메뉴 건너뛰기




Volumn 28, Issue 3, 2006, Pages 633-639

Down-regulation of uPAR and cathepsin B retards cofilin dephosphorylation

Author keywords

Actin; Cathepsin B; Cofilin; Cytoskeleton; Integrin; uPAR

Indexed keywords

ACTIN; ACTIN DEPOLYMERIZING FACTOR; APOPTOSIS REGULATORY PROTEIN; CATHEPSIN B; CELL SURFACE RECEPTOR; MITOGEN ACTIVATED PROTEIN KINASE P38; ONCOPROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; PLASMINOGEN ACTIVATOR, UROKINASE RECEPTORS; PROSTATE APOPTOSIS RESPONSE 4 PROTEIN; PROSTATE APOPTOSIS RESPONSE-4 PROTEIN; SMALL INTERFERING RNA; VITRONECTIN RECEPTOR;

EID: 33645244156     PISSN: 10196439     EISSN: 17912423     Source Type: Journal    
DOI: 10.3892/ijo.28.3.633     Document Type: Article
Times cited : (19)

References (27)
  • 1
    • 11144225205 scopus 로고    scopus 로고
    • Integrin-linked kinase: A cancer therapeutic target unique among its ILK
    • Hannigan G, Troussard AA and Dedhar S: Integrin-linked kinase: a cancer therapeutic target unique among its ILK. Nat Rev Cancer 5: 51-63, 2005.
    • (2005) Nat Rev Cancer , vol.5 , pp. 51-63
    • Hannigan, G.1    Troussard, A.A.2    Dedhar, S.3
  • 2
    • 0029417238 scopus 로고
    • Phosphorylation by p34cdc2 regulates spindle association of human Eg5, a kinesin-related motor essential for bipolar spindle formation in vivo
    • Blangy A, Lane HA, d'Herin P, Harper M, Kress M and Nigg EA: Phosphorylation by p34cdc2 regulates spindle association of human Eg5, a kinesin-related motor essential for bipolar spindle formation in vivo. Cell 83: 1159-1169, 1995.
    • (1995) Cell , vol.83 , pp. 1159-1169
    • Blangy, A.1    Lane, H.A.2    D'Herin, P.3    Harper, M.4    Kress, M.5    Nigg, E.A.6
  • 4
    • 0031878090 scopus 로고    scopus 로고
    • The ADF homology (ADF-H) domain: A highly exploited actin-binding module
    • Lappalainen P, Kessels MM, Cope MJ and Drubin DG: The ADF homology (ADF-H) domain: a highly exploited actin-binding module. Mol Biol Cell 9: 1951-1959, 1998.
    • (1998) Mol Biol Cell , vol.9 , pp. 1951-1959
    • Lappalainen, P.1    Kessels, M.M.2    Cope, M.J.3    Drubin, D.G.4
  • 5
    • 0033280237 scopus 로고    scopus 로고
    • Proteins of the ADF/cofilin family: Essential regulators of actin dynamics
    • Bamburg JR: Proteins of the ADF/cofilin family: essential regulators of actin dynamics. Annu Rev Cell Dev Biol 15: 185-230, 1999.
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 185-230
    • Bamburg, J.R.1
  • 6
    • 0023387681 scopus 로고
    • Cofilin is a component of intranuclear and cytoplasmic actin rods induced in cultured cells
    • Nishida E, Iida K, Yonezawa N, Koyasu S, Yahara I and Sakai H: Cofilin is a component of intranuclear and cytoplasmic actin rods induced in cultured cells. Proc Natl Acad Sci USA 84: 5262-5266, 1987.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5262-5266
    • Nishida, E.1    Iida, K.2    Yonezawa, N.3    Koyasu, S.4    Yahara, I.5    Sakai, H.6
  • 7
    • 0036900955 scopus 로고    scopus 로고
    • ADF/cofilin and actin dynamics in disease
    • Bamburg JR and Wiggan OP: ADF/cofilin and actin dynamics in disease. Trends Cell Biol 12: 598-605, 2002.
    • (2002) Trends Cell Biol , vol.12 , pp. 598-605
    • Bamburg, J.R.1    Wiggan, O.P.2
  • 8
    • 0037178873 scopus 로고    scopus 로고
    • MEK mediates v-Src-induced disruption of the actin cytoskeleton via inactivation of the Rho-ROCK-LIM kinase pathway
    • Pawlak G and Helfman DM: MEK mediates v-Src-induced disruption of the actin cytoskeleton via inactivation of the Rho-ROCK-LIM kinase pathway. J Biol Chem 277: 26927-26933, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 26927-26933
    • Pawlak, G.1    Helfman, D.M.2
  • 10
    • 0031425359 scopus 로고    scopus 로고
    • Altered in vitro spreading and cytoskeletal organization in human glioma cells by down-regulation of urokinase receptor
    • Chintala SK, Mohanam S, Go Y, Venkaiah B, Sawaya R, Gokaslan ZL and Rao JS: Altered in vitro spreading and cytoskeletal organization in human glioma cells by down-regulation of urokinase receptor. Mol Carcinog 20: 355-365, 1997.
    • (1997) Mol Carcinog , vol.20 , pp. 355-365
    • Chintala, S.K.1    Mohanam, S.2    Go, Y.3    Venkaiah, B.4    Sawaya, R.5    Gokaslan, Z.L.6    Rao, J.S.7
  • 11
    • 0041737535 scopus 로고    scopus 로고
    • Molecular mechanisms of glioma invasiveness: The role of proteases
    • Rao JS: Molecular mechanisms of glioma invasiveness: the role of proteases. Nat Rev Cancer 3: 489-501, 2003.
    • (2003) Nat Rev Cancer , vol.3 , pp. 489-501
    • Rao, J.S.1
  • 12
    • 9144231998 scopus 로고    scopus 로고
    • RNAi-mediated inhibition of cathepsin B and uPAR leads to decreased cell invasion, angiogenesis and tumor growth in gliomas
    • Gondi CS, Lakka SS, Dinh DH, Olivero WC, Gujrati M and Rao JS: RNAi-mediated inhibition of cathepsin B and uPAR leads to decreased cell invasion, angiogenesis and tumor growth in gliomas. Oncogene 23: 8486-8496, 2004.
    • (2004) Oncogene , vol.23 , pp. 8486-8496
    • Gondi, C.S.1    Lakka, S.S.2    Dinh, D.H.3    Olivero, W.C.4    Gujrati, M.5    Rao, J.S.6
  • 13
    • 0029117595 scopus 로고
    • Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets
    • Hartwig JH, Bokoch GM, Carpenter CL, Janmey PA, Taylor LA, Toker A and Stossel TP: Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets. Cell 82: 643-653, 1995.
    • (1995) Cell , vol.82 , pp. 643-653
    • Hartwig, J.H.1    Bokoch, G.M.2    Carpenter, C.L.3    Janmey, P.A.4    Taylor, L.A.5    Toker, A.6    Stossel, T.P.7
  • 14
    • 0034614942 scopus 로고    scopus 로고
    • Role of cofilin in epidermal growth factor-stimulated actin polymerization and lamellipod protrusion
    • Chan AY, Bailly M, Zebda N, Segall JE and Condeelis JS: Role of cofilin in epidermal growth factor-stimulated actin polymerization and lamellipod protrusion. J Cell Biol 148: 531-542, 2000.
    • (2000) J Cell Biol , vol.148 , pp. 531-542
    • Chan, A.Y.1    Bailly, M.2    Zebda, N.3    Segall, J.E.4    Condeelis, J.S.5
  • 16
    • 0037461901 scopus 로고    scopus 로고
    • Downregulation of uPA inhibits migration and PI3k/Akt signaling in glioblastoma cells
    • DOI 10.1038/sj.onc.1206164
    • Chandrasekar N, Mohanam S, Gujrati M, Olivero WC, Dinh DH and Rao JS: Down-regulation of uPA inhibits migration and PI3k/Akt signaling in glioblastoma cells. Oncogene 22: 392-400, 2003. (Pubitemid 36194335)
    • (2003) Oncogene , vol.22 , Issue.3 , pp. 392-400
    • Chandrasekar, N.1    Mohanam, S.2    Gujrati, M.3    Olivero, W.C.4    Dinh, D.H.5    Rao, J.S.6
  • 17
    • 1342281679 scopus 로고    scopus 로고
    • Physical association of uPAR with the alphaV integrin on the surface of human NK cells
    • Gellert GC, Goldfarb RH and Kitson RP: Physical association of uPAR with the alphaV integrin on the surface of human NK cells. Biochem Biophys Res Commun 315: 1025-1032, 2004.
    • (2004) Biochem Biophys Res Commun , vol.315 , pp. 1025-1032
    • Gellert, G.C.1    Goldfarb, R.H.2    Kitson, R.P.3
  • 18
    • 0033604464 scopus 로고    scopus 로고
    • Negative regulation of Par-4 by oncogenic Ras is essential for cellular transformation
    • Qiu SG, Krishnan S, El Guendy N and Rangnekar VM: Negative regulation of Par-4 by oncogenic Ras is essential for cellular transformation. Oncogene 18: 7115-7123, 1999. (Pubitemid 30028883)
    • (1999) Oncogene , vol.18 , Issue.50 , pp. 7115-7123
    • Qiu, S.G.1    Krishnan, S.2    El-Guendy, N.3    Rangnekar, V.M.4
  • 21
    • 0036794093 scopus 로고    scopus 로고
    • 14-3-3 Regulates actin dynamics by stabilizing phosphorylated cofilin
    • Gohla A and Bokoch GM: 14-3-3 regulates actin dynamics by stabilizing phosphorylated cofilin. Curr Biol 12: 1704-1710, 2002.
    • (2002) Curr Biol , vol.12 , pp. 1704-1710
    • Gohla, A.1    Bokoch, G.M.2
  • 22
    • 0344391975 scopus 로고    scopus 로고
    • Regulation of actin filament dynamics by actin depolymerizing factor/cofilin and actin-interacting protein 1: New blades for twisted filaments
    • Ono S: Regulation of actin filament dynamics by actin depolymerizing factor/cofilin and actin-interacting protein 1: new blades for twisted filaments. Biochemistry 42: 13363-13370, 2003.
    • (2003) Biochemistry , vol.42 , pp. 13363-13370
    • Ono, S.1
  • 23
    • 0242656355 scopus 로고    scopus 로고
    • Dephosphorylation of cofilin is regulated through Ras and requires the combined activities of the Ras-effectors MEK and PI3K
    • Nebl G, Fischer S, Penzel R and Samstag Y: Dephosphorylation of cofilin is regulated through Ras and requires the combined activities of the Ras-effectors MEK and PI3K. Cell Signal 16: 235-243, 2004.
    • (2004) Cell Signal , vol.16 , pp. 235-243
    • Nebl, G.1    Fischer, S.2    Penzel, R.3    Samstag, Y.4
  • 25
    • 20044394412 scopus 로고    scopus 로고
    • VEGF treatment induces signaling pathways that regulate both actin polymerization and depolymerization
    • Gong C, Stoletov KV and Terman BI: VEGF treatment induces signaling pathways that regulate both actin polymerization and depolymerization. Angiogenesis 7: 313-322, 2004.
    • (2004) Angiogenesis , vol.7 , pp. 313-322
    • Gong, C.1    Stoletov, K.V.2    Terman, B.I.3
  • 27
    • 12344250639 scopus 로고    scopus 로고
    • Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics
    • DOI 10.1038/ncb1201
    • Gohla A, Birkenfeld J and Bokoch GM: Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics. Nat Cell Biol 7: 21-29, 2005. (Pubitemid 40123379)
    • (2005) Nature Cell Biology , vol.7 , Issue.1 , pp. 21-29
    • Gohla, A.1    Birkenfeld, J.2    Bokoch, G.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.