메뉴 건너뛰기




Volumn 291, Issue 9, 2016, Pages 4323-4333

Rapid remodeling of Invadosomes by Gi-coupled receptors: Dissecting the role of Rho GTPases

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; PHOSPHOLIPIDS; SIGNALING;

EID: 84966415524     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.695940     Document Type: Article
Times cited : (36)

References (60)
  • 1
    • 80054031825 scopus 로고    scopus 로고
    • Degrading devices: Invadosomes in proteolytic cell invasion
    • Linder, S., Wiesner, C., and Himmel, M. (2011) Degrading devices: invadosomes in proteolytic cell invasion. Annu. Rev. Cell Dev. Biol. 27, 185-211
    • (2011) Annu. Rev. Cell Dev. Biol. , vol.27 , pp. 185-211
    • Linder, S.1    Wiesner, C.2    Himmel, M.3
  • 2
    • 79959541003 scopus 로고    scopus 로고
    • The "ins" and "outs" of podosomes and invadopodia: Characteristics, formation and function
    • Murphy, D. A., and Courtneidge, S. A. (2011) The "ins" and "outs" of podosomes and invadopodia: characteristics, formation and function. Nat. Rev. Mol. Cell Biol. 12, 413-426
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 413-426
    • Murphy, D.A.1    Courtneidge, S.A.2
  • 4
    • 84920611863 scopus 로고    scopus 로고
    • Digging a little deeper: The stages of invadopodium formation and maturation
    • Beaty, B. T., and Condeelis, J. (2014) Digging a little deeper: the stages of invadopodium formation and maturation. Eur. J. Cell Biol. 93, 438-444
    • (2014) Eur. J. Cell Biol. , vol.93 , pp. 438-444
    • Beaty, B.T.1    Condeelis, J.2
  • 5
    • 3543114271 scopus 로고    scopus 로고
    • Foot and mouth: Podosomes, invadopodia and circular dorsal ruffles
    • Buccione, R., Orth, J. D., and McNiven, M. A. (2004) Foot and mouth: podosomes, invadopodia and circular dorsal ruffles. Nat. Rev. Mol. Cell Biol. 5, 647-657
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 647-657
    • Buccione, R.1    Orth, J.D.2    McNiven, M.A.3
  • 6
    • 84880648624 scopus 로고    scopus 로고
    • Signaling inputs to invadopodia and podosomes
    • Hoshino, D., Branch, K. M., and Weaver, A. M. (2013) Signaling inputs to invadopodia and podosomes. J. Cell Sci. 126, 2979-2989
    • (2013) J. Cell Sci. , vol.126 , pp. 2979-2989
    • Hoshino, D.1    Branch, K.M.2    Weaver, A.M.3
  • 10
    • 84939263309 scopus 로고    scopus 로고
    • Invadosomes in their natural habitat
    • Génot, E., and Gligorijevic, B. (2014) Invadosomes in their natural habitat. Eur. J. Cell Biol. 93, 367-379
    • (2014) Eur. J. Cell Biol. , vol.93 , pp. 367-379
    • Génot, E.1    Gligorijevic, B.2
  • 11
    • 84867398875 scopus 로고    scopus 로고
    • Spatiotemporal regulation of Src and its substrates at invadosomes
    • Boateng, L. R., and Huttenlocher, A. (2012) Spatiotemporal regulation of Src and its substrates at invadosomes. Eur. Cell Biol. 91, 878-888
    • (2012) Eur. Cell Biol. , vol.91 , pp. 878-888
    • Boateng, L.R.1    Huttenlocher, A.2
  • 13
    • 0347286962 scopus 로고    scopus 로고
    • Involvement of Cdc42 and Rac small G proteins in invadopodia formation of RPMI7951 cells
    • Nakahara, H., Otani, T., Sasaki, T., Miura, Y., Takai, Y., and Kogo, M. (2003) Involvement of Cdc42 and Rac small G proteins in invadopodia formation of RPMI7951 cells. Genes Cells 8, 1019-1027
    • (2003) Genes Cells , vol.8 , pp. 1019-1027
    • Nakahara, H.1    Otani, T.2    Sasaki, T.3    Miura, Y.4    Takai, Y.5    Kogo, M.6
  • 17
    • 84862629472 scopus 로고    scopus 로고
    • Hic-5 promotes invadopodia formation and invasion during TGF-β-induced epithelial-mesenchymal transition
    • Pignatelli, J., Tumbarello, D. A., Schmidt, R. P., and Turner, C. E. (2012) Hic-5 promotes invadopodia formation and invasion during TGF-β-induced epithelial-mesenchymal transition. J. Cell Biol. 197, 421-437
    • (2012) J. Cell Biol. , vol.197 , pp. 421-437
    • Pignatelli, J.1    Tumbarello, D.A.2    Schmidt, R.P.3    Turner, C.E.4
  • 19
    • 58849085553 scopus 로고    scopus 로고
    • Ezrin interacts with cortactin to form podosomal rosettes in pancreatic cancer cells
    • Kocher, H. M., Sandle, J., Mirza, T. A., Li, N. F., and Hart, I. R. (2009) Ezrin interacts with cortactin to form podosomal rosettes in pancreatic cancer cells. Gut 58, 271-284
    • (2009) Gut , vol.58 , pp. 271-284
    • Kocher, H.M.1    Sandle, J.2    Mirza, T.A.3    Li, N.F.4    Hart, I.R.5
  • 20
    • 80053944532 scopus 로고    scopus 로고
    • FAK is required for the assembly of podosome rosettes
    • Pan, Y. R., Chen, C. L., and Chen, H. C. (2011) FAK is required for the assembly of podosome rosettes. J. Cell Biol. 195, 113-129
    • (2011) J. Cell Biol. , vol.195 , pp. 113-129
    • Pan, Y.R.1    Chen, C.L.2    Chen, H.C.3
  • 21
    • 0019294081 scopus 로고
    • Altered distributions of the cytoskeletal proteins vinculin and α-actinin in cultured fibroblasts transformed by Rous sarcoma virus
    • David-Pfeuty, T., and Singer, S. J. (1980) Altered distributions of the cytoskeletal proteins vinculin and α-actinin in cultured fibroblasts transformed by Rous sarcoma virus. Proc. Natl. Acad. Sci. U. S. A. 77, 6687-6691
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , pp. 6687-6691
    • David-Pfeuty, T.1    Singer, S.J.2
  • 22
    • 0034978195 scopus 로고    scopus 로고
    • Organization of cytoskeletal F-actin, G-actin, and gelsolin in the adhesion structures in cultured osteoclast
    • Akisaka, T., Yoshida, H., Inoue, S., and Shimizu, K. (2001) Organization of cytoskeletal F-actin, G-actin, and gelsolin in the adhesion structures in cultured osteoclast. J. Bone Miner. Res. 16, 1248-1255
    • (2001) J. Bone Miner. Res. , vol.16 , pp. 1248-1255
    • Akisaka, T.1    Yoshida, H.2    Inoue, S.3    Shimizu, K.4
  • 24
    • 0029032202 scopus 로고
    • Lysophosphatidic acid, a multifunctional phospholipid messenger
    • Moolenaar, W. H. (1995) Lysophosphatidic acid, a multifunctional phospholipid messenger. J. Biol. Chem. 270, 12949-12952
    • (1995) J. Biol. Chem. , vol.270 , pp. 12949-12952
    • Moolenaar, W.H.1
  • 27
    • 34247534260 scopus 로고    scopus 로고
    • Regulation and biological activities of the autotaxin-LPA axis
    • van Meeteren, L. A., and Moolenaar, W. H. (2007) Regulation and biological activities of the autotaxin-LPA axis. Prog. Lipid Res. 46, 145-160
    • (2007) Prog. Lipid Res. , vol.46 , pp. 145-160
    • Van Meeteren, L.A.1    Moolenaar, W.H.2
  • 30
    • 83855160838 scopus 로고    scopus 로고
    • Autotaxin and LPA receptor signaling in cancer
    • Houben, A. J., and Moolenaar, W. H. (2011) Autotaxin and LPA receptor signaling in cancer. Cancer Metastasis Rev. 30, 557-565
    • (2011) Cancer Metastasis Rev. , vol.30 , pp. 557-565
    • Houben, A.J.1    Moolenaar, W.H.2
  • 31
    • 77949389034 scopus 로고    scopus 로고
    • Roles of endothelin signaling in melanocyte development and melanoma
    • Saldana-Caboverde, A., and Kos, L. (2010) Roles of endothelin signaling in melanocyte development and melanoma. Pigment Cell Melanoma Res. 23, 160-170
    • (2010) Pigment Cell Melanoma Res. , vol.23 , pp. 160-170
    • Saldana-Caboverde, A.1    Kos, L.2
  • 34
    • 0036724188 scopus 로고    scopus 로고
    • Activation of rac and cdc42 video imaged by fluorescent resonance energy transfer-based single-molecule probes in the membrane of living cells
    • Itoh, R. E., Kurokawa, K., Ohba, Y., Yoshizaki, H., Mochizuki, N., and Matsuda, M. (2002) Activation of rac and cdc42 video imaged by fluorescent resonance energy transfer-based single-molecule probes in the membrane of living cells. Mol. Cell. Biol. 22, 6582-6591
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6582-6591
    • Itoh, R.E.1    Kurokawa, K.2    Ohba, Y.3    Yoshizaki, H.4    Mochizuki, N.5    Matsuda, M.6
  • 36
    • 33646197411 scopus 로고    scopus 로고
    • Spatiotemporal dynamics of RhoA activity in migrating cells
    • Pertz, O., Hodgson, L., Klemke, R. L., and Hahn, K. M. (2006) Spatiotemporal dynamics of RhoA activity in migrating cells. Nature 440, 1069-1072
    • (2006) Nature , vol.440 , pp. 1069-1072
    • Pertz, O.1    Hodgson, L.2    Klemke, R.L.3    Hahn, K.M.4
  • 38
    • 0037329229 scopus 로고    scopus 로고
    • Podosomes display actin turnover and dynamic self-organization in osteoclasts expressing actin-green fluorescent protein
    • Destaing, O., Saltel, F., Géminard, J. C., Jurdic, P., and Bard, F. (2003) Podosomes display actin turnover and dynamic self-organization in osteoclasts expressing actin-green fluorescent protein. Mol. Biol. Cell 14, 407-416
    • (2003) Mol. Biol. Cell , vol.14 , pp. 407-416
    • Destaing, O.1    Saltel, F.2    Géminard, J.C.3    Jurdic, P.4    Bard, F.5
  • 42
    • 0347520943 scopus 로고    scopus 로고
    • Rac activation by lysophosphatidic acid LPA1 receptors through the guanine nucleotide exchange factor Tiam1
    • Van Leeuwen, F. N., Olivo, C., Grivell, S., Giepmans, B. N., Collard, J. G., and Moolenaar, W. H. (2003) Rac activation by lysophosphatidic acid LPA1 receptors through the guanine nucleotide exchange factor Tiam1. J. Biol. Chem. 278, 400-406
    • (2003) J. Biol. Chem. , vol.278 , pp. 400-406
    • Van Leeuwen, F.N.1    Olivo, C.2    Grivell, S.3    Giepmans, B.N.4    Collard, J.G.5    Moolenaar, W.H.6
  • 43
    • 70350089250 scopus 로고    scopus 로고
    • Identification of direct transcriptional targets of (V600E) BRAF/MEK signalling in melanoma
    • Packer, L. M., East, P., Reis-Filho, J. S., and Marais, R. (2009) Identification of direct transcriptional targets of (V600E) BRAF/MEK signalling in melanoma. Pigment Cell Melanoma Res. 22, 785-798
    • (2009) Pigment Cell Melanoma Res. , vol.22 , pp. 785-798
    • Packer, L.M.1    East, P.2    Reis-Filho, J.S.3    Marais, R.4
  • 44
    • 0030603158 scopus 로고    scopus 로고
    • Inhibition of protein kinase C μ by various inhibitors: Differentiation from protein kinase C isoenzymes
    • Gschwendt, M., Dieterich, S., Rennecke, J., Kittstein, W., Mueller, H. J., and Johannes, F. J. (1996) Inhibition of protein kinase C μ by various inhibitors: differentiation from protein kinase C isoenzymes. FEBS Lett. 392, 77-80
    • (1996) FEBS Lett. , vol.392 , pp. 77-80
    • Gschwendt, M.1    Dieterich, S.2    Rennecke, J.3    Kittstein, W.4    Mueller, H.J.5    Johannes, F.J.6
  • 45
    • 0033572662 scopus 로고    scopus 로고
    • The pleckstrin homology domains of protein kinase B and GRP1 (general receptor for phosphoinositides-1) are sensitive and selective probes for the cellular detection of phosphatidylinositol 3, 4-bisphosphate and/or phosphatidylinositol 3, 4, 5-trisphosphate in vivo
    • Gray, A., Van Der Kaay, J., and Downes, C. P. (1999) The pleckstrin homology domains of protein kinase B and GRP1 (general receptor for phosphoinositides-1) are sensitive and selective probes for the cellular detection of phosphatidylinositol 3, 4-bisphosphate and/or phosphatidylinositol 3, 4, 5-trisphosphate in vivo. Biochem. J. 344, 929-936
    • (1999) Biochem. J. , vol.344 , pp. 929-936
    • Gray, A.1    Van Der Kaay, J.2    Downes, C.P.3
  • 46
    • 83355173005 scopus 로고    scopus 로고
    • LPA is a chemorepellent for B16 melanoma cells: Action through the cAMP-elevating LPA5 receptor
    • Jongsma, M., Matas-Rico, E., Rzadkowski, A., Jalink, K., and Moolenaar, W. H. (2011) LPA is a chemorepellent for B16 melanoma cells: action through the cAMP-elevating LPA5 receptor. PLoS One 6, e29260
    • (2011) PLoS One , vol.6 , pp. e29260
    • Jongsma, M.1    Matas-Rico, E.2    Rzadkowski, A.3    Jalink, K.4    Moolenaar, W.H.5
  • 47
    • 84941283246 scopus 로고    scopus 로고
    • Rho GTPase signalling in cell migration
    • Ridley, A. J. (2015) Rho GTPase signalling in cell migration. Curr. Opin. Cell Biol. 36, 103-112
    • (2015) Curr. Opin. Cell Biol. , vol.36 , pp. 103-112
    • Ridley, A.J.1
  • 48
    • 18144420388 scopus 로고    scopus 로고
    • The G protein-coupled receptor S1P2 regulates Rho/Rho kinase pathway to inhibit tumor cell migration
    • Lepley, D., Paik, J. H., Hla, T., and Ferrer, F. (2005) The G protein-coupled receptor S1P2 regulates Rho/Rho kinase pathway to inhibit tumor cell migration. Cancer Res. 65, 3788-3795
    • (2005) Cancer Res. , vol.65 , pp. 3788-3795
    • Lepley, D.1    Paik, J.H.2    Hla, T.3    Ferrer, F.4
  • 49
    • 67449132285 scopus 로고    scopus 로고
    • Regulation of vascular physiology and pathology by the S1P2 receptor subtype
    • Skoura, A., and Hla, T. (2009) Regulation of vascular physiology and pathology by the S1P2 receptor subtype. Cardiovasc. Res. 82, 221-228
    • (2009) Cardiovasc. Res. , vol.82 , pp. 221-228
    • Skoura, A.1    Hla, T.2
  • 50
    • 84925859885 scopus 로고    scopus 로고
    • ARF6 promotes the formation of Rac1 and WAVE-dependent ventral F-actin rosettes in breast cancer cells in response to epidermal growth factor
    • Marchesin, V., Montagnac, G., and Chavrier, P. (2015) ARF6 promotes the formation of Rac1 and WAVE-dependent ventral F-actin rosettes in breast cancer cells in response to epidermal growth factor. PLoS One 10, e0121747
    • (2015) PLoS One , vol.10 , pp. e0121747
    • Marchesin, V.1    Montagnac, G.2    Chavrier, P.3
  • 53
    • 52149106669 scopus 로고    scopus 로고
    • Cellular signaling for activation of Rho GTPase Cdc42
    • Sinha, S., and Yang, W. (2008) Cellular signaling for activation of Rho GTPase Cdc42. Cell. Signal. 20, 1927-1934
    • (2008) Cell. Signal. , vol.20 , pp. 1927-1934
    • Sinha, S.1    Yang, W.2
  • 54
    • 38349156992 scopus 로고    scopus 로고
    • Heterotrimeric G protein βγ subunits stimulate FLJ00018, a guanine nucleotide exchange factor for Rac1 and Cdc42
    • Ueda, H., Nagae, R., Kozawa, M., Morishita, R., Kimura, S., Nagase, T., Ohara, O., Yoshida, S., and Asano, T. (2008) Heterotrimeric G protein βγ subunits stimulate FLJ00018, a guanine nucleotide exchange factor for Rac1 and Cdc42. J. Biol. Chem. 283, 1946-1953
    • (2008) J. Biol. Chem. , vol.283 , pp. 1946-1953
    • Ueda, H.1    Nagae, R.2    Kozawa, M.3    Morishita, R.4    Kimura, S.5    Nagase, T.6    Ohara, O.7    Yoshida, S.8    Asano, T.9
  • 55
  • 56
    • 0030658939 scopus 로고    scopus 로고
    • The guanine nucleotide exchange factor Tiam1 affects neuronal morphology: Opposing roles for the small GTPases Rac and Rho
    • Leeuwen, F. N., Kain, H. E., Kammen, R. A., Michiels, F., Kranenburg, O. W., and Collard, J. G. (1997) The guanine nucleotide exchange factor Tiam1 affects neuronal morphology: opposing roles for the small GTPases Rac and Rho. J. Cell Biol. 139, 797-807
    • (1997) J. Cell Biol. , vol.139 , pp. 797-807
    • Leeuwen, F.N.1    Kain, H.E.2    Kammen, R.A.3    Michiels, F.4    Kranenburg, O.W.5    Collard, J.G.6
  • 57
    • 0033615966 scopus 로고    scopus 로고
    • Rac downregulates Rho activity: Reciprocal balance between both GTPases determines cellular morphology and migratory behavior
    • Sander, E. E., ten Klooster, J. P., van Delft, S., van der Kammen, R. A., and Collard, J. G. (1999) Rac downregulates Rho activity: reciprocal balance between both GTPases determines cellular morphology and migratory behavior. J. Cell Biol. 147, 1009-1022
    • (1999) J. Cell Biol. , vol.147 , pp. 1009-1022
    • Sander, E.E.1    Ten Klooster, J.P.2    Van Delft, S.3    Van Der Kammen, R.A.4    Collard, J.G.5
  • 58
    • 84879009671 scopus 로고    scopus 로고
    • FilGAP and its close relatives: A mediator of Rho-Rac antagonism that regulates cell morphology and migration
    • Nakamura, F. (2013) FilGAP and its close relatives: a mediator of Rho-Rac antagonism that regulates cell morphology and migration. Biochem. J. 453, 17-25
    • (2013) Biochem. J. , vol.453 , pp. 17-25
    • Nakamura, F.1
  • 59
    • 65249165570 scopus 로고    scopus 로고
    • ECM degradation assays for analyzing local cell invasion
    • Artym, V. V., Yamada, K. M., and Mueller, S. C. (2009) ECM degradation assays for analyzing local cell invasion. Methods Mol. Biol. 522, 211-219
    • (2009) Methods Mol. Biol. , vol.522 , pp. 211-219
    • Artym, V.V.1    Yamada, K.M.2    Mueller, S.C.3
  • 60


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.