메뉴 건너뛰기




Volumn 102, Issue 9, 2010, Pages 489-498

Sodium fluoride induces podosome formation in endothelial cells

Author keywords

Actin cytoskeleton; Podosome; RhoGTPase; Sodium fluoride (NaF); Src

Indexed keywords

CARRIER PROTEIN; F ACTIN; FLUORIDE SODIUM; PROTEIN CDC42; PROTEIN SRC; RAC1 PROTEIN; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; UNCLASSIFIED DRUG; ACTIN; GUANINE NUCLEOTIDE BINDING PROTEIN; PROTEIN BINDING; SODIUM FLUORIDE;

EID: 77956651731     PISSN: 02484900     EISSN: 1768322X     Source Type: Journal    
DOI: 10.1042/BC20100030     Document Type: Article
Times cited : (15)

References (24)
  • 1
    • 3543072944 scopus 로고    scopus 로고
    • Active Rho is localized to podosomes induced by oncogenic Src and is required for their assembly and function
    • DOI 10.1083/jcb.200312168
    • Berdeaux, R. L., Diaz, B., Kim, L. and Martin, G. S. (2004) Active Rho is localized to podosomes induced by oncogenic Src and is required for their assembly and function. J. Cell Biol. 166, 317-323 (Pubitemid 39031235)
    • (2004) Journal of Cell Biology , vol.166 , Issue.3 , pp. 317-323
    • Berdeaux, R.L.1    Diaz, B.2    Kim, L.3    Martin, G.S.4
  • 2
    • 1642421365 scopus 로고    scopus 로고
    • Actin cytoskeleton remodelling via local inhibition of contractility at discrete microdomains
    • Burgstaller, G. and Gimona, M. (2004) Actin cytoskeleton remodelling via local inhibition of contractility at discrete microdomains. J. Cell Sci. 117, 223-231
    • (2004) J. Cell Sci. , vol.117 , pp. 223-231
    • Burgstaller, G.1    Gimona, M.2
  • 3
    • 0035861686 scopus 로고    scopus 로고
    • Phosphatidylinositol 3,4,5-trisphosphate directs association of Src homology 2-containing signaling proteins with gelsolin
    • Chellaiah, M. A., Biswas, R. S., Yuen, D., Alvarez, U. M. and Hruska, K. A. (2001) Phosphatidylinositol 3,4,5-trisphosphate directs association of Src homology 2-containing signaling proteins with gelsolin. J. Biol. Chem. 276, 47434-47444
    • (2001) J. Biol. Chem. , vol.276 , pp. 47434-47444
    • Chellaiah, M.A.1    Biswas, R.S.2    Yuen, D.3    Alvarez, U.M.4    Hruska, K.A.5
  • 4
    • 0037384873 scopus 로고    scopus 로고
    • EphrinA1 inactivates integrin-mediated vascular smooth muscle cell spreading via the Rac/PAK pathway
    • Deroanne, C., Vouret-Craviari, V., Wang, B. and Pouyssegur, J. (2003) EphrinA1 inactivates integrin-mediated vascular smooth muscle cell spreading via the Rac/PAK pathway. J. Cell Sci. 116, 1367-1376
    • (2003) J. Cell Sci. , vol.116 , pp. 1367-1376
    • Deroanne, C.1    Vouret-Craviari, V.2    Wang, B.3    Pouyssegur, J.4
  • 5
    • 4344689971 scopus 로고    scopus 로고
    • Protein kinase Cα activates c-Src and induces podosome formation via AFAP-110
    • Gatesman, A., Walker, V. G., Baisden, J. M., Weed, S. A. and Flynn, D. C. (2004) Protein kinase Cα activates c-Src and induces podosome formation via AFAP-110. Mol. Cell. Biol. 24, 7578-7597
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 7578-7597
    • Gatesman, A.1    Walker, V.G.2    Baisden, J.M.3    Weed, S.A.4    Flynn, D.C.5
  • 6
    • 47649130432 scopus 로고    scopus 로고
    • P190B RhoGAP regulates endothelial-cell-associated proteolysis through MT1-MMP and MMP2
    • DOI 10.1242/jcs.025817
    • Guegan, F., Tatin, F., Leste-Lasserre, T., Drutel, G., Genot, E. and Moreau, V. (2008) p190B RhoGAP regulates endothelial-cell-associated proteolysis through MT1-MMP and MMP2. J. Cell Sci. 121, 2054-2061 (Pubitemid 352015203)
    • (2008) Journal of Cell Science , vol.121 , Issue.12 , pp. 2054-2061
    • Guegan, F.1    Tatin, F.2    Leste-Lasserre, T.3    Drutel, G.4    Genot, E.5    Moreau, V.6
  • 7
    • 27944479854 scopus 로고    scopus 로고
    • Rho GTPases: Biochemistry and biology
    • Jaffe, A. B. and Hall, A. (2005) Rho GTPases: biochemistry and biology. Annu. Rev. Cell Dev. Biol. 21, 247-269
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 247-269
    • Jaffe, A.B.1    Hall, A.2
  • 8
    • 70350374205 scopus 로고    scopus 로고
    • Invadosomes at a glance
    • Linder, S. (2009) Invadosomes at a glance. J. Cell Sci. 122, 3009-3013
    • (2009) J. Cell Sci. , vol.122 , pp. 3009-3013
    • Linder, S.1
  • 9
    • 0034536206 scopus 로고    scopus 로고
    • Microtubule-dependent formation of podosomal adhesion structures in primary human macrophages
    • Linder, S., Hufner, K., Wintergerst, U. and Aepfelbacher, M. (2000) Microtubule-dependent formation of podosomal adhesion structures in primary human macrophages. J. Cell Sci. 113, 4165-4176
    • (2000) J. Cell Sci. , vol.113 , pp. 4165-4176
    • Linder, S.1    Hufner, K.2    Wintergerst, U.3    Aepfelbacher, M.4
  • 10
    • 0023769661 scopus 로고
    • Vanadate-treated baby hamster kidney fibroblasts show cytoskeleton and adhesion patterns similar to their Rous sarcoma virus-transformed counterparts
    • Marchisio, P. C., D'Urso, N., Comoglio, P. M., Giancotti, F. G. and Tarone, G. (1988) Vanadate-treated baby hamster kidney fibroblasts show cytoskeleton and adhesion patterns similar to their Rous sarcoma virus-transformed counterparts. J. Cell. Biochem. 37, 151-159
    • (1988) J. Cell. Biochem. , vol.37 , pp. 151-159
    • Marchisio, P.C.1    D'Urso, N.2    Comoglio, P.M.3    Giancotti, F.G.4    Tarone, G.5
  • 11
    • 0033531237 scopus 로고    scopus 로고
    • A balance of signaling by Rho family small GTPases RhoA, Rac1 and Cdc42 coordinates cytoskeletal morphology but not cell survival
    • Moorman, J. P., Luu, D., Wickham, J., Bobak, D. A. and Hahn, C. S. (1999) A balance of signaling by Rho family small GTPases RhoA, Rac1 and Cdc42 coordinates cytoskeletal morphology but not cell survival. Oncogene 18, 47-57
    • (1999) Oncogene , vol.18 , pp. 47-57
    • Moorman, J.P.1    Luu, D.2    Wickham, J.3    Bobak, D.A.4    Hahn, C.S.5
  • 12
    • 0141669167 scopus 로고    scopus 로고
    • Actin can reorganize into podosomes in aortic endothelial cells, a process controlled by Cdc42 and RhoA
    • Moreau, V., Tatin, F., Varon, C. and Genot, E. (2003) Actin can reorganize into podosomes in aortic endothelial cells, a process controlled by Cdc42 and RhoA. Mol. Cell. Biol. 23, 6809-6822
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 6809-6822
    • Moreau, V.1    Tatin, F.2    Varon, C.3    Genot, E.4
  • 13
    • 0031762533 scopus 로고    scopus 로고
    • Structures of Cdc42 bound to the active and catalytically compromised forms of Cdc42GAP
    • Nassar, N., Hoffman, G. R., Manor, D., Clardy, J. C. and Cerione, R. A. (1998) Structures of Cdc42 bound to the active and catalytically compromised forms of Cdc42GAP. Nat. Struct. Biol. 5, 1047-1052
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1047-1052
    • Nassar, N.1    Hoffman, G.R.2    Manor, D.3    Clardy, J.C.4    Cerione, R.A.5
  • 14
    • 0028961293 scopus 로고
    • Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes, C. D. and Hall, A. (1995) Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81, 53-62
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 15
    • 0029795963 scopus 로고    scopus 로고
    • Aluminum fluoride stimulates surface protrusions in cells overexpressing the ARF6 GTPase
    • Radhakrishna, H., Klausner, R. D. and Donaldson, J. G. (1996) Aluminum fluoride stimulates surface protrusions in cells overexpressing the ARF6 GTPase. J. Cell Biol. 134, 935-947
    • (1996) J. Cell Biol. , vol.134 , pp. 935-947
    • Radhakrishna, H.1    Klausner, R.D.2    Donaldson, J.G.3
  • 16
    • 0030716497 scopus 로고    scopus 로고
    • Structure at 1.65 å of RhoA and its GTPase-activating protein in complex with a transition-state analogue
    • DOI 10.1038/39651
    • Rittinger, K., Walker, P. A., Eccleston, J. F., Smerdon, S. J. and Gamblin, S. J. (1997) Structure at 1.65 Å of RhoA and its GTPase-activating protein in complex with a transition-state analogue. Nature 389, 758-762 (Pubitemid 27458966)
    • (1997) Nature , vol.389 , Issue.6652 , pp. 758-762
    • Rittinger, K.1    Walker, P.A.2    Eccleston, J.F.3    Smerdon, S.J.4    Gamblin, S.J.5
  • 17
    • 0031724591 scopus 로고    scopus 로고
    • Phosphotyrosine (p-Tyr)-dependent and -independent mechanisms of p190 RhoGAP-p120 RasGAP interaction: Tyr1105 of p190, a substrate for c-Src, is the sole p-Tyr mediator of complex formation
    • Roof, R. W., Haskell, M. D., Dukes, B. D., Sherman, N., Kinter, M. and Parsons, S. J. (1998) Phosphotyrosine (p-Tyr)-dependent and -independent mechanisms of p190 RhoGAP-p120 RasGAP interaction: Tyr1105 of p190, a substrate for c-Src, is the sole p-Tyr mediator of complex formation. Mol. Cell. Biol. 18, 7052-7063
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7052-7063
    • Roof, R.W.1    Haskell, M.D.2    Dukes, B.D.3    Sherman, N.4    Kinter, M.5    Parsons, S.J.6
  • 18
    • 0026740716 scopus 로고
    • Molecular cloning of cDNAs encoding the GAP-associated protein p190: Implications for a signaling pathway from Ras to the nucleus
    • Settleman, J., Narasimhan, V., Foster, L. C. and Weinberg, R. A. (1992) Molecular cloning of cDNAs encoding the GAP-associated protein p190: implications for a signaling pathway from Ras to the nucleus. Cell 69, 539-549
    • (1992) Cell , vol.69 , pp. 539-549
    • Settleman, J.1    Narasimhan, V.2    Foster, L.C.3    Weinberg, R.A.4
  • 19
    • 33645064530 scopus 로고    scopus 로고
    • A signalling cascade involving PKC, Src and Cdc42 regulates podosome assembly in cultured endothelial cells in response to phorbol ester
    • Tatin, F., Varon, C., Genot, E. and Moreau, V. (2006) A signalling cascade involving PKC, Src and Cdc42 regulates podosome assembly in cultured endothelial cells in response to phorbol ester. J. Cell Sci. 119, 769-781
    • (2006) J. Cell Sci. , vol.119 , pp. 769-781
    • Tatin, F.1    Varon, C.2    Genot, E.3    Moreau, V.4
  • 21
    • 0032478165 scopus 로고    scopus 로고
    • Evidence for distinct mechanisms of transition state stabilization of GTPases by fluoride
    • Vincent, S., Brouns, M., Hart, M. J. and Settleman, J. (1998) Evidence for distinct mechanisms of transition state stabilization of GTPases by fluoride. Proc. Natl. Acad. Sci. U.S.A. 95, 2210-2215
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 2210-2215
    • Vincent, S.1    Brouns, M.2    Hart, M.J.3    Settleman, J.4
  • 22
    • 0032831382 scopus 로고    scopus 로고
    • Inhibition of RhoGAP activity is sufficient for the induction of Rho-mediated actin reorganization
    • Vincent, S. and Settleman, J. (1999) Inhibition of RhoGAP activity is sufficient for the induction of Rho-mediated actin reorganization. Eur. J. Cell Biol. 78, 539-548
    • (1999) Eur. J. Cell Biol. , vol.78 , pp. 539-548
    • Vincent, S.1    Settleman, J.2
  • 24
    • 25444450611 scopus 로고    scopus 로고
    • PAK1 induces podosome formation in A7r5 vascular smooth muscle cells in a PAK-interacting exchange factor-dependent manner
    • Webb, B. A., Eves, R., Crawley, S. W., Zhou, S., Cote, G. P. and Mak, A. S. (2005) PAK1 induces podosome formation in A7r5 vascular smooth muscle cells in a PAK-interacting exchange factor-dependent manner. Am. J. Physiol. Cell. Physiol. 289, C898-C907
    • (2005) Am. J. Physiol. Cell. Physiol. , vol.289
    • Webb, B.A.1    Eves, R.2    Crawley, S.W.3    Zhou, S.4    Cote, G.P.5    Mak, A.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.