메뉴 건너뛰기




Volumn 16, Issue 7, 2005, Pages 3117-3127

Protein kinase A gating of a pseudopodial-located RhoA/ROCK/p38/NHE1 signal module regulates invasion in breast cancer cell lines

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP DEPENDENT PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; PHOSPHOPROTEIN; RHO ASSOCIATED COILED COIL CONTAINING PROTEIN KINASE; RHO KINASE; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; SODIUM PROTON EXCHANGE PROTEIN 1; UNCLASSIFIED DRUG;

EID: 21844438240     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E04-10-0945     Document Type: Article
Times cited : (98)

References (60)
  • 2
    • 3042692979 scopus 로고    scopus 로고
    • + exchanger (NHE1) creates acidic microenvironments leading to hyaluronidase-2 and cathepsin B activation and breast tumor cell invasion
    • + exchanger (NHE1) creates acidic microenvironments leading to hyaluronidase-2 and cathepsin B activation and breast tumor cell invasion. J. Biol. Chem. 279, 26991-27007.
    • (2004) J. Biol. Chem. , vol.279 , pp. 26991-27007
    • Bourguignon, L.Y.W.1    Singleton, P.A.2    Diedrich, P.3    Stern, R.4    Gilad, E.5
  • 4
    • 0018236173 scopus 로고
    • Long term human breast carcinoma cell lines of metastatic origin: Preliminary characterization
    • Cailleau, R., Olivé, M., and Cruciger, Q.V.J. (1978). Long term human breast carcinoma cell lines of metastatic origin: preliminary characterization. In Vitro 14, 911-915.
    • (1978) In Vitro , vol.14 , pp. 911-915
    • Cailleau, R.1    Olivé, M.2    Cruciger, Q.V.J.3
  • 5
    • 0035977205 scopus 로고    scopus 로고
    • Cell adhesion in tumor invasion and metastasis: Loss of the glue is not enough
    • Cavallaro, U., and Christofori, G. (2001). Cell adhesion in tumor invasion and metastasis: loss of the glue is not enough. Biochim. Biophys. Acta 1552, 39-45.
    • (2001) Biochim. Biophys. Acta , vol.1552 , pp. 39-45
    • Cavallaro, U.1    Christofori, G.2
  • 7
    • 0034503095 scopus 로고    scopus 로고
    • Direct binding of the Na-H exchanger NHE1 to ERM proteins regulates the cortical cytoskeleton and cell shape independently of H(+) translocation
    • Denker, S. P., Huang, D. C., Orlowski, J., Furthmayr, H., and Barber, D. L. (2000). Direct binding of the Na-H exchanger NHE1 to ERM proteins regulates the cortical cytoskeleton and cell shape independently of H(+) translocation. Mol. Cell 6, 1425-1436.
    • (2000) Mol. Cell , vol.6 , pp. 1425-1436
    • Denker, S.P.1    Huang, D.C.2    Orlowski, J.3    Furthmayr, H.4    Barber, D.L.5
  • 8
    • 5444248307 scopus 로고    scopus 로고
    • Tenascin-C and SF/HGF produced by myofibroblasts in vitro provide convergent pro-invasive signals to human colon cancer cells through RhoA and Rac
    • De Wever, O., Nguyen, Q. D., Van Hoorde, L., Bracke, M., Bruyneel, E., Gespach, C., and Mareel, M. (2004). Tenascin-C and SF/HGF produced by myofibroblasts in vitro provide convergent pro-invasive signals to human colon cancer cells through RhoA and Rac. FASEB J. 18, 1016-1018.
    • (2004) FASEB J. , vol.18 , pp. 1016-1018
    • De Wever, O.1    Nguyen, Q.D.2    Van Hoorde, L.3    Bracke, M.4    Bruyneel, E.5    Gespach, C.6    Mareel, M.7
  • 9
    • 0032575667 scopus 로고    scopus 로고
    • cAMP-induced morphological changes are counteracted by the activated RhoA small GTPase and the Rho kinase ROKα
    • Dong, J. M., Leung, T., Manser, E., and Lim, L. (1998). cAMP-induced morphological changes are counteracted by the activated RhoA small GTPase and the Rho kinase ROKα. J. Biol. Chem. 273, 22554-22562.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22554-22562
    • Dong, J.M.1    Leung, T.2    Manser, E.3    Lim, L.4
  • 10
    • 0037805583 scopus 로고    scopus 로고
    • Serine phosphorylation negatively regulates RhoA in vivo
    • Ellerbroek, S. M., Wennerberg, K., and Burridge, K. (2003). Serine phosphorylation negatively regulates RhoA in vivo. J. Biol. Chem. 278, 19023-19031.
    • (2003) J. Biol. Chem. , vol.278 , pp. 19023-19031
    • Ellerbroek, S.M.1    Wennerberg, K.2    Burridge, K.3
  • 11
    • 0037081858 scopus 로고    scopus 로고
    • Phosphorylation states of Cdc42 and RhoA regulate their interactions with Rho GDP dissociation inhibitor and their extraction from biological membranes
    • Forget, M. A., Desrosiers, R. R., Gingras, D., and Beliveau, R. (2002). Phosphorylation states of Cdc42 and RhoA regulate their interactions with Rho GDP dissociation inhibitor and their extraction from biological membranes. Biochem. J. 361, 243-254.
    • (2002) Biochem. J. , vol.361 , pp. 243-254
    • Forget, M.A.1    Desrosiers, R.R.2    Gingras, D.3    Beliveau, R.4
  • 12
    • 0035233633 scopus 로고    scopus 로고
    • Mathematical models of tumour invasion mediated by transformation-induced alteration of microenvironmental pH
    • Gatenby, R. A., and Gawlinski, E. T. (2001). Mathematical models of tumour invasion mediated by transformation-induced alteration of microenvironmental pH. Novartis Found. Symp. 240, 85-96.
    • (2001) Novartis Found. Symp. , vol.240 , pp. 85-96
    • Gatenby, R.A.1    Gawlinski, E.T.2
  • 13
    • 0034054067 scopus 로고    scopus 로고
    • Cell regulation. Cellular aspects of signal transduction
    • Hancock, J. F., and Moon, R. T. (2000). Cell regulation. Cellular aspects of signal transduction. Curr. Opin. Cell Biol. 12, 153-156.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 153-156
    • Hancock, J.F.1    Moon, R.T.2
  • 14
    • 0032935495 scopus 로고    scopus 로고
    • An essential part for Rho-associated kinase in the transcellular invasion of tumor cells
    • Itoh, K., Yoshioka, K., Akedo, H., Uehata, M., Ishizaki, T., and Narumiya, S. (1999). An essential part for Rho-associated kinase in the transcellular invasion of tumor cells. Nat. Med. 5, 221-225.
    • (1999) Nat. Med. , vol.5 , pp. 221-225
    • Itoh, K.1    Yoshioka, K.2    Akedo, H.3    Uehata, M.4    Ishizaki, T.5    Narumiya, S.6
  • 15
    • 20244390565 scopus 로고    scopus 로고
    • Involvement of phosphorylation of Tyr-31 and Tyr-118 of paxillin in MM1 cancer cell migration
    • Iwasaki, T., et al. (2002). Involvement of phosphorylation of Tyr-31 and Tyr-118 of paxillin in MM1 cancer cell migration. Int. J. Cancer 97, 330-335.
    • (2002) Int. J. Cancer , vol.97 , pp. 330-335
    • Iwasaki, T.1
  • 16
    • 0034625353 scopus 로고    scopus 로고
    • Accumulation of GTP-bound RhoA during cytokinesis and a critical role of ECT2 in this accumulation
    • Kimura, K., Tsuji, T., Takada, Y., Miki, T., and Narumiya, S. (2000). Accumulation of GTP-bound RhoA during cytokinesis and a critical role of ECT2 in this accumulation. J. Biol. Chem. 275, 17233-17236.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17233-17236
    • Kimura, K.1    Tsuji, T.2    Takada, Y.3    Miki, T.4    Narumiya, S.5
  • 17
    • 2942592798 scopus 로고    scopus 로고
    • Wnt-3a and Dvl induce neurite retraction by activating Rho-associated kinase
    • Kishida, S., Yamamoto, H., and Kikuchi, A. (2004). Wnt-3a and Dvl induce neurite retraction by activating Rho-associated kinase. Mol. Cell. Biol. 24, 4487-4501.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4487-4501
    • Kishida, S.1    Yamamoto, H.2    Kikuchi, A.3
  • 18
    • 0033304513 scopus 로고    scopus 로고
    • Similar and divergent patterns in the regulation of matrix metalloproteinase-1 (MMP-1) and tissue inhibitor of MMP-1 gene expression in benign and malignant human thyroid cells
    • Korem, S., Resnick, M. B., and Kraiem, Z. (1999). Similar and divergent patterns in the regulation of matrix metalloproteinase-1 (MMP-1) and tissue inhibitor of MMP-1 gene expression in benign and malignant human thyroid cells. J. Clin. Endocrinol. Metab. 84, 3322-3327.
    • (1999) J. Clin. Endocrinol. Metab. , vol.84 , pp. 3322-3327
    • Korem, S.1    Resnick, M.B.2    Kraiem, Z.3
  • 19
    • 0030961752 scopus 로고    scopus 로고
    • Rho regulates association of both the ERM family and vinculin with the plasma membrane in MDCK cells
    • Kotani, H., Takaishi, K., Sasaki, T., and Takai, Y. (1997). Rho regulates association of both the ERM family and vinculin with the plasma membrane in MDCK cells. Oncogene 14, 1705-1713.
    • (1997) Oncogene , vol.14 , pp. 1705-1713
    • Kotani, H.1    Takaishi, K.2    Sasaki, T.3    Takai, Y.4
  • 21
    • 0035066383 scopus 로고    scopus 로고
    • Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation
    • Kyriakis, J. M., and Avruch, J. (2001). Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation. Physiol. Rev. 81, 808-869.
    • (2001) Physiol. Rev. , vol.81 , pp. 808-869
    • Kyriakis, J.M.1    Avruch, J.2
  • 22
    • 0033739497 scopus 로고    scopus 로고
    • Regulation of the formation of tumor cell pseudopodia by the Na(+)/H(+) exchanger NHE1
    • Lagana, A., Vadnais, J., Le, P. U., Nguyen, T. N., Laprade, R., Nabi, I. R., and Noel, J. (2000). Regulation of the formation of tumor cell pseudopodia by the Na(+)/H(+) exchanger NHE1. J. Cell Sci. 113, 3649-3662.
    • (2000) J. Cell Sci. , vol.113 , pp. 3649-3662
    • Lagana, A.1    Vadnais, J.2    Le, P.U.3    Nguyen, T.N.4    Laprade, R.5    Nabi, I.R.6    Noel, J.7
  • 23
    • 0030040750 scopus 로고    scopus 로고
    • Protein kinase A phosphorylation of RhoA mediates the morphological and functional effects of cyclic AMP in cytotoxic lymphocytes
    • Lang, P., Gesbert, F., Delespine-Carmagnat, M., Stancou, R., Pouchelet, M., and Bertoglio, J. (1996). Protein kinase A phosphorylation of RhoA mediates the morphological and functional effects of cyclic AMP in cytotoxic lymphocytes. EMBO J. 15, 510-519.
    • (1996) EMBO J. , vol.15 , pp. 510-519
    • Lang, P.1    Gesbert, F.2    Delespine-Carmagnat, M.3    Stancou, R.4    Pouchelet, M.5    Bertoglio, J.6
  • 24
    • 0030813029 scopus 로고    scopus 로고
    • Elevation of intracellular cAMP inhibits RhoA activation and integrin-dependent leukocyte adhesion induced by chemoattractants
    • Laudanna, C., Campbell, J. J., and Butcher, E. C. (1997). Elevation of intracellular cAMP inhibits RhoA activation and integrin-dependent leukocyte adhesion induced by chemoattractants. J. Biol. Chem. 272, 24141-24144.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24141-24144
    • Laudanna, C.1    Campbell, J.J.2    Butcher, E.C.3
  • 25
    • 0034053448 scopus 로고    scopus 로고
    • The cAMP signaling pathway as a therapeutic target in lymphoid malignancies
    • Lerner, A., Kim, D. H., and Lee, R. (2000). The cAMP signaling pathway as a therapeutic target in lymphoid malignancies. Leuk. Lymphoma 37, 39-51.
    • (2000) Leuk. Lymphoma , vol.37 , pp. 39-51
    • Lerner, A.1    Kim, D.H.2    Lee, R.3
  • 26
    • 1642273617 scopus 로고    scopus 로고
    • Rho-regulatory proteins in breast cancer cell cell motility and invasion
    • Lin, M., and van Golen, K. L. (2004). Rho-regulatory proteins in breast cancer cell cell motility and invasion. Breast Cancer Res. Treat. 84, 49-60.
    • (2004) Breast Cancer Res. Treat. , vol.84 , pp. 49-60
    • Lin, M.1    Van Golen, K.L.2
  • 27
    • 0034682170 scopus 로고    scopus 로고
    • Checkpoint for invasion
    • Liotta, L. A., and Clair, T. (2000). Checkpoint for invasion. Nature 405, 287-288.
    • (2000) Nature , vol.405 , pp. 287-288
    • Liotta, L.A.1    Clair, T.2
  • 28
    • 0034574572 scopus 로고    scopus 로고
    • Rho GTPases in neuronal morphogenesis
    • Luo, L. (2000). Rho GTPases in neuronal morphogenesis. Nat. Rev. Neurosci. 1, 173-180.
    • (2000) Nat. Rev. Neurosci. , vol.1 , pp. 173-180
    • Luo, L.1
  • 30
    • 10744224916 scopus 로고    scopus 로고
    • The tumor invasion inhibitor dihyromotuporamine C activates RHO, remodels stress fibers and focal adhesions, and stimulates sodium-proton exchange
    • McHardy, L. M., Sinotte, R., Troussard, A., Sheldon, C., Church, J., Williams, D. E., Anderson, R. J., Dedhar, S., Roberge, M., and Roskelley, C. D. (2004). The tumor invasion inhibitor dihyromotuporamine C activates RHO, remodels stress fibers and focal adhesions, and stimulates sodium-proton exchange. Cancer Res. 64, 1468-1475.
    • (2004) Cancer Res. , vol.64 , pp. 1468-1475
    • McHardy, L.M.1    Sinotte, R.2    Troussard, A.3    Sheldon, C.4    Church, J.5    Williams, D.E.6    Anderson, R.J.7    Dedhar, S.8    Roberge, M.9    Roskelley, C.D.10
  • 31
    • 0034602561 scopus 로고    scopus 로고
    • Hepatoma cell migration through a mesothelial cell monolayer is inhibited by cyclic AMP-elevating agents via a Rho-dependent pathway
    • Mukai, M., Nakamura, H., Tatsuta, M., Iwasaki, T., Togawa, A., Imamura, F., and Akedo, H. (2000). Hepatoma cell migration through a mesothelial cell monolayer is inhibited by cyclic AMP-elevating agents via a Rho-dependent pathway. FEBS Lett. 484, 69-73.
    • (2000) FEBS Lett. , vol.484 , pp. 69-73
    • Mukai, M.1    Nakamura, H.2    Tatsuta, M.3    Iwasaki, T.4    Togawa, A.5    Imamura, F.6    Akedo, H.7
  • 32
    • 0037571979 scopus 로고    scopus 로고
    • Inhibition of sustained smooth muscle contraction by PKA and PKG preferentially mediated by phosphorylation of RhoA
    • Murthy, K. S., Zhou, H., Grider, J. R., and Makhlouf, G. M. (2003). Inhibition of sustained smooth muscle contraction by PKA and PKG preferentially mediated by phosphorylation of RhoA. Am. J. Physiol. 284, G1006-G1016.
    • (2003) Am. J. Physiol. , vol.284
    • Murthy, K.S.1    Zhou, H.2    Grider, J.R.3    Makhlouf, G.M.4
  • 33
    • 0034707597 scopus 로고    scopus 로고
    • RhoA function in lamellae formation and migration is regulated by the α 6β 4 integrin and cAMP metabolism
    • O'Connor, K. L., Nguyen, B.-K., and Mercurio, A. M. (2000). RhoA function in lamellae formation and migration is regulated by the α 6β 4 integrin and cAMP metabolism. J. Cell Biol. 148, 253-258.
    • (2000) J. Cell Biol. , vol.148 , pp. 253-258
    • O'Connor, K.L.1    Nguyen, B.-K.2    Mercurio, A.M.3
  • 34
    • 0032517857 scopus 로고    scopus 로고
    • Release of cAMP gating by the α 6β 4 integrin stimulates lamellae formation and the chemotactic migration of invasive carcinoma cells
    • O'Connor, K. L., Shaw, L. M., and Mercurio, A. M. (1998). Release of cAMP gating by the α 6β 4 integrin stimulates lamellae formation and the chemotactic migration of invasive carcinoma cells. J. Cell Biol. 143, 1749-1760.
    • (1998) J. Cell Biol. , vol.143 , pp. 1749-1760
    • O'Connor, K.L.1    Shaw, L.M.2    Mercurio, A.M.3
  • 36
    • 0029986283 scopus 로고    scopus 로고
    • Metastasis from human breast cancer cell lines
    • Price, J. E. (1996). Metastasis from human breast cancer cell lines. Breast Cancer Res. Treat. 39, 93-102.
    • (1996) Breast Cancer Res. Treat. , vol.39 , pp. 93-102
    • Price, J.E.1
  • 37
    • 0038172667 scopus 로고    scopus 로고
    • PKA inhibits RhoA activation: A protection mechanism against endothelial dysfunction
    • Qiao, J., Huang, F., and Lum, H. (2003). PKA inhibits RhoA activation: a protection mechanism against endothelial dysfunction. Am. J. Physiol. 284, L972-L980.
    • (2003) Am. J. Physiol. , vol.284
    • Qiao, J.1    Huang, F.2    Lum, H.3
  • 38
    • 0007528052 scopus 로고
    • Parathyroid hormone regulation in OK cells: In situ protein phosphorylation reactions involving PKA, protein kinase C and GTP-binding proteins
    • Reshkin, S. J., and Murer, H. (1991). Parathyroid hormone regulation in OK cells: in situ protein phosphorylation reactions involving PKA, protein kinase C and GTP-binding proteins. Cell Physiol. Biochem. 1, 143-159.
    • (1991) Cell Physiol. Biochem. , vol.1 , pp. 143-159
    • Reshkin, S.J.1    Murer, H.2
  • 39
    • 0026524306 scopus 로고
    • Involvement of C3 exotoxin-sensitive G proteins (rho/rac) in PTH signal transduction in OK cells
    • Reshkin, S. J., and Murer, H. (1992). Involvement of C3 exotoxin-sensitive G proteins (rho/rac) in PTH signal transduction in OK cells. Am. J. Physiol. 262, F572-F577.
    • (1992) Am. J. Physiol. , vol.262
    • Reshkin, S.J.1    Murer, H.2
  • 42
    • 0034037286 scopus 로고    scopus 로고
    • Microenvironment-induced cancer metastasis
    • Rofstad, E. K. (2000). Microenvironment-induced cancer metastasis. Int. J. Radiat. Biol. 76, 589-605.
    • (2000) Int. J. Radiat. Biol. , vol.76 , pp. 589-605
    • Rofstad, E.K.1
  • 43
    • 0344824500 scopus 로고    scopus 로고
    • Rapid microtubule-dependent induction of neurite-like extensions in NIH-3T3 fibroblasts by inhibition of ROCK and Cbl
    • Scaife, R. M., Job, D., and Langdon, W. Y. (2003). Rapid microtubule-dependent induction of neurite-like extensions in NIH-3T3 fibroblasts by inhibition of ROCK and Cbl. Mol. Biol. Cell 14, 4605-4617.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4605-4617
    • Scaife, R.M.1    Job, D.2    Langdon, W.Y.3
  • 44
    • 0031907484 scopus 로고    scopus 로고
    • RhoA-dependent phosphorylation and relocalization of ERM proteins into apical membrane/ actin protrusions in fibroblasts
    • Shaw, R. J., Henry, M., Solomon, F., and Jacks, T. (1998). RhoA-dependent phosphorylation and relocalization of ERM proteins into apical membrane/ actin protrusions in fibroblasts. Mol. Biol. Cell 9, 403-419.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 403-419
    • Shaw, R.J.1    Henry, M.2    Solomon, F.3    Jacks, T.4
  • 45
    • 0034241380 scopus 로고    scopus 로고
    • Specificity in the cAMP/PKA signaling pathway. Differential expression, regulation, and subcellular localization of subunits of PKA
    • Skalhegg, B. S., and Tasken, K. (2000). Specificity in the cAMP/PKA signaling pathway. Differential expression, regulation, and subcellular localization of subunits of PKA. Front. Biosci. 5, 678-693.
    • (2000) Front. Biosci. , vol.5 , pp. 678-693
    • Skalhegg, B.S.1    Tasken, K.2
  • 46
    • 0034682315 scopus 로고    scopus 로고
    • Blockade of RAGE-amphoterin signalling suppresses tumour growth and metastases
    • Taguchi, A., et al. (2000). Blockade of RAGE-amphoterin signalling suppresses tumour growth and metastases. Nature 405, 354-360.
    • (2000) Nature , vol.405 , pp. 354-360
    • Taguchi, A.1
  • 47
    • 0347359224 scopus 로고    scopus 로고
    • Localized effects of cAMP mediated by distinct routes of protein kinase A
    • Tasken, K., and Aandahl, E. M. (2004). Localized effects of cAMP mediated by distinct routes of protein kinase A. Physiol. Rev. 84, 137-167.
    • (2004) Physiol. Rev. , vol.84 , pp. 137-167
    • Tasken, K.1    Aandahl, E.M.2
  • 48
    • 0031878095 scopus 로고    scopus 로고
    • Na-H exchange acts downstream of RhoA to regulate integrin-induced cell adhesion and spreading
    • Tominaga, T., and Barber, D. L. (1998). Na-H exchange acts downstream of RhoA to regulate integrin-induced cell adhesion and spreading. Mol. Biol. Cell 9, 2287-2303.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2287-2303
    • Tominaga, T.1    Barber, D.L.2
  • 49
    • 0032541338 scopus 로고    scopus 로고
    • p160ROCK mediates RhoA activation of Na-H exchange
    • Tominaga, T., Ishizaki, T., Narumiya, S., and Barber, D. L. (1998). p160ROCK mediates RhoA activation of Na-H exchange. EMBO J. 17, 4712-4722.
    • (1998) EMBO J. , vol.17 , pp. 4712-4722
    • Tominaga, T.1    Ishizaki, T.2    Narumiya, S.3    Barber, D.L.4
  • 50
    • 0035475318 scopus 로고    scopus 로고
    • Expanding the role of NHERF, a PDZ-domain containing protein adapter, to growth regulation
    • Voltz, J. W., Weinman, E. J., and Shenolikar, S. (2001). Expanding the role of NHERF, a PDZ-domain containing protein adapter, to growth regulation. Oncogene 20, 6309-6314.
    • (2001) Oncogene , vol.20 , pp. 6309-6314
    • Voltz, J.W.1    Weinman, E.J.2    Shenolikar, S.3
  • 51
    • 0344758986 scopus 로고    scopus 로고
    • Regulation of cell polarity and protrusion formation by targeting RhoA for degradation
    • Wang, H. R., Zhang, Y., Ozdamar, B., Ogunjimi, A. A., Alexandrova, E., Thomsen, G. H., and Wrana, J. L. (2003). Regulation of cell polarity and protrusion formation by targeting RhoA for degradation. Science 302, 1775-1779.
    • (2003) Science , vol.302 , pp. 1775-1779
    • Wang, H.R.1    Zhang, Y.2    Ozdamar, B.3    Ogunjimi, A.A.4    Alexandrova, E.5    Thomsen, G.H.6    Wrana, J.L.7
  • 52
    • 0034899045 scopus 로고    scopus 로고
    • Signal pathways which promote invasion and metastasis: Critical and distinct contributions of extracellular signal-regulated kinase and Ral-specific guanine exchange factor pathways
    • Ward, Y., Wang, W., Woodhouse, E., Linnoila, I., Liotta, L., and Kelly, K. (2001). Signal pathways which promote invasion and metastasis: critical and distinct contributions of extracellular signal-regulated kinase and Ral-specific guanine exchange factor pathways. Mol. Cell. Biol. 21, 5958-5969.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5958-5969
    • Ward, Y.1    Wang, W.2    Woodhouse, E.3    Linnoila, I.4    Liotta, L.5    Kelly, K.6
  • 53
    • 0038586530 scopus 로고    scopus 로고
    • NZO-3 expression causes global changes to actin cytoskeleton in Madin-Darby canine kidney cells: Linking a tight junction protein to Rho GTPases
    • Wittchen, E. S., Haskins, J., and Stevenson, B. R. (2003). NZO-3 expression causes global changes to actin cytoskeleton in Madin-Darby canine kidney cells: linking a tight junction protein to Rho GTPases. Mol. Biol. Cell 14, 1757-1768.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1757-1768
    • Wittchen, E.S.1    Haskins, J.2    Stevenson, B.R.3
  • 54
    • 0034810232 scopus 로고    scopus 로고
    • Reliable and global measurement of fluorescence resonance energy transfer using fluorescence microscopes
    • Xia, Z., and Liu, Y. (2001). Reliable and global measurement of fluorescence resonance energy transfer using fluorescence microscopes. Biophys. J. 81, 2395-2402.
    • (2001) Biophys. J. , vol.81 , pp. 2395-2402
    • Xia, Z.1    Liu, Y.2
  • 55
    • 0037192802 scopus 로고    scopus 로고
    • Acidic extracellular pH induces vascular endothelial growth factor (VEGF) in human glioblastoma cells via ERK1/2 MAPK signaling pathway: Mechanism of low pH-induced VEGF
    • Xu, L., Fukumura, D., and Jain, R. K. (2002). Acidic extracellular pH induces vascular endothelial growth factor (VEGF) in human glioblastoma cells via ERK1/2 MAPK signaling pathway: mechanism of low pH-induced VEGF. J. Biol. Chem. 277, 11368-11374.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11368-11374
    • Xu, L.1    Fukumura, D.2    Jain, R.K.3
  • 56
    • 0033523842 scopus 로고    scopus 로고
    • Signal transduction. Grabbing phosphoproteins
    • Yaffe, M. B., and Cantley, L. C. (1999). Signal transduction. Grabbing phosphoproteins. Nature 402, 30-31.
    • (1999) Nature , vol.402 , pp. 30-31
    • Yaffe, M.B.1    Cantley, L.C.2
  • 58
    • 0037223854 scopus 로고    scopus 로고
    • Signalling and cross-talk of Rho-GTPases in mediating axon guidance
    • Yuan, X., Jin, M., Xu, X., Song, Y., Wu, C., Poo, M., and Duan, S. (2003). Signalling and cross-talk of Rho-GTPases in mediating axon guidance. Nat. Cell Biol. 5, 38-45.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 38-45
    • Yuan, X.1    Jin, M.2    Xu, X.3    Song, Y.4    Wu, C.5    Poo, M.6    Duan, S.7
  • 59
    • 0036532032 scopus 로고    scopus 로고
    • Compartmentalisation of cAMP and Ca(2+) signals
    • Zaccolo, M., Magalhaes, P., and Pozzan, T. (2002). Compartmentalisation of cAMP and Ca(2+) signals. Curr. Opin. Cell Biol. 14, 160-166.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 160-166
    • Zaccolo, M.1    Magalhaes, P.2    Pozzan, T.3
  • 60
    • 10744224225 scopus 로고    scopus 로고
    • Expression profile of genes associated with antimetastatic gene: Nm23-mediated metastasis inhibition in breast carcinoma cells
    • Zhao, H., et al. (2004). Expression profile of genes associated with antimetastatic gene: nm23-mediated metastasis inhibition in breast carcinoma cells. Int. J. Cancer. 109, 65-70.
    • (2004) Int. J. Cancer. , vol.109 , pp. 65-70
    • Zhao, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.