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1
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Dynamic molecular processes mediate cellular mechanotransduction
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1 Hoffman, B.D., Grashoff, C., Schwartz, M.A., Dynamic molecular processes mediate cellular mechanotransduction. Nature 475 (2011), 316–323.
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Hoffman, B.D.1
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Cell adhesion: integrating cytoskeletal dynamics and cellular tension
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2 Parsons, J.T., Horwitz, A.R., Schwartz, M.A., Cell adhesion: integrating cytoskeletal dynamics and cellular tension. Nat Rev Mol Cell Biol 11 (2010), 633–643.
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Mechanotransduction at a distance: mechanically coupling the extracellular matrix with the nucleus
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3 Wang, N., Tytell, J.D., Ingber, D.E., Mechanotransduction at a distance: mechanically coupling the extracellular matrix with the nucleus. Nat Rev Mol Cell Biol 10 (2009), 75–82.
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Nuclear membrane proteins with potential disease links found by subtractive proteomics
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4 Schirmer, E.C., Florens, L., Guan, T., Yates, J.R., Gerace, L., Nuclear membrane proteins with potential disease links found by subtractive proteomics. Science 301 (2003), 1380–1382.
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5 Simon, D.N., Wilson, K.L., The nucleoskeleton as a genome-associated dynamic “network of networks.”. Nat Rev Mol Cell Biol 12 (2011), 695–708.
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Simon, D.N.1
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6
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Linear arrays of nuclear envelope proteins harness retrograde actin flow for nuclear movement
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6 Luxton, G.W.G., Gomes, E.R., Folker, E.S., Vintinner, E., Gundersen, G.G., Linear arrays of nuclear envelope proteins harness retrograde actin flow for nuclear movement. Science 329 (2010), 956–959.
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Luxton, G.W.G.1
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Gundersen, G.G.5
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7
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84903777793
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FHOD1 interaction with nesprin-2G mediates TAN line formation and nuclear movement
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This study found that FHOD1 interacts with Nesprin 2G and mediates LINC reinforcement by providing an additional actin binding site.
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7•• Kutscheidt, S., Zhu, R., Antoku, S., Luxton, G.W.G., Stagljar, I., Fackler, O.T., Gundersen, G.G., FHOD1 interaction with nesprin-2G mediates TAN line formation and nuclear movement. Nat Cell Biol 16 (2014), 708–715 This study found that FHOD1 interacts with Nesprin 2G and mediates LINC reinforcement by providing an additional actin binding site.
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Nat Cell Biol
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Kutscheidt, S.1
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Stagljar, I.5
Fackler, O.T.6
Gundersen, G.G.7
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8
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84897583394
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Isolated nuclei adapt to force and reveal a mechanotransduction pathway in the nucleus
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This work demonstrates that application of tension to Nesprin triggers an emerin-dependent LINC rearrangement that resists the applied tension.
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8•• Guilluy, C., Osborne, L.D., Van Landeghem, L., Sharek, L., Superfine, R., Garcia-Mata, R., Burridge, K., Isolated nuclei adapt to force and reveal a mechanotransduction pathway in the nucleus. Nat Cell Biol 16 (2014), 376–381 This work demonstrates that application of tension to Nesprin triggers an emerin-dependent LINC rearrangement that resists the applied tension.
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Nat Cell Biol
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Guilluy, C.1
Osborne, L.D.2
Van Landeghem, L.3
Sharek, L.4
Superfine, R.5
Garcia-Mata, R.6
Burridge, K.7
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9
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84883059455
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Nuclear lamin-A scales with tissue stiffness and enhances matrix-directed differentiation
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This remarkable work used proteomics and observed that lamin A/C scales with tissue elasticity and participates to matrix-directed stem cells differentiation.
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9•• Swift, J., Ivanovska, I.L., Buxboim, A., Harada, T., Dingal, P.C.D.P., Pinter, J., Pajerowski, J.D., Spinler, K.R., Shin, J.-W., Tewari, M., Rehfeldt, F., Speicher, D.W., Discher, D.E., Nuclear lamin-A scales with tissue stiffness and enhances matrix-directed differentiation. Science, 341, 2013, 1240104 This remarkable work used proteomics and observed that lamin A/C scales with tissue elasticity and participates to matrix-directed stem cells differentiation.
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Science
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Swift, J.1
Ivanovska, I.L.2
Buxboim, A.3
Harada, T.4
Dingal, P.C.D.P.5
Pinter, J.6
Pajerowski, J.D.7
Spinler, K.R.8
Shin, J.-W.9
Tewari, M.10
Rehfeldt, F.11
Speicher, D.W.12
Discher, D.E.13
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10
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58049211966
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Mechanotransduction at a distance: mechanically coupling the extracellular matrix with the nucleus
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10 Wang, N., Tytell, J.D., Ingber, D.E., Mechanotransduction at a distance: mechanically coupling the extracellular matrix with the nucleus. Nat Rev Mol Cell Biol 10 (2009), 75–82.
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Nat Rev Mol Cell Biol
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Wang, N.1
Tytell, J.D.2
Ingber, D.E.3
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11
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0031017220
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Demonstration of mechanical connections between integrins, cytoskeletal filaments, and nucleoplasm that stabilize nuclear structure
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11 Maniotis, A.J., Chen, C.S., Ingber, D.E., Demonstration of mechanical connections between integrins, cytoskeletal filaments, and nucleoplasm that stabilize nuclear structure. Proc Natl Acad Sci U S A 94 (1997), 849–854.
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Maniotis, A.J.1
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12
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84924341763
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An inside-out origin for the eukaryotic cell
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This work proposes a new ‘inside-out’ model to explain the evolutionary origin of the cell nucleus.
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12•• Baum, D.A., Baum, B., An inside-out origin for the eukaryotic cell. BMC Biol, 12, 2014, 76 This work proposes a new ‘inside-out’ model to explain the evolutionary origin of the cell nucleus.
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Baum, D.A.1
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13
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NUANCE, a giant protein connecting the nucleus and actin cytoskeleton
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13 Zhen, Y.-Y., Libotte, T., Munck, M., Noegel, A.A., Korenbaum, E., NUANCE, a giant protein connecting the nucleus and actin cytoskeleton. J Cell Sci 115 (2002), 3207–3222.
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14
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The inner nuclear membrane protein Sun1 mediates the anchorage of Nesprin-2 to the nuclear envelope
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14 Padmakumar, V.C., Libotte, T., Lu, W., Zaim, H., Abraham, S., Noegel, A.A., Gotzmann, J., Foisner, R., Karakesisoglou, I., The inner nuclear membrane protein Sun1 mediates the anchorage of Nesprin-2 to the nuclear envelope. J Cell Sci 118 (2005), 3419–3430.
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Padmakumar, V.C.1
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Gotzmann, J.7
Foisner, R.8
Karakesisoglou, I.9
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15
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Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectin
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15 Wilhelmsen, K., Litjens, S.H.M., Kuikman, I., Tshimbalanga, N., Janssen, H., van den Bout, I., Raymond, K., Sonnenberg, A., Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectin. J Cell Biol 171 (2005), 799–810.
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Wilhelmsen, K.1
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van den Bout, I.6
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16
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29944445023
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Coupling of the nucleus and cytoplasm: role of the LINC complex
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16 Crisp, M., Liu, Q., Roux, K., Rattner, J.B., Shanahan, C., Burke, B., Stahl, P.D., Hodzic, D., Coupling of the nucleus and cytoplasm: role of the LINC complex. J Cell Biol 172 (2006), 41–53.
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Crisp, M.1
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Hodzic, D.8
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17
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33646555082
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SUN1 interacts with nuclear lamin A and cytoplasmic nesprins to provide a physical connection between the nuclear lamina and the cytoskeleton
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17 Haque, F., Lloyd, D.J., Smallwood, D.T., Dent, C.L., Shanahan, C.M., Fry, A.M., Trembath, R.C., Shackleton, S., SUN1 interacts with nuclear lamin A and cytoplasmic nesprins to provide a physical connection between the nuclear lamina and the cytoskeleton. Mol Cell Biol 26 (2006), 3738–3751.
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Haque, F.1
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18
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34249292723
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Transmembrane protein Sun2 is involved in tethering mammalian meiotic telomeres to the nuclear envelope
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18 Schmitt, J., Benavente, R., Hodzic, D., Höög, C., Stewart, C.L., Alsheimer, M., Transmembrane protein Sun2 is involved in tethering mammalian meiotic telomeres to the nuclear envelope. Proc Natl Acad Sci U S A 104 (2007), 7426–7431.
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Schmitt, J.1
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19
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Identification of a nuclear protein matrix
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19 Berezney, R., Coffey, D.S., Identification of a nuclear protein matrix. Biochem Biophys Res Commun 60 (1974), 1410–1417.
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20
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84896488591
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Estimation of the mechanical connection between apical stress fibers and the nucleus in vascular smooth muscle cells cultured on a substrate
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20 Nagayama, K., Yamazaki, S., Yahiro, Y., Matsumoto, T., Estimation of the mechanical connection between apical stress fibers and the nucleus in vascular smooth muscle cells cultured on a substrate. J Biomech 47 (2014), 1422–1429.
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Nagayama, K.1
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21
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84953409777
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Nesprin-2G, a component of the nuclear LINC complex, is subject to myosin-dependent tension
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21 Arsenovic, P.T., Ramachandran, I., Bathula, K., Zhu, R., Narang, J.D., Noll, N.A., Lemmon, C.A., Gundersen, G.G., Conway, D.E., Nesprin-2G, a component of the nuclear LINC complex, is subject to myosin-dependent tension. Biophys J 110 (2016), 34–43.
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Arsenovic, P.T.1
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22
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Focal contacts as mechanosensors: externally applied local mechanical force induces growth of focal contacts by an mDia1-dependent and ROCK-independent mechanism
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22 Riveline, D., Zamir, E., Balaban, N.Q., Schwarz, U.S., Ishizaki, T., Narumiya, S., Kam, Z., Geiger, B., Bershadsky, A.D., Focal contacts as mechanosensors: externally applied local mechanical force induces growth of focal contacts by an mDia1-dependent and ROCK-independent mechanism. J Cell Biol 153 (2001), 1175–1186.
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Riveline, D.1
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23
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β1- and αv-class integrins cooperate to regulate myosin II during rigidity sensing of fibronectin-based microenvironments
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23 Schiller, H.B., Hermann, M.-R., Polleux, J., Vignaud, T., Zanivan, S., Friedel, C.C., Sun, Z., Raducanu, A., Gottschalk, K.-E., Théry, M., Mann, M., Fässler, R., β1- and αv-class integrins cooperate to regulate myosin II during rigidity sensing of fibronectin-based microenvironments. Nat Cell Biol 15 (2013), 625–636.
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Schiller, H.B.1
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24
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84978174328
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Mechanical regulation of transcription controls Polycomb-mediated gene silencing during lineage commitment
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This work demonstrates that heterochromatin connection to the lamina is affected by tension, via an emerin-dependent regulation of nuclear actin level, resulting in gene expression regulation and stem cell commitment.
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24•• Huy, Q.L., Ghatak, S., Chloé Yeung, C.-Y., Tellkamp, F., Günschmann, C., Dieterich, C., Yeroslaviz, A., Habermann, B., Pombo, A., Niessen, C.M., Wickström, S.A., Mechanical regulation of transcription controls Polycomb-mediated gene silencing during lineage commitment. Nat Cell Biol, 2016 This work demonstrates that heterochromatin connection to the lamina is affected by tension, via an emerin-dependent regulation of nuclear actin level, resulting in gene expression regulation and stem cell commitment.
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Nat Cell Biol
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Huy, Q.L.1
Ghatak, S.2
Chloé Yeung, C.-Y.3
Tellkamp, F.4
Günschmann, C.5
Dieterich, C.6
Yeroslaviz, A.7
Habermann, B.8
Pombo, A.9
Niessen, C.M.10
Wickström, S.A.11
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25
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Rho-stimulated contractility drives the formation of stress fibers and focal adhesions
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25 Chrzanowska-Wodnicka, M., Burridge, K., Rho-stimulated contractility drives the formation of stress fibers and focal adhesions. J Cell Biol 133 (1996), 1403–1415.
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Chrzanowska-Wodnicka, M.1
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26
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LINC complexes form by binding of three KASH peptides to domain interfaces of trimeric SUN proteins
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26 Sosa, B.A., Rothballer, A., Kutay, U., Schwartz, T.U., LINC complexes form by binding of three KASH peptides to domain interfaces of trimeric SUN proteins. Cell 149 (2012), 1035–1047.
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Sosa, B.A.1
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27
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Coiled-coil domains of SUN proteins as intrinsic dynamic regulators
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27 Nie, S., Ke, H., Gao, F., Ren, J., Wang, M., Huo, L., Gong, W., Feng, W., Coiled-coil domains of SUN proteins as intrinsic dynamic regulators. Struct Lond Engl 1993 24 (2016), 80–91.
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28 Schwartz, M.A., Cell biology. The force is with us. Science 323 (2009), 588–589.
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Lamin A variants that cause striated muscle disease are defective in anchoring transmembrane actin-associated nuclear lines for nuclear movement
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29 Folker, E.S., Ostlund, C., Luxton, G.W.G., Worman, H.J., Gundersen, G.G., Lamin A variants that cause striated muscle disease are defective in anchoring transmembrane actin-associated nuclear lines for nuclear movement. Proc Natl Acad Sci U S A 108 (2011), 131–136.
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30
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Matrix elasticity regulates lamin-A, C phosphorylation and turnover with feedback to actomyosin
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30 Buxboim, A., Swift, J., Irianto, J., Spinler, K.R., Dingal, P.C.D.P., Athirasala, A., Kao, Y.-R.C., Cho, S., Harada, T., Shin, J.-W., Discher, D.E., Matrix elasticity regulates lamin-A, C phosphorylation and turnover with feedback to actomyosin. Curr Biol CB, 2014.
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Use the force: membrane tension as an organizer of cell shape and motility
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31 Diz-Muñoz, A., Fletcher, D.A., Weiner, O.D., Use the force: membrane tension as an organizer of cell shape and motility. Trends Cell Biol 23 (2013), 47–53.
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32 Malhas, A., Goulbourne, C., Vaux, D.J., The nucleoplasmic reticulum: form and function. Trends Cell Biol 21 (2011), 362–373.
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33
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The nuclear envelope lamina network has elasticity and a compressibility limit suggestive of a molecular shock absorber
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33 Dahl, K.N., Kahn, S.M., Wilson, K.L., Discher, D.E., The nuclear envelope lamina network has elasticity and a compressibility limit suggestive of a molecular shock absorber. J Cell Sci 117 (2004), 4779–4786.
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Dahl, K.N.1
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34
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34 Dahl, K.N., Engler, A.J., Pajerowski, J.D., Discher, D.E., Power-law rheology of isolated nuclei with deformation mapping of nuclear substructures. Biophys J 89 (2005), 2855–2864.
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Dahl, K.N.1
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35 van Meer, G., Voelker, D.R., Feigenson, G.W., Membrane lipids: where they are and how they behave. Nat Rev Mol Cell Biol 9 (2008), 112–124.
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36 Bigay, J., Antonny, B., Curvature, Lipid packing, and electrostatics of membrane organelles: defining cellular territories in determining specificity. Dev Cell 23 (2012), 886–895.
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Integrative structure–function mapping of the nucleoporin Nup133 suggests a conserved mechanism for membrane anchoring of the nuclear pore complex
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37 Kim, S.J., Fernandez-Martinez, J., Sampathkumar, P., Martel, A., Matsui, T., Tsuruta, H., Weiss, T.M., Shi, Y., Markina-Inarrairaegui, A., Bonanno, J.B., Sauder, J.M., Burley, S.K., Chait, B.T., Almo, S.C., Rout, M.P., Sali, A., Integrative structure–function mapping of the nucleoporin Nup133 suggests a conserved mechanism for membrane anchoring of the nuclear pore complex. Mol Cell Proteomics MCP 13 (2014), 2911–2926.
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38
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The cell nucleus serves as a mechanotransducer of tissue damage-induced inflammation
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This study demonstrated that nuclear translocation of PLA2 mediates a mechanotransduction mechanism in response to nuclear swelling during tissue damage.
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38•• Enyedi, B., Jelcic, M., Niethammer, P., The cell nucleus serves as a mechanotransducer of tissue damage-induced inflammation. Cell 165 (2016), 1160–1170 This study demonstrated that nuclear translocation of PLA2 mediates a mechanotransduction mechanism in response to nuclear swelling during tissue damage.
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Enyedi, B.1
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39
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