메뉴 건너뛰기




Volumn 191, Issue 1, 2010, Pages 169-185

LIM kinases are required for invasive path generation by tumor and tumor-associated stromal cells

Author keywords

[No Author keywords available]

Indexed keywords

COFILIN; COLLAGEN; F ACTIN; LIM KINASE; LIM KINASE 1; LIM KINASE 2; MATRIX PROTEIN; SERUM RESPONSE FACTOR; UNCLASSIFIED DRUG; ACTIN; ACTIN DEPOLYMERIZING FACTOR;

EID: 77957732541     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.201002041     Document Type: Article
Times cited : (148)

References (62)
  • 1
    • 33645507413 scopus 로고    scopus 로고
    • Dynamic interactions of cortactin and membrane type 1 matrix metalloproteinase at invadopodia: Defining the stages of invadopodia formation and function
    • doi:10.1158/0008-5472.CAN-05-2177
    • Artym, V.V., Y. Zhang, F. Seillier-Moiseiwitsch, K.M. Yamada, and S.C. Mueller. 2006. Dynamic interactions of cortactin and membrane type 1 matrix metalloproteinase at invadopodia: defining the stages of invadopodia formation and function. Cancer Res. 66:3034-3043. doi:10.1158/0008-5472.CAN-05-2177
    • (2006) Cancer Res. , vol.66 , pp. 3034-3043
    • Artym, V.V.1    Zhang, Y.2    Seillier-Moiseiwitsch, F.3    Yamada, K.M.4    Mueller, S.C.5
  • 2
    • 33646376457 scopus 로고    scopus 로고
    • LIM kinase 1 increases tumor metastasis of human breast cancer cells via regulation of the urokinase-type plasminogen activator system
    • DOI 10.1002/ijc.21650
    • Bagheri-Yarmand, R., A. Mazumdar, A.A. Sahin, and R. Kumar. 2006. LIM kinase 1 increases tumor metastasis of human breast cancer cells via regulation of the urokinase-type plasminogen activator system. Int. J. Cancer. 118:2703-2710. doi:10.1002/ijc.21650 (Pubitemid 43673347)
    • (2006) International Journal of Cancer , vol.118 , Issue.11 , pp. 2703-2710
    • Bagheri-Yarmand, R.1    Mazumdar, A.2    Sahin, A.A.3    Kumar, R.4
  • 3
    • 9944251987 scopus 로고    scopus 로고
    • Rho GTPases in human cancer: An unresolved link to upstream and downstream transcriptional regulation
    • Benitah, S.A., P.F. Valerón, L. van Aelst, C.J. Marshall, and J.C. Lacal. 2004. Rho GTPases in human cancer: an unresolved link to upstream and downstream transcriptional regulation. Biochim. Biophys. Acta. 1705:121-132.
    • (2004) Biochim. Biophys. Acta , vol.1705 , pp. 121-132
    • Benitah, S.A.1    Valerón, P.F.2    Van Aelst, L.3    Marshall, C.J.4    Lacal, J.C.5
  • 4
    • 68549107801 scopus 로고    scopus 로고
    • Invadopodia: Specialized tumor cell structures for the focal degradation of the extracellular matrix
    • doi:10.1007/s10555-008-9176-1
    • Buccione, R., G. Caldieri, and I. Ayala. 2009. Invadopodia: specialized tumor cell structures for the focal degradation of the extracellular matrix. Cancer Metastasis Rev. 28:137-149. doi:10.1007/s10555-008-9176-1
    • (2009) Cancer Metastasis Rev. , vol.28 , pp. 137-149
    • Buccione, R.1    Caldieri, G.2    Ayala, I.3
  • 5
    • 0026045382 scopus 로고
    • Kinetic analysis of F-actin depolymerization in polymorphonuclear leukocyte lysates indicates that chemoattractant stimulation increases actin filament number without altering the filament length distribution
    • doi:10.1083/jcb.115.3.677
    • Cano, M.L., D.A. Lauffenburger, and S.H. Zigmond. 1991. Kinetic analysis of F-actin depolymerization in polymorphonuclear leukocyte lysates indicates that chemoattractant stimulation increases actin filament number without altering the filament length distribution. J. Cell Biol. 115:677-687. doi:10.1083/jcb.115.3.677
    • (1991) J. Cell Biol. , vol.115 , pp. 677-687
    • Cano, M.L.1    Lauffenburger, D.A.2    Zigmond, S.H.3
  • 6
    • 0035072953 scopus 로고    scopus 로고
    • Membrane blebbing during apoptosis results from caspase-mediated activation of ROCK I
    • doi:10.1038/35070009
    • Coleman, M.L., E.A. Sahai, M. Yeo, M. Bosch, A. Dewar, and M.F. Olson. 2001. Membrane blebbing during apoptosis results from caspase-mediated activation of ROCK I. Nat. Cell Biol. 3:339-345. doi:10.1038/35070009
    • (2001) Nat. Cell Biol. , vol.3 , pp. 339-345
    • Coleman, M.L.1    Sahai, E.A.2    Yeo, M.3    Bosch, M.4    Dewar, A.5    Olson, M.F.6
  • 7
    • 0036854328 scopus 로고    scopus 로고
    • The diaphanous-related formin mDia1 controls serum response factor activity through its effects on actin polymerization
    • doi:10.1091/mbc.02-06-0092
    • Copeland, J.W., and R. Treisman. 2002. The diaphanous-related formin mDia1 controls serum response factor activity through its effects on actin polymerization. Mol. Biol. Cell. 13:4088-4099. doi:10.1091/mbc.02-06-0092
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4088-4099
    • Copeland, J.W.1    Treisman, R.2
  • 8
    • 0035941075 scopus 로고    scopus 로고
    • Taking cell-matrix adhesions to the third dimension
    • DOI 10.1126/science.1064829
    • Cukierman, E., R. Pankov, D.R. Stevens, and K.M. Yamada. 2001. Taking cell-matrix adhesions to the third dimension. Science. 294:1708-1712. doi:10.1126/science.1064829 (Pubitemid 33104840)
    • (2001) Science , vol.294 , Issue.5547 , pp. 1708-1712
    • Cukierman, E.1    Pankov, R.2    Stevens, D.R.3    Yamada, K.M.4
  • 9
    • 0141480275 scopus 로고    scopus 로고
    • LIM kinase 1 is essential for the invasive growth of prostate epithelial cells: Implications in prostate cancer
    • doi:10.1074/jbc.M306196200
    • Davila, M., A.R. Frost, W.E. Grizzle, and R. Chakrabarti. 2003. LIM kinase 1 is essential for the invasive growth of prostate epithelial cells: implications in prostate cancer. J. Biol. Chem. 278:36868-36875. doi:10.1074/jbc.M306196200
    • (2003) J. Biol. Chem. , vol.278 , pp. 36868-36875
    • Davila, M.1    Frost, A.R.2    Grizzle, W.E.3    Chakrabarti, R.4
  • 10
    • 0032529241 scopus 로고    scopus 로고
    • Remodeling of collagen matrix by human tumor cells requires activation and cell surface association of matrix metalloproteinase-2
    • Deryugina, E.I., M.A. Bourdon, R.A. Reisfeld, and A. Strongin. 1998. Remodeling of collagen matrix by human tumor cells requires activation and cell surface association of matrix metalloproteinase-2. Cancer Res. 58:3743-3750.
    • (1998) Cancer Res. , vol.58 , pp. 3743-3750
    • Deryugina, E.I.1    Bourdon, M.A.2    Reisfeld, R.A.3    Strongin, A.4
  • 11
    • 44349130374 scopus 로고    scopus 로고
    • Nischarin inhibits LIM kinase to regulate cofilin phosphorylation and cell invasion
    • DOI 10.1128/MCB.01832-07
    • Ding, Y., T. Milosavljevic, and S.K. Alahari. 2008. Nischarin inhibits LIM kinase to regulate cofilin phosphorylation and cell invasion. Mol. Cell. Biol. 28:3742-3756. doi:10.1128/MCB.01832-07 (Pubitemid 351732909)
    • (2008) Molecular and Cellular Biology , vol.28 , Issue.11 , pp. 3742-3756
    • Ding, Y.1    Milosavljevic, T.2    Alahari, S.K.3
  • 12
    • 61449181308 scopus 로고    scopus 로고
    • One-dimensional topography underlies three-dimensional fibrillar cell migration
    • doi:10.1083/jcb.200810041
    • Doyle, A.D., F.W. Wang, K. Matsumoto, and K.M. Yamada. 2009. One-dimensional topography underlies three-dimensional fibrillar cell migration. J. Cell Biol. 184:481-490. doi:10.1083/jcb.200810041
    • (2009) J. Cell Biol. , vol.184 , pp. 481-490
    • Doyle, A.D.1    Wang, F.W.2    Matsumoto, K.3    Yamada, K.M.4
  • 13
    • 54749146365 scopus 로고    scopus 로고
    • Tube travel: The role of proteases in individual and collective cancer cell invasion
    • doi:10.1158/0008-5472.CAN-08-0784
    • Friedl, P., and K. Wolf. 2008. Tube travel: the role of proteases in individual and collective cancer cell invasion. Cancer Res. 68:7247-7249. doi:10.1158/0008-5472.CAN-08-0784
    • (2008) Cancer Res. , vol.68 , pp. 7247-7249
    • Friedl, P.1    Wolf, K.2
  • 14
    • 66749098416 scopus 로고    scopus 로고
    • Collective invasion of carcinoma cells: When the fibroblasts take the lead
    • doi:10.4161/cam.2.1.5705
    • Gaggioli, C. 2008. Collective invasion of carcinoma cells: when the fibroblasts take the lead. Cell Adh Migr. 2:45-47. doi:10.4161/cam.2.1.5705
    • (2008) Cell Adh Migr. , vol.2 , pp. 45-47
    • Gaggioli, C.1
  • 15
    • 36749013537 scopus 로고    scopus 로고
    • Fibroblast-led collective invasion of carcinoma cells with differing roles for RhoGTPases in leading and following cells
    • DOI 10.1038/ncb1658, PII NCB1658
    • Gaggioli, C., S. Hooper, C. Hidalgo-Carcedo, R. Grosse, J.F. Marshall, K. Harrington, and E. Sahai. 2007. Fibroblast-led collective invasion of carcinoma cells with differing roles for RhoGTPases in leading and following cells. Nat. Cell Biol. 9:1392-1400. doi:10.1038/ncb1658 (Pubitemid 350201752)
    • (2007) Nature Cell Biology , vol.9 , Issue.12 , pp. 1392-1400
    • Gaggioli, C.1    Hooper, S.2    Hidalgo-Carcedo, C.3    Grosse, R.4    Marshall, J.F.5    Harrington, K.6    Sahai, E.7
  • 16
    • 0037182585 scopus 로고    scopus 로고
    • LIM kinase and diaphanous cooperate to regulate serum response factor and actin dynamics
    • DOI 10.1083/jcb.200203126
    • Geneste, O., J.W. Copeland, and R. Treisman. 2002. LIM kinase and Diaphanous cooperate to regulate serum response factor and actin dynamics. J. Cell Biol. 157:831-838. doi:10.1083/jcb.200203126 (Pubitemid 34847820)
    • (2002) Journal of Cell Biology , vol.157 , Issue.5 , pp. 831-838
    • Geneste, O.1    Copeland, J.W.2    Treisman, R.3
  • 17
    • 68549126922 scopus 로고    scopus 로고
    • The cytoskeleton and cancer
    • doi:10.1007/s10555-008-9166-3
    • Hall, A. 2009. The cytoskeleton and cancer. Cancer Metastasis Rev. 28:5-14. doi:10.1007/s10555-008-9166-3
    • (2009) Cancer Metastasis Rev. , vol.28 , pp. 5-14
    • Hall, A.1
  • 18
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • doi:10.1016/S0092-8674(00)81683-9
    • Hanahan, D., and R.A. Weinberg. 2000. The hallmarks of cancer. Cell. 100:57-70. doi:10.1016/S0092-8674(00)81683-9
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 19
    • 0027439319 scopus 로고
    • Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments
    • doi:10.1021/bi00089a014
    • Hawkins, M., B. Pope, S.K. Maciver, and A.G. Weeds. 1993. Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments. Biochemistry. 32:9985-9993. doi:10.1021/bi00089a014
    • (1993) Biochemistry , vol.32 , pp. 9985-9993
    • Hawkins, M.1    Pope, B.2    Maciver, S.K.3    Weeds, A.G.4
  • 20
    • 0027996872 scopus 로고
    • Fos-transformation activates genes associated with invasion
    • Hennigan, R.F., K.L. Hawker, and B.W. Ozanne. 1994. Fos-transformation activates genes associated with invasion. Oncogene. 9:3591-3600.
    • (1994) Oncogene , vol.9 , pp. 3591-3600
    • Hennigan, R.F.1    Hawker, K.L.2    Ozanne, B.W.3
  • 21
    • 0035863391 scopus 로고    scopus 로고
    • Synthetic protein transduction domains: Enhanced transduction potential in vitro and in vivo
    • Ho, A., S.R. Schwarze, S.J. Mermelstein, G. Waksman, and S.F. Dowdy. 2001. Synthetic protein transduction domains: enhanced transduction potential in vitro and in vivo. Cancer Res. 61:474-477. (Pubitemid 32128600)
    • (2001) Cancer Research , vol.61 , Issue.2 , pp. 474-477
    • Ho, A.1    Schwarze, S.R.2    Mermelstein, S.J.3    Waksman, G.4    Dowdy, S.F.5
  • 22
    • 75549090379 scopus 로고    scopus 로고
    • A chemical biology screen reveals a role for Rab21-mediated control of actomyosin contractility in fibroblast-driven cancer invasion
    • doi:10.1038/sj.bjc.6605469
    • Hooper, S., C. Gaggioli, and E. Sahai. 2010. A chemical biology screen reveals a role for Rab21-mediated control of actomyosin contractility in fibroblast-driven cancer invasion. Br. J. Cancer. 102:392-402. doi:10.1038/sj.bjc.6605469
    • (2010) Br. J. Cancer , vol.102 , pp. 392-402
    • Hooper, S.1    Gaggioli, C.2    Sahai, E.3
  • 23
    • 44449120976 scopus 로고    scopus 로고
    • Suppression of the invasive capacity of rat ascites hepatoma cells by knockdown of Slingshot or LIM kinase
    • doi:10.1074/jbc.M706538200
    • Horita, Y., K. Ohashi, M. Mukai, M. Inoue, and K. Mizuno. 2008. Suppression of the invasive capacity of rat ascites hepatoma cells by knockdown of Slingshot or LIM kinase. J. Biol. Chem. 283:6013-6021. doi:10.1074/jbc. M706538200
    • (2008) J. Biol. Chem. , vol.283 , pp. 6013-6021
    • Horita, Y.1    Ohashi, K.2    Mukai, M.3    Inoue, M.4    Mizuno, K.5
  • 24
    • 3242772983 scopus 로고    scopus 로고
    • MT1-MMP: An enzyme with multidimensional regulation
    • doi:10.1016/j.tibs.2004.04.001
    • Itoh, Y., and M. Seiki. 2004. MT1-MMP: an enzyme with multidimensional regulation. Trends Biochem. Sci. 29:285-289. doi:10.1016/j.tibs.2004.04.001
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 285-289
    • Itoh, Y.1    Seiki, M.2
  • 25
    • 23744449992 scopus 로고    scopus 로고
    • Matrigel: Basement membrane matrix with biological activity
    • DOI 10.1016/j.semcancer.2005.05.004, PII S1044579X05000313
    • Kleinman, H.K., and G.R. Martin. 2005. Matrigel: basement membrane matrix with biological activity. Semin. Cancer Biol. 15:378-386. doi:10.1016/j. semcancer.2005.05.004 (Pubitemid 41140305)
    • (2005) Seminars in Cancer Biology , vol.15 , Issue.5 SPEC. ISSUE , pp. 378-386
    • Kleinman, H.K.1    Martin, G.R.2
  • 26
    • 33644508365 scopus 로고    scopus 로고
    • MAPKAPK-2-mediated LIM-kinase activation is critical for VEGF-induced actin remodeling and cell migration
    • DOI 10.1038/sj.emboj.7600973, PII 7600973
    • Kobayashi, M., M. Nishita, T. Mishima, K. Ohashi, and K. Mizuno. 2006. MAPKAPK-2-mediated LIM-kinase activation is critical for VEGF-induced actin remodeling and cell migration. EMBO J. 25:713-726. doi:10.1038/sj.emboj.7600973 (Pubitemid 43292434)
    • (2006) EMBO Journal , vol.25 , Issue.4 , pp. 713-726
    • Kobayashi, M.1    Nishita, M.2    Mishima, T.3    Ohashi, K.4    Mizuno, K.5
  • 27
    • 35348905119 scopus 로고    scopus 로고
    • RNAi-mediated downregulation of urokinase plasminogen activator receptor and matrix metalloprotease-9 in human breast cancer cells results in decreased tumor invasion, angiogenesis and growth
    • doi:10.1002/ijc.22962
    • Kunigal, S., S.S. Lakka, C.S. Gondi, N. Estes, and J.S. Rao. 2007. RNAi-mediated downregulation of urokinase plasminogen activator receptor and matrix metalloprotease-9 in human breast cancer cells results in decreased tumor invasion, angiogenesis and growth. Int. J. Cancer. 121:2307-2316. doi:10.1002/ijc.22962
    • (2007) Int. J. Cancer , vol.121 , pp. 2307-2316
    • Kunigal, S.1    Lakka, S.S.2    Gondi, C.S.3    Estes, N.4    Rao, J.S.5
  • 28
    • 77049108859 scopus 로고    scopus 로고
    • The actin-bundling protein fascin stabilizes actin in invadopodia and potentiates protrusive invasion
    • doi:10.1016/j.cub.2009.12.035
    • Li, A., J.C. Dawson, M. Forero-Vargas, H.J. Spence, X. Yu, I. König, K. Anderson, and L.M. Machesky. 2010. The actin-bundling protein fascin stabilizes actin in invadopodia and potentiates protrusive invasion. Curr. Biol. 20:339-345. doi:10.1016/j.cub.2009.12.035
    • (2010) Curr. Biol. , vol.20 , pp. 339-345
    • Li, A.1    Dawson, J.C.2    Forero-Vargas, M.3    Spence, H.J.4    Yu, X.5    König, I.6    Anderson, K.7    Machesky, L.M.8
  • 29
    • 0030842253 scopus 로고    scopus 로고
    • Upregulation of MMP-9 expression in MDA-MB231 tumor cells by platelet granular membrane
    • doi:10.1016/S0014-5793(97)01336-7
    • Lindenmeyer, F., Y. Legrand, and S. Menashi. 1997. Upregulation of MMP-9 expression in MDA-MB231 tumor cells by platelet granular membrane. FEBS Lett. 418:19-22. doi:10.1016/S0014-5793(97)01336-7
    • (1997) FEBS Lett. , vol.418 , pp. 19-22
    • Lindenmeyer, F.1    Legrand, Y.2    Menashi, S.3
  • 30
    • 33847343034 scopus 로고    scopus 로고
    • The matrix corroded: Podosomes and invadopodia in extracellular matrix degradation
    • doi:10.1016/j.tcb.2007.01.002
    • Linder, S. 2007. The matrix corroded: podosomes and invadopodia in extracellular matrix degradation. Trends Cell Biol. 17:107-117. doi:10.1016/j.tcb.2007.01.002
    • (2007) Trends Cell Biol. , vol.17 , pp. 107-117
    • Linder, S.1
  • 31
    • 66149139847 scopus 로고    scopus 로고
    • Diaphanous-related formins are required for invadopodia formation and invasion of breast tumor cells
    • doi:10.1158/0008-5472.CAN-08-3709
    • Lizárraga, F., R. Poincloux, M. Romao, G. Montagnac, G. Le Dez, I. Bonne, G. Rigaill, G. Raposo, and P. Chavrier. 2009. Diaphanous-related formins are required for invadopodia formation and invasion of breast tumor cells. Cancer Res. 69:2792-2800. doi:10.1158/0008-5472.CAN-08-3709
    • (2009) Cancer Res. , vol.69 , pp. 2792-2800
    • Lizárraga, F.1    Poincloux, R.2    Romao, M.3    Montagnac, G.4    Le Dez, G.5    Bonne, I.6    Rigaill, G.7    Raposo, G.8    Chavrier, P.9
  • 32
    • 76749126470 scopus 로고    scopus 로고
    • 2010. LIM-kinase is critical for the mesenchymal-to-amoeboid cell morphological transition in 3D matrices
    • doi:10.1016/j.bbrc.2010.01.075
    • Mishima, T., M. Naotsuka, Y. Horita, M. Sato, K. Ohashi, and K. Mizuno. 2010. LIM-kinase is critical for the mesenchymal-to-amoeboid cell morphological transition in 3D matrices. Biochem. Biophys. Res. Commun. 392:577-581. doi:10.1016/j.bbrc.2010.01.075
    • Biochem. Biophys. Res. Commun. , vol.392 , pp. 577-581
    • Mishima, T.1    Naotsuka, M.2    Horita, Y.3    Sato, M.4    Ohashi, K.5    Mizuno, K.6
  • 33
    • 27544502276 scopus 로고    scopus 로고
    • Spatial and temporal regulation of cofilin activity by LIM kinase and Slingshot is critical for directional cell migration
    • doi:10.1083/jcb.200504029
    • Nishita, M., C. Tomizawa, M. Yamamoto, Y. Horita, K. Ohashi, and K. Mizuno. 2005. Spatial and temporal regulation of cofilin activity by LIM kinase and Slingshot is critical for directional cell migration. J. Cell Biol. 171:349-359. doi:10.1083/jcb.200504029
    • (2005) J. Cell Biol. , vol.171 , pp. 349-359
    • Nishita, M.1    Tomizawa, C.2    Yamamoto, M.3    Horita, Y.4    Ohashi, K.5    Mizuno, K.6
  • 34
    • 18644374224 scopus 로고    scopus 로고
    • Seven novel and stable translocations associated with oncogenic gene expression in malignant melanoma
    • doi:10.1593/neo.04514
    • Okamoto, I., C. Pirker, M. Bilban, W. Berger, D. Losert, C. Marosi, O.A. Haas, K. Wolff, and H. Pehamberger. 2005. Seven novel and stable translocations associated with oncogenic gene expression in malignant melanoma. Neoplasia. 7:303-311. doi:10.1593/neo.04514
    • (2005) Neoplasia , vol.7 , pp. 303-311
    • Okamoto, I.1    Pirker, C.2    Bilban, M.3    Berger, W.4    Losert, D.5    Marosi, C.6    Haas, O.A.7    Wolff, K.8    Pehamberger, H.9
  • 35
    • 41749091574 scopus 로고    scopus 로고
    • Applications for ROCK kinase inhibition
    • doi:10.1016/j.ceb.2008.01.002
    • Olson, M.F. 2008. Applications for ROCK kinase inhibition. Curr. Opin. Cell Biol. 20:242-248. doi:10.1016/j.ceb.2008.01.002
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 242-248
    • Olson, M.F.1
  • 36
    • 62449294770 scopus 로고    scopus 로고
    • The actin cytoskeleton in cancer cell motility
    • doi:10.1007/s10585-008-9174-2
    • Olson, M.F., and E. Sahai. 2009. The actin cytoskeleton in cancer cell motility. Clin. Exp. Metastasis. 26:273-287. doi:10.1007/s10585-008-9174-2
    • (2009) Clin. Exp. Metastasis , vol.26 , pp. 273-287
    • Olson, M.F.1    Sahai, E.2
  • 37
    • 71749095987 scopus 로고    scopus 로고
    • The cofilin activity cycle in lamellipodia and invadopodia
    • doi:10.1002/jcb.22372
    • Oser, M., and J. Condeelis. 2009. The cofilin activity cycle in lamellipodia and invadopodia. J. Cell. Biochem. 108:1252-1262. doi:10.1002/jcb.22372
    • (2009) J. Cell. Biochem. , vol.108 , pp. 1252-1262
    • Oser, M.1    Condeelis, J.2
  • 39
    • 70350417461 scopus 로고    scopus 로고
    • Matrix invasion by tumour cells: A focus on MT1-MMP trafficking to invadopodia
    • doi:10.1242/jcs.034561
    • Poincloux, R., F. Lizárraga, and P. Chavrier. 2009. Matrix invasion by tumour cells: a focus on MT1-MMP trafficking to invadopodia. J. Cell Sci. 122:3015-3024. doi:10.1242/jcs.034561
    • (2009) J. Cell Sci. , vol.122 , pp. 3015-3024
    • Poincloux, R.1    Lizárraga, F.2    Chavrier, P.3
  • 40
    • 0038024241 scopus 로고    scopus 로고
    • Rocks: Multifunctional kinases in cell behaviour
    • doi:10.1038/nrm1128
    • Riento, K., and A.J. Ridley. 2003. Rocks: multifunctional kinases in cell behaviour. Nat. Rev. Mol. Cell Biol. 4:446-456. doi:10.1038/nrm1128
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 446-456
    • Riento, K.1    Ridley, A.J.2
  • 42
    • 12344252751 scopus 로고    scopus 로고
    • Mechanisms of cancer cell invasion
    • doi:10.1016/j.gde.2004.12.002
    • Sahai, E. 2005. Mechanisms of cancer cell invasion. Curr. Opin. Genet. Dev. 15:87-96. doi:10.1016/j.gde.2004.12.002
    • (2005) Curr. Opin. Genet. Dev. , vol.15 , pp. 87-96
    • Sahai, E.1
  • 43
    • 0036488510 scopus 로고    scopus 로고
    • RHO-GTPases and cancer
    • doi:10.1038/nrc725
    • Sahai, E., and C.J. Marshall. 2002. RHO-GTPases and cancer. Nat. Rev. Cancer. 2:133-142. doi:10.1038/nrc725
    • (2002) Nat. Rev. Cancer. , vol.2 , pp. 133-142
    • Sahai, E.1    Marshall, C.J.2
  • 44
    • 0035865137 scopus 로고    scopus 로고
    • Cross-talk between Ras and Rho signalling pathways in transformation favours proliferation and increased motility
    • doi:10.1093/emboj/20.4.755
    • Sahai, E., M.F. Olson, and C.J. Marshall. 2001. Cross-talk between Ras and Rho signalling pathways in transformation favours proliferation and increased motility. EMBO J. 20:755-766. doi:10.1093/emboj/20.4.755
    • (2001) EMBO J. , vol.20 , pp. 755-766
    • Sahai, E.1    Olson, M.F.2    Marshall, C.J.3
  • 45
    • 62849099048 scopus 로고    scopus 로고
    • Circulating tumour cells as prognostic markers in progressive, castration-resistant prostate cancer: A reanalysis of IMMC38 trial data
    • doi:10.1016/S1470-2045(08)70340-1
    • Scher, H.I., X. Jia, J.S. de Bono, M. Fleisher, K.J. Pienta, D. Raghavan, and G. Heller. 2009. Circulating tumour cells as prognostic markers in progressive, castration-resistant prostate cancer: a reanalysis of IMMC38 trial data. Lancet Oncol. 10:233-239. doi:10.1016/S1470-2045(08)70340-1
    • (2009) Lancet Oncol. , vol.10 , pp. 233-239
    • Scher, H.I.1    Jia, X.2    De Bono, J.S.3    Fleisher, M.4    Pienta, K.J.5    Raghavan, D.6    Heller, G.7
  • 46
    • 77951771838 scopus 로고    scopus 로고
    • Actin, microtubules, and vimentin intermediate filaments cooperate for elongation of invadopodia
    • doi:10.1083/jcb.200909113
    • Schoumacher, M., R.D. Goldman, D. Louvard, and D.M. Vignjevic. 2010. Actin, microtubules, and vimentin intermediate filaments cooperate for elongation of invadopodia. J. Cell Biol. 189:541-556. doi:10.1083/jcb.200909113
    • (2010) J. Cell Biol. , vol.189 , pp. 541-556
    • Schoumacher, M.1    Goldman, R.D.2    Louvard, D.3    Vignjevic, D.M.4
  • 47
    • 34249887660 scopus 로고    scopus 로고
    • LIM kinases: Function, regulation and association with human disease
    • doi:10.1007/s00109-007-0165-6
    • Scott, R.W., and M.F. Olson. 2007. LIM kinases: function, regulation and association with human disease. J. Mol. Med. 85:555-568. doi:10.1007/s00109-007- 0165-6
    • (2007) J. Mol. Med. , vol.85 , pp. 555-568
    • Scott, R.W.1    Olson, M.F.2
  • 48
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosintroponin complex with actin and the proteolytic fragments of myosin
    • Spudich, J.A., and S. Watt. 1971. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosintroponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem. 246:4866-4871.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 49
    • 44249097734 scopus 로고    scopus 로고
    • Invadopodia: At the cutting edge of tumour invasion
    • doi:10.1016/j.jocn.2008.03.003
    • Stylli, S.S., A.H. Kaye, and P. Lock. 2008. Invadopodia: at the cutting edge of tumour invasion. J. Clin. Neurosci. 15:725-737. doi:10.1016/j.jocn.2008. 03.003
    • (2008) J. Clin. Neurosci. , vol.15 , pp. 725-737
    • Stylli, S.S.1    Kaye, A.H.2    Lock, P.3
  • 50
    • 65249141705 scopus 로고    scopus 로고
    • A common cofilin activity cycle in invasive tumor cells and inflammatory cells
    • doi:10.1242/jcs.031146
    • van Rheenen, J., J. Condeelis, and M. Glogauer. 2009. A common cofilin activity cycle in invasive tumor cells and inflammatory cells. J. Cell Sci. 122:305-311. doi:10.1242/jcs.031146
    • (2009) J. Cell Sci. , vol.122 , pp. 305-311
    • Van Rheenen, J.1    Condeelis, J.2    Glogauer, M.3
  • 52
    • 44449178868 scopus 로고    scopus 로고
    • Rho GTPases in cancer cell biology
    • doi:10.1016/j.febslet.2008.04.039
    • Vega, F.M., and A.J. Ridley. 2008. Rho GTPases in cancer cell biology. FEBS Lett. 582:2093-2101. doi:10.1016/j.febslet.2008.04.039
    • (2008) FEBS Lett. , vol.582 , pp. 2093-2101
    • Vega, F.M.1    Ridley, A.J.2
  • 53
    • 74049146689 scopus 로고    scopus 로고
    • LIMK1 and LIMK2 are important for metastatic behavior and tumor cell-induced angiogenesis of pancreatic cancer cells
    • doi:10.1089/zeb.2009.0602
    • Vlecken, D.H., and C.P. Bagowski. 2009. LIMK1 and LIMK2 are important for metastatic behavior and tumor cell-induced angiogenesis of pancreatic cancer cells. Zebrafish. 6:433-439. doi:10.1089/zeb.2009.0602
    • (2009) Zebrafish , vol.6 , pp. 433-439
    • Vlecken, D.H.1    Bagowski, C.P.2
  • 54
    • 12344264745 scopus 로고    scopus 로고
    • Targeting Ras and Rho GTPases as opportunities for cancer therapeutics
    • doi:10.1016/j.gde.2004.11.001
    • Walker, K., and M.F. Olson. 2005. Targeting Ras and Rho GTPases as opportunities for cancer therapeutics. Curr. Opin. Genet. Dev. 15:62-68. doi:10.1016/j.gde.2004.11.001
    • (2005) Curr. Opin. Genet. Dev. , vol.15 , pp. 62-68
    • Walker, K.1    Olson, M.F.2
  • 55
    • 9244222742 scopus 로고    scopus 로고
    • Identification and testing of a gene expression signature of invasive carcinoma cells within primary mammary tumors
    • doi:10.1158/0008-5472.CAN-04-1136
    • Wang, W., S. Goswami, K. Lapidus, A.L. Wells, J.B. Wyckoff, E. Sahai, R.H. Singer, J.E. Segall, and J.S. Condeelis. 2004. Identification and testing of a gene expression signature of invasive carcinoma cells within primary mammary tumors. Cancer Res. 64:8585-8594. doi:10.1158/0008-5472.CAN-04-1136
    • (2004) Cancer Res. , vol.64 , pp. 8585-8594
    • Wang, W.1    Goswami, S.2    Lapidus, K.3    Wells, A.L.4    Wyckoff, J.B.5    Sahai, E.6    Singer, R.H.7    Segall, J.E.8    Condeelis, J.S.9
  • 56
    • 33646386905 scopus 로고    scopus 로고
    • The activity status of cofilin is directly related to invasion, intravasation, and metastasis of mammary tumors
    • doi:10.1083/jcb.200510115
    • Wang, W., G. Mouneimne, M. Sidani, J. Wyckoff, X. Chen, A. Makris, S. Goswami, A.R. Bresnick, and J.S. Condeelis. 2006. The activity status of cofilin is directly related to invasion, intravasation, and metastasis of mammary tumors. J. Cell Biol. 173:395-404. doi:10.1083/jcb.200510115
    • (2006) J. Cell Biol. , vol.173 , pp. 395-404
    • Wang, W.1    Mouneimne, G.2    Sidani, M.3    Wyckoff, J.4    Chen, X.5    Makris, A.6    Goswami, S.7    Bresnick, A.R.8    Condeelis, J.S.9
  • 57
    • 34547569807 scopus 로고    scopus 로고
    • Multi-step pericellular proteolysis controls the transition from individual to collective cancer cell invasion
    • doi:10.1038/ncb1616
    • Wolf, K., Y.I. Wu, Y. Liu, J. Geiger, E. Tam, C. Overall, M.S. Stack, and P. Friedl. 2007. Multi-step pericellular proteolysis controls the transition from individual to collective cancer cell invasion. Nat. Cell Biol. 9:893-904. doi:10.1038/ncb1616
    • (2007) Nat. Cell Biol. , vol.9 , pp. 893-904
    • Wolf, K.1    Wu, Y.I.2    Liu, Y.3    Geiger, J.4    Tam, E.5    Overall, C.6    Stack, M.S.7    Friedl, P.8
  • 58
    • 33746562929 scopus 로고    scopus 로고
    • ROCK- and myosin-dependent matrix deformation enables protease-independent tumor-cell invasion in vivo
    • doi:10.1016/j.cub.2006.05.065
    • Wyckoff, J.B., S.E. Pinner, S. Gschmeissner, J.S. Condeelis, and E. Sahai. 2006. ROCK- and myosin-dependent matrix deformation enables protease-independent tumor-cell invasion in vivo. Curr. Biol. 16:1515-1523. doi:10.1016/j.cub.2006.05.065
    • (2006) Curr. Biol. , vol.16 , pp. 1515-1523
    • Wyckoff, J.B.1    Pinner, S.E.2    Gschmeissner, S.3    Condeelis, J.S.4    Sahai, E.5
  • 60
    • 33644935220 scopus 로고    scopus 로고
    • Invadopodia and podosomes in tumor invasion
    • doi:10.1016/j.ejcb.2005.10.004
    • Yamaguchi, H., F. Pixley, and J. Condeelis. 2006. Invadopodia and podosomes in tumor invasion. Eur. J. Cell Biol. 85:213-218. doi:10.1016/j.ejcb. 2005.10.004
    • (2006) Eur. J. Cell Biol. , vol.85 , pp. 213-218
    • Yamaguchi, H.1    Pixley, F.2    Condeelis, J.3
  • 61
    • 0038132257 scopus 로고    scopus 로고
    • A role for LIM kinase in cancer invasion
    • doi:10.1073/pnas.1232344100
    • Yoshioka, K., V. Foletta, O. Bernard, and K. Itoh. 2003. A role for LIM kinase in cancer invasion. Proc. Natl. Acad. Sci. USA. 100:7247-7252. doi:10.1073/pnas.1232344100
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 7247-7252
    • Yoshioka, K.1    Foletta, V.2    Bernard, O.3    Itoh, K.4
  • 62
    • 0034722329 scopus 로고    scopus 로고
    • Phosphorylation of ADF/cofilin abolishes EGF-induced actin nucleation at the leading edge and subsequent lamellipod extension
    • doi:10.1083/jcb.151.5.1119
    • Zebda, N., O. Bernard, M. Bailly, S. Welti, D.S. Lawrence, and J.S. Condeelis. 2000. Phosphorylation of ADF/cofilin abolishes EGF-induced actin nucleation at the leading edge and subsequent lamellipod extension. J. Cell Biol. 151:1119-1128. doi:10.1083/jcb.151.5.1119
    • (2000) J. Cell Biol. , vol.151 , pp. 1119-1128
    • Zebda, N.1    Bernard, O.2    Bailly, M.3    Welti, S.4    Lawrence, D.S.5    Condeelis, J.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.