메뉴 건너뛰기




Volumn 116, Issue 24, 2003, Pages 4915-4924

Podosome formation in cultured A7r5 vascular smooth muscle cells requires Arp2/3-dependent denovo actin polymerization at discrete microdomains

Author keywords

Arp2 3; Cytoskeleton; Dynamics; Podosome; Smooth muscle

Indexed keywords

ACTIN RELATED PROTEIN 2; ACTIN RELATED PROTEIN 3; ALPHA ACTININ; CORTACTIN; F ACTIN; PHORBOL ESTER; VINCULIN; ZYXIN;

EID: 0348143126     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.00818     Document Type: Article
Times cited : (117)

References (45)
  • 1
    • 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
  • 3
    • 0029761790 scopus 로고    scopus 로고
    • Coordination of protrusion and translocation of the keratocyte involves rolling of the cell body
    • Anderson, K. I., Wang, Y.-L. and Small, J. V. (1996). Coordination of protrusion and translocation of the keratocyte involves rolling of the cell body. J. Cell Biol. 134, 1209-1218.
    • (1996) J. Cell Biol. , vol.134 , pp. 1209-1218
    • Anderson, K.I.1    Wang, Y.-L.2    Small, J.V.3
  • 4
    • 0036711804 scopus 로고    scopus 로고
    • Regulation of focal complex composition and disassemly by the calcium-dependent protease calpain
    • Bhatt, A., Kaverina, I., Otey, C. and Huttenlocher, A. (2002). Regulation of focal complex composition and disassemly by the calcium-dependent protease calpain. J. Cell Sci. 115, 3415-3425.
    • (2002) J. Cell Sci. , vol.115 , pp. 3415-3425
    • Bhatt, A.1    Kaverina, I.2    Otey, C.3    Huttenlocher, A.4
  • 5
    • 0037036373 scopus 로고    scopus 로고
    • Protein kinase C induces actin reorganization via a Src- and Rho-dependent pathway
    • Brandt, D., Gimona, M., Hillmann, M., Haller, H. and Mischak, H. (2002). Protein kinase C induces actin reorganization via a Src- and Rho-dependent pathway. J. Biol. Chem. 277, 20903-20910.
    • (2002) J. Biol. Chem. , vol.277 , pp. 20903-20910
    • Brandt, D.1    Gimona, M.2    Hillmann, M.3    Haller, H.4    Mischak, H.5
  • 6
    • 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
  • 7
    • 0029995797 scopus 로고    scopus 로고
    • Rho-stimulated contractility drives the formation of stress fibers and focal adhesions
    • Chrzanowska-Wodnicka, M. and Burridge, K. (1996). Rho-stimulated contractility drives the formation of stress fibers and focal adhesions. J. Cell Biol. 133, 1403-1415.
    • (1996) J. Cell Biol. , vol.133 , pp. 1403-1415
    • Chrzanowska-Wodnicka, M.1    Burridge, K.2
  • 8
    • 0037329229 scopus 로고    scopus 로고
    • Podosomes display actin turnover and dynamic self-organization in osteoclasts expressing actin-green fluorescent protein
    • Destaing, O., Saltel, F., Geminard, 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    Geminard, J.C.3    Jurdic, P.4    Bard, F.5
  • 9
    • 0033743866 scopus 로고    scopus 로고
    • PYK2 is an adhesion kinase in macrophages, localized in podosomes and activated by beta(2)-integrin ligation
    • Duong, L. T. and Rodan, G. A. (2000). PYK2 is an adhesion kinase in macrophages, localized in podosomes and activated by beta(2)-integrin ligation. Cell Motil. Cytoskel. 47, 174-188.
    • (2000) Cell Motil. Cytoskel. , vol.47 , pp. 174-188
    • Duong, L.T.1    Rodan, G.A.2
  • 10
    • 0033847250 scopus 로고    scopus 로고
    • The SH3 domain directs acto-myosin-dependent targeting of v-Src to focal adhesions via phosphatidylinositol 3-kinase
    • Fincham, V. J., Brunton, V. G. and Frame, M. C. (2000). The SH3 domain directs acto-myosin-dependent targeting of v-Src to focal adhesions via phosphatidylinositol 3-kinase. Mol. Cell. Biol. 20, 6518-6536.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6518-6536
    • Fincham, V.J.1    Brunton, V.G.2    Frame, M.C.3
  • 11
    • 0018692430 scopus 로고
    • A 130K protein from chicken gizzard: Its localization at the termini of microfilament bundles in cultured chicken cells
    • Geiger, B. (1979). A 130K protein from chicken gizzard: its localization at the termini of microfilament bundles in cultured chicken cells. Cell 18, 193-205.
    • (1979) Cell , vol.18 , pp. 193-205
    • Geiger, B.1
  • 13
    • 0038308424 scopus 로고    scopus 로고
    • Calponin repeats regulate actin filament stabilty and formation of podosomes in A7r5 smooth muscle cells
    • Gimona, M., Kaverina, I., Resch, G. P., Vignal, E. and Burgstaller, G. (2003). Calponin repeats regulate actin filament stabilty and formation of podosomes in A7r5 smooth muscle cells. Mol. Biol. Cell 14, 2482-2491.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2482-2491
    • Gimona, M.1    Kaverina, I.2    Resch, G.P.3    Vignal, E.4    Burgstaller, G.5
  • 14
    • 0036636101 scopus 로고    scopus 로고
    • Enhanced invasive properties exhibited by smooth muscle cells are associated with elevated production of MMP-2 in patients with aortic aneurisms
    • Goodall, S., Porter, K. E., Bell, P. R. and Thompson, M. M. (2002). Enhanced invasive properties exhibited by smooth muscle cells are associated with elevated production of MMP-2 in patients with aortic aneurisms. Eur. J. Endovasc. Surg. 24, 72-80.
    • (2002) Eur. J. Endovasc. Surg. , vol.24 , pp. 72-80
    • Goodall, S.1    Porter, K.E.2    Bell, P.R.3    Thompson, M.M.4
  • 15
    • 0036033308 scopus 로고    scopus 로고
    • Conventional PKC mediates Phorbol Dibutyrate-induced cytoskeletal remodeling in A7r5 smooth muscle cells
    • Hai, C. M., Hahne, P., Harrington, E. O. and Gimona, M. (2002). Conventional PKC mediates Phorbol Dibutyrate-induced cytoskeletal remodeling in A7r5 smooth muscle cells. Exp. Cell Res. 280, 64-74.
    • (2002) Exp. Cell Res. , vol.280 , pp. 64-74
    • Hai, C.M.1    Hahne, P.2    Harrington, E.O.3    Gimona, M.4
  • 16
    • 0034729686 scopus 로고    scopus 로고
    • Shp-2 mediated v-src-induced morphological changes and activation of the anti-apoptotic protein kinase Akt
    • Hakak, Y., Hsu, Y. S. and Martin, G. S. (2000). Shp-2 mediated v-src-induced morphological changes and activation of the anti-apoptotic protein kinase Akt. Oncogene 19, 3164-3174.
    • (2000) Oncogene , vol.19 , pp. 3164-3174
    • Hakak, Y.1    Hsu, Y.S.2    Martin, G.S.3
  • 18
    • 0033852462 scopus 로고    scopus 로고
    • Matrix metalloproteinase-1 expression by interaction between monocytes and vascular endothelial cells
    • Hojo, Y., Ikeda, U., Takahashi, M., Sakata, Y., Takizawa, T., Okada, K., Saito, T. and Shimada, K. (2000). Matrix metalloproteinase-1 expression by interaction between monocytes and vascular endothelial cells. J. Mol. Cardiol. 32, 1459-1468.
    • (2000) J. Mol. Cardiol. , vol.32 , pp. 1459-1468
    • Hojo, Y.1    Ikeda, U.2    Takahashi, M.3    Sakata, Y.4    Takizawa, T.5    Okada, K.6    Saito, T.7    Shimada, K.8
  • 20
    • 0033526397 scopus 로고    scopus 로고
    • Possible role of calponin h1 as a tumor suppressor in human uterine leiomyoma
    • Horiuchi, A., Nikaido, T., Taniguchi, S. and Fujii, S. (1999). Possible role of calponin h1 as a tumor suppressor in human uterine leiomyoma. J. Natl. Cancer Inst. 91, 790-796.
    • (1999) J. Natl. Cancer Inst. , vol.91 , pp. 790-796
    • Horiuchi, A.1    Nikaido, T.2    Taniguchi, S.3    Fujii, S.4
  • 22
    • 0036225779 scopus 로고    scopus 로고
    • Regulation of substrate adhesion dynamics during cell motility
    • Kaverina, I., Krylyshkina, O. and Small, J. V. (2002b). Regulation of substrate adhesion dynamics during cell motility. Int. J. Biochem. Cell Biol. 34, 746-761.
    • (2002) Int. J. Biochem. Cell Biol. , vol.34 , pp. 746-761
    • Kaverina, I.1    Krylyshkina, O.2    Small, J.V.3
  • 24
    • 0033578374 scopus 로고    scopus 로고
    • Wiskott-Aldrich Syndrome protein regulates podosomes in primary human macrophages
    • Linder, S., Nelson, D., Weiss, M. and Aepfelbacher, M. (1999). Wiskott-Aldrich Syndrome protein regulates podosomes in primary human macrophages. Proc. Natl. Acad. Sci. USA 96, 9648-9653.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9648-9653
    • Linder, S.1    Nelson, D.2    Weiss, M.3    Aepfelbacher, M.4
  • 25
    • 0034234559 scopus 로고    scopus 로고
    • The polarization effect of Wiskott-Aldrich Syndrome macrophages is linked to dislocalization of the Arp2/3 complex
    • Linder, S., Higgs, H., Hüfner, K., Schwartz, K., Pannicke, U. and Aepfelbacher, M. (2000a). The polarization effect of Wiskott-Aldrich Syndrome macrophages is linked to dislocalization of the Arp2/3 complex. J. Immunol. 165, 221-225.
    • (2000) J. Immunol. , vol.165 , pp. 221-225
    • Linder, S.1    Higgs, H.2    Hüfner, K.3    Schwartz, K.4    Pannicke, U.5    Aepfelbacher, M.6
  • 26
    • 0034536206 scopus 로고    scopus 로고
    • Microtubule-dependent formation of podosomal adhesion structures in primary human macrophages
    • Linder, S., Hüfner, K., Wintergerst, U. and Aepfelbacher, M. (2000b). 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    Hüfner, K.2    Wintergerst, U.3    Aepfelbacher, M.4
  • 27
    • 0032585538 scopus 로고    scopus 로고
    • Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex
    • Machesky, L. M. and Insall, R. H. (1998). Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex. Curr. Biol. 8, 1347-1356.
    • (1998) Curr. Biol. , vol.8 , pp. 1347-1356
    • Machesky, L.M.1    Insall, R.H.2
  • 28
    • 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
  • 30
    • 0036138874 scopus 로고    scopus 로고
    • Proteomic analysis of normal and malignant prostate tissue to identify novel proteins lost in cancer
    • Meehan, K. L., Holland, J. W. and Dawkins, H. J. (2002). Proteomic analysis of normal and malignant prostate tissue to identify novel proteins lost in cancer. Prostate 50, 54-63.
    • (2002) Prostate , vol.50 , pp. 54-63
    • Meehan, K.L.1    Holland, J.W.2    Dawkins, H.J.3
  • 31
    • 0036468250 scopus 로고    scopus 로고
    • Essential role of neural Wiskott-Aldrich syndrome protein in podosome formation and degradation of extracellular matrix in src-transformed fibroblasts
    • Mizutani, K., Miki, H., He, H., Maruta, H. and Takenawa, T. (2002). Essential role of neural Wiskott-Aldrich syndrome protein in podosome formation and degradation of extracellular matrix in src-transformed fibroblasts. Cancer Res. 62, 669-674.
    • (2002) Cancer Res. , vol.62 , pp. 669-674
    • Mizutani, K.1    Miki, H.2    He, H.3    Maruta, H.4    Takenawa, T.5
  • 32
    • 0037143448 scopus 로고    scopus 로고
    • Rho-Kinase and Myosin-II Control Phagocytic Cup Formation during CR, but Not FcγR, Phagocytosis
    • Olazabal, I., Caron, E., May, R., Schilling, K., Knecht, D. and Machesky, L. (2002). Rho-Kinase and Myosin-II Control Phagocytic Cup Formation during CR, but Not FcγR, Phagocytosis. Curr. Biol. 12, 1413-1418.
    • (2002) Curr. Biol. , vol.12 , pp. 1413-1418
    • Olazabal, I.1    Caron, E.2    May, R.3    Schilling, K.4    Knecht, D.5    Machesky, L.6
  • 33
    • 0034865951 scopus 로고    scopus 로고
    • Podosomes in osteoclast-like cells. Structural analysis and cooperative roles of paxillin, proline-rich tyrosine kinase (Pyk2) and integrin alpha v beta 3
    • Pfaff, M. and Jurdic, P. (2001). Podosomes in osteoclast-like cells. Structural analysis and cooperative roles of paxillin, proline-rich tyrosine kinase (Pyk2) and integrin alpha v beta 3. J. Cell Sci. 114, 2775-2786.
    • (2001) J. Cell Sci. , vol.114 , pp. 2775-2786
    • Pfaff, M.1    Jurdic, P.2
  • 34
    • 0031846612 scopus 로고    scopus 로고
    • Eps8, a tyrosine kinase substrate, is recruited to the cell cortex and dynamic F-actin upon cytoskeleton remodeling
    • Provenzano, C., Gallo, R., Carbone, R., Di Fiore, P. P., Falcone, G., Castellani, L. and Alema, S. (1998). Eps8, a tyrosine kinase substrate, is recruited to the cell cortex and dynamic F-actin upon cytoskeleton remodeling. Exp. Cell Res. 242, 186-200.
    • (1998) Exp. Cell Res. , vol.242 , pp. 186-200
    • Provenzano, C.1    Gallo, R.2    Carbone, R.3    Di Fiore, P.P.4    Falcone, G.5    Castellani, L.6    Alema, S.7
  • 35
    • 0033577975 scopus 로고    scopus 로고
    • Interplay between Rac and Rho in the control of substrate contact dynamics
    • Rottner, K., Hall, A. and Small, J. V. (1999). Interplay between Rac and Rho in the control of substrate contact dynamics. Curr. Biol. 9, 640-648.
    • (1999) Curr. Biol. , vol.9 , pp. 640-648
    • Rottner, K.1    Hall, A.2    Small, J.V.3
  • 36
    • 0034715923 scopus 로고    scopus 로고
    • Focal adhesions: A nexus for intracellular signaling and cytoskeletal dynamics
    • Sastry, S. K. and Burridge, K. (2000). Focal adhesions: a nexus for intracellular signaling and cytoskeletal dynamics. Exp. Cell Res. 261, 25-36.
    • (2000) Exp. Cell Res. , vol.261 , pp. 25-36
    • Sastry, S.K.1    Burridge, K.2
  • 38
    • 0032911020 scopus 로고    scopus 로고
    • Bidirectional signaling between the cytoskeleton and integrins
    • Schoenwaelder, S. M. and Burridge, K. (1999). Bidirectional signaling between the cytoskeleton and integrins. Curr. Opin. Cell Biol. 11, 274-286.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 274-286
    • Schoenwaelder, S.M.1    Burridge, K.2
  • 40
    • 0036164721 scopus 로고    scopus 로고
    • Calponin h1 induced a flattened morphology and suppressed the growth of human fibrosarcoma HT1080 cells
    • Takeoka, M., Ehara, T., Sagara, J., Hashimoto, S. and Taniguchi, S. (2002). Calponin h1 induced a flattened morphology and suppressed the growth of human fibrosarcoma HT1080 cells. Eur. J. Cancer 38, 436-442.
    • (2002) Eur. J. Cancer , vol.38 , pp. 436-442
    • Takeoka, M.1    Ehara, T.2    Sagara, J.3    Hashimoto, S.4    Taniguchi, S.5
  • 41
    • 0022357441 scopus 로고
    • Rous sacroma virus-transformed fibroblasts adhere primarily at discrete protrusions of the ventral membrane called podosomes
    • Tarone, G., Cirillo, D., Giancotti, F. G., Comoglio, P. M. and Marchisio, P. C. (1985). Rous sacroma virus-transformed fibroblasts adhere primarily at discrete protrusions of the ventral membrane called podosomes. Exp. Cell Res. 159, 141-157.
    • (1985) Exp. Cell Res. , vol.159 , pp. 141-157
    • Tarone, G.1    Cirillo, D.2    Giancotti, F.G.3    Comoglio, P.M.4    Marchisio, P.C.5
  • 42
    • 0024340706 scopus 로고
    • Calpain proteolysis of free and bound forms of calponin, a troponin T-like protein in smooth muscle
    • Tsunekawa, S., Takahashi, K., Abe, M., Hiwada, K., Ozawa, K. and Murachi, T. (1989). Calpain proteolysis of free and bound forms of calponin, a troponin T-like protein in smooth muscle. FEBS Lett. 250, 493-496.
    • (1989) FEBS Lett. , vol.250 , pp. 493-496
    • Tsunekawa, S.1    Takahashi, K.2    Abe, M.3    Hiwada, K.4    Ozawa, K.5    Murachi, T.6
  • 43
    • 0034597092 scopus 로고    scopus 로고
    • Cortactin localization to sites of actin assembly in lamellipodia requires interaction with F-actin and the Arp2/3 complex
    • Weed, S. A., Karginov, A. V., Schafer, D. A., Weaver, A. M., Kinley, A. W., Cooper, J. A. and Parsons, J. T. (2000). Cortactin localization to sites of actin assembly in lamellipodia requires interaction with F-actin and the Arp2/3 complex. J. Cell Biol. 151, 29-40.
    • (2000) J. Cell Biol. , vol.151 , pp. 29-40
    • Weed, S.A.1    Karginov, A.V.2    Schafer, D.A.3    Weaver, A.M.4    Kinley, A.W.5    Cooper, J.A.6    Parsons, J.T.7
  • 44
    • 0035524007 scopus 로고    scopus 로고
    • Integrins as targets of angiogenesis inhibition
    • Westlin, W. F. (2001). Integrins as targets of angiogenesis inhibition. Cancer J. Supplement 3, S139-143.
    • (2001) Cancer J. , Issue.SUPPL. 3
    • Westlin, W.F.1
  • 45
    • 0034528581 scopus 로고    scopus 로고
    • Proteolysis of acidic calponin by μ-calpain
    • Yoshimoto, R., Hori, M., Ozaki, H. and Karaki, H. (2000). Proteolysis of acidic calponin by μ-calpain. J. Biochem. 128,
    • (2000) J. Biochem. , vol.128 , pp. 1045-1049
    • Yoshimoto, R.1    Hori, M.2    Ozaki, H.3    Karaki, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.