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Volumn 17, Issue 2, 2015, Pages 148-159

Cdk1-dependent mitotic enrichment of cortical myosin II promotes cell rounding against confinement

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIN DEPENDENT KINASE 1; F ACTIN; MYOSIN ADENOSINE TRIPHOSPHATASE; MYOSIN II; P21 ACTIVATED KINASE; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; RHO KINASE; 3-TRITYLTHIO-L-ALANINE; ACTIN; ACTIN BINDING PROTEIN; CYSTEINE; FETOPROTEIN; FORMIN 1; GREEN FLUORESCENT PROTEIN; NUCLEAR PROTEIN;

EID: 84923200288     PISSN: 14657392     EISSN: 14764679     Source Type: Journal    
DOI: 10.1038/ncb3098     Document Type: Article
Times cited : (114)

References (69)
  • 1
    • 8844269688 scopus 로고
    • Observations on the changes seen in living cells during growth and division
    • Strangeways, T. S. P. Observations on the changes seen in living cells during growth and division. Proc. R. Soc. Lond. B 94, 137-141 (1922).
    • (1922) Proc. R. Soc. Lond. B , vol.94 , pp. 137-141
    • Strangeways, T.S.P.1
  • 2
    • 79952815145 scopus 로고    scopus 로고
    • Interkinetic nuclear migration is a broadly conserved feature of cell division in pseudostratified epithelia
    • Meyer, E. J., Ikmi, A. & Gibson, M. C. Interkinetic nuclear migration is a broadly conserved feature of cell division in pseudostratified epithelia. Curr. Biol. 21, 485-491 (2011).
    • (2011) Curr. Biol. , vol.21 , pp. 485-491
    • Meyer, E.J.1    Ikmi, A.2    Gibson, M.C.3
  • 3
    • 79952282364 scopus 로고    scopus 로고
    • Developmental roles for Srf, cortical cytoskeleton and cell shape in epidermal spindle orientation
    • Luxenburg, C., Amalia Pasolli, H., Williams, S. E. & Fuchs, E. Developmental roles for Srf, cortical cytoskeleton and cell shape in epidermal spindle orientation. Nat. Cell Biol. 13, 203-214 (2011).
    • (2011) Nat. Cell Biol. , vol.13 , pp. 203-214
    • Luxenburg, C.1    Amalia Pasolli, H.2    Williams, S.E.3    Fuchs, E.4
  • 4
    • 84874740674 scopus 로고    scopus 로고
    • Mitotic cell rounding accelerates epithelial invagination
    • Kondo, T. & Hayashi, S. Mitotic cell rounding accelerates epithelial invagination. Nature 494, 125-129 (2013).
    • (2013) Nature , vol.494 , pp. 125-129
    • Kondo, T.1    Hayashi, S.2
  • 5
    • 84881663995 scopus 로고    scopus 로고
    • Epithelial junctions maintain tissue architecture by directing planar spindle orientation
    • Nakajima, Y., Meyer, E. J., Kroesen, A., McKinney, S. A. & Gibson, M. C. Epithelial junctions maintain tissue architecture by directing planar spindle orientation. Nature 500, 359-362 (2013).
    • (2013) Nature , vol.500 , pp. 359-362
    • Nakajima, Y.1    Meyer, E.J.2    Kroesen, A.3    McKinney, S.A.4    Gibson, M.C.5
  • 6
    • 84877800188 scopus 로고    scopus 로고
    • Mitotic rounding alters cell geometry to ensure efficient bipolar spindle formation
    • Lancaster, O. M. et al. Mitotic rounding alters cell geometry to ensure efficient bipolar spindle formation. Dev. Cell 25, 270-283 (2013).
    • (2013) Dev. Cell , vol.25 , pp. 270-283
    • Lancaster, O.M.1
  • 7
    • 84862661844 scopus 로고    scopus 로고
    • Increased asymmetric and multidaughter cell division in mechanically confined microenvironments
    • Tse, H. T. K., Weaver, W. M. & Di Carlo, D. Increased asymmetric and multidaughter cell division in mechanically confined microenvironments. PLoS ONE 7, e38986 (2012).
    • (2012) PLoS ONE , vol.7 , pp. e38986
    • Tse, H.T.K.1    Weaver, W.M.2    Di Carlo, D.3
  • 8
    • 27144473914 scopus 로고    scopus 로고
    • The extracellular matrix guides the orientation of the cell division axis
    • Thery, M. et al. The extracellular matrix guides the orientation of the cell division axis. Nat. Cell Biol. 7, 947-953 (2005).
    • (2005) Nat. Cell Biol. , vol.7 , pp. 947-953
    • Thery, M.1
  • 9
    • 33947596005 scopus 로고    scopus 로고
    • Integrin-mediated adhesion orients the spindle parallel to the substratum in an EB1-and myosin X-dependent manner
    • Toyoshima, F. & Nishida, E. Integrin-mediated adhesion orients the spindle parallel to the substratum in an EB1-and myosin X-dependent manner. EMBO J. 26, 1487-1498 (2007).
    • (2007) EMBO J. , vol.26 , pp. 1487-1498
    • Toyoshima, F.1    Nishida, E.2
  • 10
    • 78651388574 scopus 로고    scopus 로고
    • Hydrostatic pressure and the actomyosin cortex drive mitotic cell rounding
    • Stewart, M. P. et al. Hydrostatic pressure and the actomyosin cortex drive mitotic cell rounding. Nature 469, 226-230 (2011).
    • (2011) Nature , vol.469 , pp. 226-230
    • Stewart, M.P.1
  • 11
    • 0030847202 scopus 로고    scopus 로고
    • Investigation of the mechanism of retraction of the cell margin and rearward flow of nodules during mitotic cell rounding
    • Cramer, L. P. & Mitchison, T. J. Investigation of the mechanism of retraction of the cell margin and rearward flow of nodules during mitotic cell rounding. Mol. Biol. Cell 8, 109-119 (1997).
    • (1997) Mol. Biol. Cell , vol.8 , pp. 109-119
    • Cramer, L.P.1    Mitchison, T.J.2
  • 12
    • 0037455574 scopus 로고    scopus 로고
    • RhoA is required for cortical retraction and rigidity during mitotic cell rounding
    • Maddox, A. S. & Burridge, K. RhoA is required for cortical retraction and rigidity during mitotic cell rounding. J. Cell Biol. 160, 255-265 (2003).
    • (2003) J. Cell Biol. , vol.160 , pp. 255-265
    • Maddox, A.S.1    Burridge, K.2
  • 13
    • 38349022141 scopus 로고    scopus 로고
    • Moesin controls cortical rigidity, cell rounding, and spindle morphogenesis during mitosis
    • Kunda, P., Pelling, A. E., Liu, T. & Baum, B. Moesin controls cortical rigidity, cell rounding, and spindle morphogenesis during mitosis. Curr. Biol. 18, 91-101 (2008).
    • (2008) Curr. Biol. , vol.18 , pp. 91-101
    • Kunda, P.1    Pelling, A.E.2    Liu, T.3    Baum, B.4
  • 14
    • 0033787392 scopus 로고    scopus 로고
    • Conditional expression of a truncated fragment of nonmuscle myosin II-A alters cell shape but not cytokinesis in HeLa cells
    • Wei, Q. Z. & Adelstein, R. S. Conditional expression of a truncated fragment of nonmuscle myosin II-A alters cell shape but not cytokinesis in HeLa cells. Mol. Biol. Cell 11, 3617-3627 (2000).
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3617-3627
    • Wei, Q.Z.1    Adelstein, R.S.2
  • 16
    • 84874652759 scopus 로고    scopus 로고
    • A genomic toolkit to investigate kinesin and myosin motor function in cells
    • Maliga, Z. et al. A genomic toolkit to investigate kinesin and myosin motor function in cells. Nat. Cell Biol. 15, 325-334 (2013).
    • (2013) Nat. Cell Biol. , vol.15 , pp. 325-334
    • Maliga, Z.1
  • 17
    • 84881399835 scopus 로고    scopus 로고
    • Monitoring actin cortex thickness in live cells
    • Clark, A. G., Dierkes, K. & Paluch, E. K. Monitoring actin cortex thickness in live cells. Biophys. J. 105, 570-580 (2013).
    • (2013) Biophys. J. , vol.105 , pp. 570-580
    • Clark, A.G.1    Dierkes, K.2    Paluch, E.K.3
  • 18
    • 46249118002 scopus 로고    scopus 로고
    • Lifeact: A versatile marker to visualize F-actin
    • Riedl, J. et al. Lifeact: A versatile marker to visualize F-actin. Nat. Methods 5, 605-607 (2008).
    • (2008) Nat. Methods , vol.5 , pp. 605-607
    • Riedl, J.1
  • 19
    • 0030661929 scopus 로고    scopus 로고
    • Mitosis specific serine phosphorylation and downregulation of one of the focal adhesion protein, paxillin
    • Yamaguchi, R., Mazaki, Y., Hirota, K., Hashimoto, S. & Sabe, H. Mitosis specific serine phosphorylation and downregulation of one of the focal adhesion protein, paxillin. Oncogene 15, 1753-1761 (1997).
    • (1997) Oncogene , vol.15 , pp. 1753-1761
    • Yamaguchi, R.1    Mazaki, Y.2    Hirota, K.3    Hashimoto, S.4    Sabe, H.5
  • 20
    • 0033601745 scopus 로고    scopus 로고
    • Dissociation of FAK/p130(CAS)/c-Src complex during mitosis: Role of mitosis-specific serine phosphorylation of FAK
    • Yamakita, Y. et al. Dissociation of FAK/p130(CAS)/c-Src complex during mitosis: Role of mitosis-specific serine phosphorylation of FAK. J. Cell Biol. 144, 315-324 (1999).
    • (1999) J. Cell Biol. , vol.144 , pp. 315-324
    • Yamakita, Y.1
  • 21
    • 84861148456 scopus 로고    scopus 로고
    • Tracking mechanics and volume of globular cells with atomic force microscopy using a constant-height clamp
    • Stewart, M. P., Toyoda, Y., Hyman, A. A. & Müller, D. J. Tracking mechanics and volume of globular cells with atomic force microscopy using a constant-height clamp. Nat. Protoc. 7, 143-154 (2012).
    • (2012) Nat. Protoc. , vol.7 , pp. 143-154
    • Stewart, M.P.1    Toyoda, Y.2    Hyman, A.A.3    Müller, D.J.4
  • 22
    • 84878253019 scopus 로고    scopus 로고
    • Wedged AFM-cantilevers for parallel plate cell mechanics
    • Stewart, M. P. et al. Wedged AFM-cantilevers for parallel plate cell mechanics. Methods 60, 186-194 (2013).
    • (2013) Methods , vol.60 , pp. 186-194
    • Stewart, M.P.1
  • 23
    • 84906819232 scopus 로고    scopus 로고
    • Quantification of surface tension and internal pressure generated by single mitotic cells
    • Fischer-Friedrich, E., Hyman, A. A., Jülicher, F., Müller, D. J. & Helenius, J. Quantification of surface tension and internal pressure generated by single mitotic cells. Sci. Rep. 4, 6213 (2014).
    • (2014) Sci. Rep. , vol.4 , pp. 6213
    • Fischer-Friedrich, E.1    Hyman, A.A.2    Jülicher, F.3    Müller, D.J.4    Helenius, J.5
  • 24
    • 0037436506 scopus 로고    scopus 로고
    • Dissecting temporal and spatial control of cytokinesis with a myosin II Inhibitor
    • Straight, A. F. et al. Dissecting temporal and spatial control of cytokinesis with a myosin II Inhibitor. Science 299, 1743-1747 (2003).
    • (2003) Science , vol.299 , pp. 1743-1747
    • Straight, A.F.1
  • 25
    • 0142148230 scopus 로고    scopus 로고
    • Polarized actin bundles formed by human fascin-1: Their sliding and disassembly on myosin II and myosin v in vitro
    • Ishikawa, R., Sakamoto, T., Ando, T., Higashi-Fujime, S. & Kohama, K. Polarized actin bundles formed by human fascin-1: Their sliding and disassembly on myosin II and myosin V in vitro. J. Neurochem. 87, 676-685 (2003).
    • (2003) J. Neurochem. , vol.87 , pp. 676-685
    • Ishikawa, R.1    Sakamoto, T.2    Ando, T.3    Higashi-Fujime, S.4    Kohama, K.5
  • 26
    • 18044363909 scopus 로고    scopus 로고
    • Cortical actin turnover during cytokinesis requires myosin II
    • Guha, M., Zhou, M. & Wang, Y. L. Cortical actin turnover during cytokinesis requires myosin II. Curr. Biol. 15, 732-736 (2005).
    • (2005) Curr. Biol. , vol.15 , pp. 732-736
    • Guha, M.1    Zhou, M.2    Wang, Y.L.3
  • 27
    • 18044368530 scopus 로고    scopus 로고
    • Myosin-II-dependent localization and dynamics of F-actin during cytokinesis
    • Murthy, K. & Wadsworth, P. Myosin-II-dependent localization and dynamics of F-actin during cytokinesis. Curr. Biol. 15, 724-731 (2005).
    • (2005) Curr. Biol. , vol.15 , pp. 724-731
    • Murthy, K.1    Wadsworth, P.2
  • 28
    • 77952687450 scopus 로고    scopus 로고
    • Myosin II contributes to cell-scale actin network treadmilling through network disassembly
    • Wilson, C. A. et al. Myosin II contributes to cell-scale actin network treadmilling through network disassembly. Nature 465, 373-377 (2010).
    • (2010) Nature , vol.465 , pp. 373-377
    • Wilson, C.A.1
  • 29
    • 84880007581 scopus 로고    scopus 로고
    • Myosin II does it all: Assembly, remodeling, and disassembly of actin networks are governed by myosin II activity
    • Ideses, Y., Sonn-Segev, A., Roichman, Y. & Bernheim-Groswasser, A. Myosin II does it all: Assembly, remodeling, and disassembly of actin networks are governed by myosin II activity. Soft Matter 9, 7127-7137 (2013).
    • (2013) Soft Matter , vol.9 , pp. 7127-7137
    • Ideses, Y.1    Sonn-Segev, A.2    Roichman, Y.3    Bernheim-Groswasser, A.4
  • 30
    • 84875159684 scopus 로고    scopus 로고
    • Analysis of turnover dynamics of the submembranous actin cortex
    • Fritzsche, M., Lewalle, A., Duke, T., Kruse, K. & Charras, G. Analysis of turnover dynamics of the submembranous actin cortex. Mol. Biol. Cell 24, 757-767 (2013).
    • (2013) Mol. Biol. Cell , vol.24 , pp. 757-767
    • Fritzsche, M.1    Lewalle, A.2    Duke, T.3    Kruse, K.4    Charras, G.5
  • 32
    • 43249129458 scopus 로고    scopus 로고
    • MYH9-siRNA and MYH9 mutant alleles: Expression in cultured cell lines and their effects upon cell structure and function
    • Li, Y., Friedmann, D. R., Mhatre, A. N. & Lalwani, A. K. MYH9-siRNA and MYH9 mutant alleles: Expression in cultured cell lines and their effects upon cell structure and function. Cell Motil. Cytoskeleton 65, 393-405 (2008).
    • (2008) Cell Motil. Cytoskeleton , vol.65 , pp. 393-405
    • Li, Y.1    Friedmann, D.R.2    Mhatre, A.N.3    Lalwani, A.K.4
  • 33
    • 65349102972 scopus 로고    scopus 로고
    • The decision to enter mitosis: Feedback and redundancy in the mitotic entry network
    • Lindqvist, A., Rodriguez-Bravo, V. & Medema, R. H. The decision to enter mitosis: Feedback and redundancy in the mitotic entry network. J. Cell Biol. 185, 193-202 (2009).
    • (2009) J. Cell Biol. , vol.185 , pp. 193-202
    • Lindqvist, A.1    Rodriguez-Bravo, V.2    Medema, R.H.3
  • 34
    • 77951177406 scopus 로고    scopus 로고
    • Activation of cyclin B1-Cdk1 synchronizes events in the nucleus and the cytoplasm at mitosis
    • Gavet, O. & Pines, J. Activation of cyclin B1-Cdk1 synchronizes events in the nucleus and the cytoplasm at mitosis. J. Cell Biol. 189, 247-259 (2010).
    • (2010) J. Cell Biol. , vol.189 , pp. 247-259
    • Gavet, O.1    Pines, J.2
  • 35
    • 77951184302 scopus 로고    scopus 로고
    • Progressive activation of CyclinB1-Cdk1 coordinates entry to mitosis
    • Gavet, O. & Pines, J. Progressive activation of CyclinB1-Cdk1 coordinates entry to mitosis. Dev. Cell 18, 533-543 (2010).
    • (2010) Dev. Cell , vol.18 , pp. 533-543
    • Gavet, O.1    Pines, J.2
  • 36
    • 0026648333 scopus 로고
    • Phosphorylation of myosin-II regulatory light chain by cyclin-p34cdc2: A mechanism for the timing of cytokinesis
    • Satterwhite, L. L. et al. Phosphorylation of myosin-II regulatory light chain by cyclin-p34cdc2: A mechanism for the timing of cytokinesis. J. Cell Biol. 118, 595-605 (1992).
    • (1992) J. Cell Biol. , vol.118 , pp. 595-605
    • Satterwhite, L.L.1
  • 37
    • 0028123676 scopus 로고
    • In vivo phosphorylation of regulatory light chain of myosin II during mitosis of cultured cells
    • Yamakita, Y., Yamashiro, S. & Matsumura, F. In vivo phosphorylation of regulatory light chain of myosin II during mitosis of cultured cells. J. Cell Biol. 124, 129-137 (1994).
    • (1994) J. Cell Biol. , vol.124 , pp. 129-137
    • Yamakita, Y.1    Yamashiro, S.2    Matsumura, F.3
  • 38
    • 84865102938 scopus 로고    scopus 로고
    • Changes in Ect2 localization couple actomyosin-dependent cell shape changes to mitotic progression
    • Matthews, H. K. et al. Changes in Ect2 localization couple actomyosin-dependent cell shape changes to mitotic progression. Dev. Cell 23, 371-383 (2012).
    • (2012) Dev. Cell , vol.23 , pp. 371-383
    • Matthews, H.K.1
  • 39
    • 33745867225 scopus 로고    scopus 로고
    • S-trityl-L-cysteine is a reversible, tight binding inhibitor of the human kinesin Eg5 that specifically blocks mitotic progression
    • Skoufias, D. A. et al. S-trityl-L-cysteine is a reversible, tight binding inhibitor of the human kinesin Eg5 that specifically blocks mitotic progression. J. Biol. Chem. 281, 17559-17569 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 17559-17569
    • Skoufias, D.A.1
  • 40
    • 3042789558 scopus 로고    scopus 로고
    • Phototoxicity and photoinactivation of blebbistatin in UV and visible light
    • Kolega, J. Phototoxicity and photoinactivation of blebbistatin in UV and visible light. Biochem. Biophys. Res. Commun. 320, 1020-1025 (2004).
    • (2004) Biochem. Biophys. Res. Commun. , vol.320 , pp. 1020-1025
    • Kolega, J.1
  • 41
    • 27944479854 scopus 로고    scopus 로고
    • Rho GTPases: Biochemistry and biology
    • Jaffe, A. B. & Hall, A. Rho GTPases: Biochemistry and biology. Annu. Rev. Cell Dev. Biol. 21, 247-269 (2005).
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 247-269
    • Jaffe, A.B.1    Hall, A.2
  • 42
    • 0033615978 scopus 로고    scopus 로고
    • Human Ect2 is an exchange factor for Rho GTPases, phosphorylated in G2/M Phases, and involved in cytokinesis
    • Tatsumoto, T., Xie, X., Blumenthal, R., Okamoto, I. & Miki, T. Human Ect2 is an exchange factor for Rho GTPases, phosphorylated in G2/M Phases, and involved in cytokinesis. J. Cell Biol. 147, 921-928 (1999).
    • (1999) J. Cell Biol. , vol.147 , pp. 921-928
    • Tatsumoto, T.1    Xie, X.2    Blumenthal, R.3    Okamoto, I.4    Miki, T.5
  • 43
    • 0024584734 scopus 로고
    • The rho gene product expressed in e Coli is a substrate of botulinum ADP-ribosyltransferase C3
    • Aktories, K., Braun, U., Rösener, S., Just, I. & Hall, A. The rho gene product expressed in E. Coli is a substrate of botulinum ADP-ribosyltransferase C3. Biochem. Biophys. Res. Commun. 158, 209-213 (1989).
    • (1989) Biochem. Biophys. Res. Commun. , vol.158 , pp. 209-213
    • Aktories, K.1    Braun, U.2    Rösener, S.3    Just, I.4    Hall, A.5
  • 44
    • 2442664118 scopus 로고    scopus 로고
    • Rational design and characterization of a Rac GTPase-specific small molecule inhibitor
    • Gao, Y., Dickerson, J. B., Guo, F., Zheng, J. & Zheng, Y. Rational design and characterization of a Rac GTPase-specific small molecule inhibitor. Proc. Natl Acad. Sci. USA 101, 7618-7623 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 7618-7623
    • Gao, Y.1    Dickerson, J.B.2    Guo, F.3    Zheng, J.4    Zheng, Y.5
  • 45
    • 27844581709 scopus 로고    scopus 로고
    • RAC1 inhibition targets amyloid precursor protein processing by gamma-secretase and decreases Abeta production in vitro and in vivo
    • Désiré, L. et al. RAC1 inhibition targets amyloid precursor protein processing by gamma-secretase and decreases Abeta production in vitro and in vivo. J. Biol. Chem. 280, 37516-37525 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 37516-37525
    • Désiré, L.1
  • 46
    • 33646073413 scopus 로고    scopus 로고
    • Biochemical suppression of small-molecule inhibitors: A strategy to identify inhibitor targets and signaling pathway components
    • Peterson, J. R., Lebensohn, A. M., Pelish, H. E. & Kirschner, M. W. Biochemical suppression of small-molecule inhibitors: A strategy to identify inhibitor targets and signaling pathway components. Chem. Biol. 13, 443-452 (2006).
    • (2006) Chem. Biol. , vol.13 , pp. 443-452
    • Peterson, J.R.1    Lebensohn, A.M.2    Pelish, H.E.3    Kirschner, M.W.4
  • 48
    • 0033553428 scopus 로고    scopus 로고
    • Evidence for a calpeptin-sensitive proteintyrosine phosphatase upstream of the small GTPase Rho. Novel role for the calpain inhibitor calpeptin in the inhibition of protein-tyrosine phosphatases
    • Schoenwaelder, S. M. & Burridge, K. Evidence for a calpeptin-sensitive proteintyrosine phosphatase upstream of the small GTPase Rho. Novel role for the calpain inhibitor calpeptin in the inhibition of protein-tyrosine phosphatases. J. Biol. Chem. 274, 14359-14367 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 14359-14367
    • Schoenwaelder, S.M.1    Burridge, K.2
  • 49
    • 0030656619 scopus 로고    scopus 로고
    • Calcium sensitization of smooth muscle mediated by a Rhoassociated protein kinase in hypertension
    • Uehata, M. et al. Calcium sensitization of smooth muscle mediated by a Rhoassociated protein kinase in hypertension. Nature 389, 990-994 (1997).
    • (1997) Nature , vol.389 , pp. 990-994
    • Uehata, M.1
  • 50
    • 0028078824 scopus 로고
    • A brain serine/threonine protein kinase activated by Cdc42 and Rac1
    • Manser, E., Leung, T., Salihuddin, H., Zhao, Z. & Lim, L. A brain serine/threonine protein kinase activated by Cdc42 and Rac1. Nature 367, 40-46 (1994).
    • (1994) Nature , vol.367 , pp. 40-46
    • Manser, E.1    Leung, T.2    Salihuddin, H.3    Zhao, Z.4    Lim, L.5
  • 51
    • 0034002084 scopus 로고    scopus 로고
    • Endothelial cell retraction is induced by PAK2 monophosphorylation of myosin II
    • Zeng, Q. et al. Endothelial cell retraction is induced by PAK2 monophosphorylation of myosin II. J. Cell Sci. 113, 471-482 (2000).
    • (2000) J. Cell Sci. , vol.113 , pp. 471-482
    • Zeng, Q.1
  • 52
    • 0037162289 scopus 로고    scopus 로고
    • Cell cycle-regulated phosphorylation of p21-activated kinase
    • Thiel, D. A. et al. Cell cycle-regulated phosphorylation of p21-activated kinase. Curr. Biol. 12, 1227-1232 (2002).
    • (2002) Curr. Biol. , vol.12 , pp. 1227-1232
    • Thiel, D.A.1
  • 53
    • 33646889963 scopus 로고    scopus 로고
    • Activation of myosin in HeLa cells causes redistribution of focal adhesions and F-actin from cell center to cell periphery
    • Szczepanowska, J., Korn, E. D. & Brzeska, H. Activation of myosin in HeLa cells causes redistribution of focal adhesions and F-actin from cell center to cell periphery. Cell Motil. Cytoskeleton 63, 356-374 (2006).
    • (2006) Cell Motil. Cytoskeleton , vol.63 , pp. 356-374
    • Szczepanowska, J.1    Korn, E.D.2    Brzeska, H.3
  • 54
    • 50049129364 scopus 로고    scopus 로고
    • P21-activated kinase is required for mitotic progression and regulates Plk1
    • Maroto, B., Ye, M. B., von Lohneysen, K., Schnelzer, A. & Knaus, U. G. P21-activated kinase is required for mitotic progression and regulates Plk1. Oncogene 27, 4900-4908 (2008).
    • (2008) Oncogene , vol.27 , pp. 4900-4908
    • Maroto, B.1    Ye, M.B.2    Von Lohneysen, K.3    Schnelzer, A.4    Knaus, U.G.5
  • 55
    • 41949100602 scopus 로고    scopus 로고
    • An isoform-selective, small-molecule inhibitor targets the autoregulatory mechanism of p21-activated kinase
    • Deacon, S. W. et al. An isoform-selective, small-molecule inhibitor targets the autoregulatory mechanism of p21-activated kinase. Chem. Biol. 15, 322-331 (2008).
    • (2008) Chem. Biol. , vol.15 , pp. 322-331
    • Deacon, S.W.1
  • 56
    • 0030911424 scopus 로고    scopus 로고
    • 140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin
    • Watanabe, N. et al. p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin. EMBO J. 16, 3044-3056 (1997).
    • (1997) EMBO J. , vol.16 , pp. 3044-3056
    • Watanabe, N.1
  • 57
    • 0032430263 scopus 로고    scopus 로고
    • The Arp2/3 complex mediates actin polymerization induced by the small GTP-binding protein Cdc42
    • Ma, L., Rohatgi, R. & Kirschner, M. W. The Arp2/3 complex mediates actin polymerization induced by the small GTP-binding protein Cdc42. Proc. Natl Acad. Sci. USA 95, 15362-15367 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 15362-15367
    • Ma, L.1    Rohatgi, R.2    Kirschner, M.W.3
  • 58
    • 84904968718 scopus 로고    scopus 로고
    • Cellular control of cortical actin nucleation
    • Bovellan, M. et al. Cellular control of cortical actin nucleation. Curr. Biol. 24, 1628-1635 (2014).
    • (2014) Curr. Biol. , vol.24 , pp. 1628-1635
    • Bovellan, M.1
  • 59
    • 72049090358 scopus 로고    scopus 로고
    • Identification and characterization of a small molecule inhibitor of formin-mediated actin assembly
    • Rizvi, S. A. et al. Identification and characterization of a small molecule inhibitor of formin-mediated actin assembly. Chem. Biol. 16, 1158-1168 (2009).
    • (2009) Chem. Biol. , vol.16 , pp. 1158-1168
    • Rizvi, S.A.1
  • 60
    • 69249212192 scopus 로고    scopus 로고
    • Characterization of two classes of small molecule inhibitors of Arp2/3 complex
    • Nolen, B. J. et al. Characterization of two classes of small molecule inhibitors of Arp2/3 complex. Nature 460, 1031-1034 (2009).
    • (2009) Nature , vol.460 , pp. 1031-1034
    • Nolen, B.J.1
  • 61
    • 79952282364 scopus 로고    scopus 로고
    • Developmental roles for Srf, cortical cytoskeleton and cell shape in epidermal spindle orientation
    • Luxenburg, C., Amalia Pasolli, H., Williams, S. E. & Fuchs, E. Developmental roles for Srf, cortical cytoskeleton and cell shape in epidermal spindle orientation. Nat. Cell Biol. 13, 203-214 (2011).
    • (2011) Nat. Cell Biol. , vol.13 , pp. 203-214
    • Luxenburg, C.1    Amalia Pasolli, H.2    Williams, S.E.3    Fuchs, E.4
  • 62
    • 79959723436 scopus 로고    scopus 로고
    • Mechanics and regulation of cell shape during the cell cycle
    • Clark, A. G. & Paluch, E. Mechanics and regulation of cell shape during the cell cycle. Results Probl. Cell Differ. 53, 31-73 (2011).
    • (2011) Results Probl. Cell Differ. , vol.53 , pp. 31-73
    • Clark, A.G.1    Paluch, E.2
  • 63
    • 79960922610 scopus 로고    scopus 로고
    • Quantitative proteomics reveals the basis for the biochemical specificity of the cell-cycle machinery
    • Pagliuca, F. W. et al. Quantitative proteomics reveals the basis for the biochemical specificity of the cell-cycle machinery. Mol. Cell 43, 406-417 (2011).
    • (2011) Mol. Cell , vol.43 , pp. 406-417
    • Pagliuca, F.W.1
  • 64
    • 66249133671 scopus 로고    scopus 로고
    • Plk1 self-organization and priming phosphorylation of HsCYK-4 at the spindle midzone regulate the onset of division in human cells
    • Burkard, M. E. et al. Plk1 self-organization and priming phosphorylation of HsCYK-4 at the spindle midzone regulate the onset of division in human cells. PLoS Biol. 7, e1000111 (2009).
    • (2009) PLoS Biol. , vol.7 , pp. e1000111
    • Burkard, M.E.1
  • 65
    • 66249092744 scopus 로고    scopus 로고
    • Polo-Like kinase 1 directs assembly of the HsCyk-4 RhoGAP/Ect2 RhoGEF complex to initiate cleavage furrow formation
    • Wolfe, B. A., Takaki, T., Petronczki, M. & Glotzer, M. Polo-Like kinase 1 directs assembly of the HsCyk-4 RhoGAP/Ect2 RhoGEF complex to initiate cleavage furrow formation. PLoS Biol. 7, e1000110 (2009).
    • (2009) PLoS Biol. , vol.7 , pp. e1000110
    • Wolfe, B.A.1    Takaki, T.2    Petronczki, M.3    Glotzer, M.4
  • 66
    • 31644438188 scopus 로고    scopus 로고
    • Centralspindlin regulates ECT2 and RhoA accumulation at the equatorial cortex during cytokinesis
    • Nishimura, Y. & Yonemura, S. Centralspindlin regulates ECT2 and RhoA accumulation at the equatorial cortex during cytokinesis. J. Cell Sci. 119, 104-114 (2006).
    • (2006) J. Cell Sci. , vol.119 , pp. 104-114
    • Nishimura, Y.1    Yonemura, S.2
  • 67
    • 0037244352 scopus 로고    scopus 로고
    • Rhogef and rho family gtpase-activating protein complex links the contractile ring to cortical microtubules at the onset of cytokinesis
    • Somers, W. G. & Saint, R. A RhoGEF and Rho family GTPase-activating protein complex links the contractile ring to cortical microtubules at the onset of cytokinesis. Dev. Cell 4, 29-39 (2003).
    • (2003) Dev. Cell , vol.4 , pp. 29-39
    • Somers, W.G.1    Saint, R.A.2
  • 68
    • 84856516992 scopus 로고    scopus 로고
    • Biomechanical regulation of contractility: Spatial control and dynamics
    • Levayer, R. & Lecuit, T. Biomechanical regulation of contractility: Spatial control and dynamics. Trends Cell Biol. 22, 61-81 (2012).
    • (2012) Trends Cell Biol. , vol.22 , pp. 61-81
    • Levayer, R.1    Lecuit, T.2
  • 69
    • 0033605738 scopus 로고    scopus 로고
    • Inhibition of myosin light chain kinase by p21-activated kinase
    • Sanders, L. C., Matsumura, F., Bokoch, G. M. & de Lanerolle, P. Inhibition of myosin light chain kinase by p21-activated kinase. Science 283, 2083-2085 (1999).
    • (1999) Science , vol.283 , pp. 2083-2085
    • Sanders, L.C.1    Matsumura, F.2    Bokoch, G.M.3    De Lanerolle, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.