 3880
    • (2013) Mol Biol Cell , vol.24 , Issue.24 , pp. 3869-3880
    • Chang, W.1    Folker, E.S.2    Worman, H.J.3    Gundersen, G.G.4
  • 60
    • 84864830665 scopus 로고    scopus 로고
    • Actin cap associated focal adhesions and their distinct role in cellular mechanosensing
    • D.H. Kim, S.B. Khatau, and Y. Feng et al. Actin cap associated focal adhesions and their distinct role in cellular mechanosensing Sci Rep 2 2012 555
    • (2012) Sci Rep , vol.2 , pp. 555
    • Kim, D.H.1    Khatau, S.B.2    Feng, Y.3
  • 61
    • 84878038512 scopus 로고    scopus 로고
    • The LINC-anchored actin cap connects the extracellular milieu to the nucleus for ultrafast mechanotransduction
    • A.B. Chambliss, S.B. Khatau, and N. Erdenberger et al. The LINC-anchored actin cap connects the extracellular milieu to the nucleus for ultrafast mechanotransduction Sci Rep 3 2013 1087
    • (2013) Sci Rep , vol.3 , pp. 1087
    • Chambliss, A.B.1    Khatau, S.B.2    Erdenberger, N.3
  • 62
    • 84878030653 scopus 로고    scopus 로고
    • The multi-faceted role of the actin cap in cellular mechanosensation and mechanotransduction
    • D.H. Kim, A.B. Chambliss, and D. Wirtz The multi-faceted role of the actin cap in cellular mechanosensation and mechanotransduction Soft Matter 9 23 2013 5516 5523
    • (2013) Soft Matter , vol.9 , Issue.23 , pp. 5516-5523
    • Kim, D.H.1    Chambliss, A.B.2    Wirtz, D.3
  • 63
    • 84860521306 scopus 로고    scopus 로고
    • The differential formation of the LINC-mediated perinuclear actin cap in pluripotent and somatic cells
    • S.B. Khatau, S. Kusuma, and D. Hanjaya-Putra et al. The differential formation of the LINC-mediated perinuclear actin cap in pluripotent and somatic cells PLoS One 7 5 2012 e36689
    • (2012) PLoS One , vol.7 , Issue.5 , pp. 36689
    • Khatau, S.B.1    Kusuma, S.2    Hanjaya-Putra, D.3
  • 64
    • 84863809273 scopus 로고    scopus 로고
    • The distinct roles of the nucleus and nucleus-cytoskeleton connections in three-dimensional cell migration
    • S.B. Khatau, R.J. Bloom, and S. Bajpai et al. The distinct roles of the nucleus and nucleus-cytoskeleton connections in three-dimensional cell migration Sci Rep 2 2012 488
    • (2012) Sci Rep , vol.2 , pp. 488
    • Khatau, S.B.1    Bloom, R.J.2    Bajpai, S.3
  • 66
    • 84866402748 scopus 로고    scopus 로고
    • Opposing microtubule motors drive robust nuclear dynamics in developing muscle cells
    • M.H. Wilson, and E.L. Holzbaur Opposing microtubule motors drive robust nuclear dynamics in developing muscle cells J Cell Sci 125 Pt 17 2012 4158 4169
    • (2012) J Cell Sci , vol.125 , Issue.PART 17 , pp. 4158-4169
    • Wilson, M.H.1    Holzbaur, E.L.2
  • 67
    • 74749103945 scopus 로고    scopus 로고
    • UNC-83 coordinates kinesin-1 and dynein activities at the nuclear envelope during nuclear migration
    • H.N. Fridolfsson, N. Ly, M. Meyerzon, and D.A. Starr UNC-83 coordinates kinesin-1 and dynein activities at the nuclear envelope during nuclear migration Dev Biol 338 2 2009 237 250
    • (2009) Dev Biol , vol.338 , Issue.2 , pp. 237-250
    • Fridolfsson, H.N.1    Ly, N.2    Meyerzon, M.3    Starr, D.A.4
  • 68
    • 77957735230 scopus 로고    scopus 로고
    • Kinesin-1 and dynein at the nuclear envelope mediate the bidirectional migrations of nuclei
    • H.N. Fridolfsson, and D.A. Starr Kinesin-1 and dynein at the nuclear envelope mediate the bidirectional migrations of nuclei J Cell Biol 191 1 2010 115 128
    • (2010) J Cell Biol , vol.191 , Issue.1 , pp. 115-128
    • Fridolfsson, H.N.1    Starr, D.A.2
  • 69
    • 79960679617 scopus 로고    scopus 로고
    • How dynein and microtubules rotate the nucleus
    • 10.1002/jcp.22616
    • J. Wu, K.C. Lee, R.B. Dickinson, and T.P. Lele How dynein and microtubules rotate the nucleus J Cell Physiol 226 10 2011 2666 2674 10.1002/jcp.22616
    • (2011) J Cell Physiol , vol.226 , Issue.10 , pp. 2666-2674
    • Wu, J.1    Lee, K.C.2    Dickinson, R.B.3    Lele, T.P.4
  • 70
    • 70450221490 scopus 로고    scopus 로고
    • Cytoskeletal forces span the nuclear envelope to coordinate meiotic chromosome pairing and synapsis
    • A. Sato, B. Isaac, and C.M. Phillips et al. Cytoskeletal forces span the nuclear envelope to coordinate meiotic chromosome pairing and synapsis Cell 139 5 2009 907 919
    • (2009) Cell , vol.139 , Issue.5 , pp. 907-919
    • Sato, A.1    Isaac, B.2    Phillips, C.M.3
  • 71
    • 1042265578 scopus 로고    scopus 로고
    • Two-hybrid search for proteins that interact with Sad1 and Kms1, two membrane-bound components of the spindle pole body in fission yeast
    • DOI 10.1007/s00438-003-0938-8
    • F. Miki, A. Kurabayashi, Y. Tange, K. Okazaki, M. Shimanuki, and O. Niwa Two-hybrid search for proteins that interact with Sad1 and Kms1, two membrane-bound components of the spindle pole body in fission yeast Mol Genet Genomics 270 6 2004 449 461 (Pubitemid 38200036)
    • (2004) Molecular Genetics and Genomics , vol.270 , Issue.6 , pp. 449-461
    • Miki, F.1    Kurabayashi, A.2    Tange, Y.3    Okazaki, K.4    Shimanuki, M.5    Niwa, O.6
  • 72
    • 84874408317 scopus 로고    scopus 로고
    • Microtubule-organizing center formation at telomeres induces meiotic telomere clustering
    • M. Yoshida, S. Katsuyama, and K. Tateho et al. Microtubule-organizing center formation at telomeres induces meiotic telomere clustering J Cell Biol 200 4 2013 385 395
    • (2013) J Cell Biol , vol.200 , Issue.4 , pp. 385-395
    • Yoshida, M.1    Katsuyama, S.2    Tateho, K.3
  • 73
    • 60549108384 scopus 로고    scopus 로고
    • Vascular endothelial responses to altered shear stress: Pathologic implications for atherosclerosis
    • J.J. Chiu, S. Usami, and S. Chien Vascular endothelial responses to altered shear stress: pathologic implications for atherosclerosis Ann Med 41 1 2009 19 28
    • (2009) Ann Med , vol.41 , Issue.1 , pp. 19-28
    • Chiu, J.J.1    Usami, S.2    Chien, S.3
  • 74
    • 0042360380 scopus 로고    scopus 로고
    • Mechanical strain-stimulated remodeling of tissue-engineered blood vessel constructs
    • DOI 10.1089/107632703768247359
    • D. Seliktar, R.M. Nerem, and Z.S. Galis Mechanical strain-stimulated remodeling of tissue-engineered blood vessel constructs Tissue Eng 9 4 2003 657 666 (Pubitemid 37048108)
    • (2003) Tissue Engineering , vol.9 , Issue.4 , pp. 657-666
    • Seliktar, D.1    Nerem, R.M.2    Galis, Z.S.3
  • 75
    • 27944497333 scopus 로고    scopus 로고
    • Tissue cells feel and respond to the stiffness of their substrate
    • DOI 10.1126/science.1116995
    • D.E. Discher, P. Janmey, and Y.L. Wang Tissue cells feel and respond to the stiffness of their substrate Science 310 5751 2005 1139 1143 (Pubitemid 41681732)
    • (2005) Science , vol.310 , Issue.5751 , pp. 1139-1143
    • Discher, D.E.1    Janmey, P.2    Wang, Y.-L.3
  • 77
    • 55549113990 scopus 로고    scopus 로고
    • Nuclear mechanotransduction: Response of the lamina to extracellular stress with implications in aging
    • J.T. Philip, and K.N. Dahl Nuclear mechanotransduction: response of the lamina to extracellular stress with implications in aging J Biomech 41 15 2008 3164 3170
    • (2008) J Biomech , vol.41 , Issue.15 , pp. 3164-3170
    • Philip, J.T.1    Dahl, K.N.2
  • 78
    • 84878116428 scopus 로고    scopus 로고
    • Lamin A/C and emerin regulate MKL1-SRF activity by modulating actin dynamics
    • C.Y. Ho, D.E. Jaalouk, M.K. Vartiainen, and J. Lammerding Lamin A/C and emerin regulate MKL1-SRF activity by modulating actin dynamics Nature 497 7450 2013 507 511
    • (2013) Nature , vol.497 , Issue.7450 , pp. 507-511
    • Ho, C.Y.1    Jaalouk, D.E.2    Vartiainen, M.K.3    Lammerding, J.4
  • 80
    • 84883059455 scopus 로고    scopus 로고
    • Nuclear lamin-A scales with tissue stiffness and enhances matrix-directed differentiation
    • J. Swift, I.L. Ivanovska, and A. Buxboim et al. Nuclear lamin-A scales with tissue stiffness and enhances matrix-directed differentiation Science 341 6149 2013 1240104
    • (2013) Science , vol.341 , Issue.6149 , pp. 1240104
    • Swift, J.1    Ivanovska, I.L.2    Buxboim, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.