메뉴 건너뛰기




Volumn 66, Issue 1, 1999, Pages 24-30

The benzoquinone ansamycin geldanamycin stimulates proteolytic degradation of focal adhesion kinase

Author keywords

FAK; Geldanamycin; hsp90; Proteolysis

Indexed keywords

ANSAMYCIN DERIVATIVE; BENZOQUINONE; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; PROTEIN TYROSINE KINASE;

EID: 0032787306     PISSN: 10967192     EISSN: None     Source Type: Journal    
DOI: 10.1006/mgme.1998.2774     Document Type: Article
Times cited : (67)

References (46)
  • 1
    • 0025376378 scopus 로고
    • Monoclonal antibodies to individual tyrosine-phosphorylated protein substrates of oncogene-encoded tyrosine kinases
    • Kanner SB, Reynolds AB, Vines RR, Parsons JT. Monoclonal antibodies to individual tyrosine-phosphorylated protein substrates of oncogene-encoded tyrosine kinases. Proc Natl Acad Sci USA 87:3328-3332, 1990.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 3328-3332
    • Kanner, S.B.1    Reynolds, A.B.2    Vines, R.R.3    Parsons, J.T.4
  • 2
    • 0024599702 scopus 로고
    • Transformation-specific tyrosine phosphorylation of a novel cellular protein in chicken cells expressing oncogenic variants of the avian cellular src gene
    • Reynolds AB, Roesel DJ, Kanner SB, Parsons JT. Transformation-specific tyrosine phosphorylation of a novel cellular protein in chicken cells expressing oncogenic variants of the avian cellular src gene. Mol Cell Biol 9:629-638, 1989.
    • (1989) Mol Cell Biol , vol.9 , pp. 629-638
    • Reynolds, A.B.1    Roesel, D.J.2    Kanner, S.B.3    Parsons, J.T.4
  • 4
    • 0027428367 scopus 로고
    • Identification of sequences required for the efficient localization of the focal adhesion kinase, pp125FAK, to cellular focal adhesions
    • Hildebrand JD, Schaller MD, Parsons JT. Identification of sequences required for the efficient localization of the focal adhesion kinase, pp125FAK, to cellular focal adhesions. J Cell Biol 123:993-1005, 1993.
    • (1993) J Cell Biol , vol.123 , pp. 993-1005
    • Hildebrand, J.D.1    Schaller, M.D.2    Parsons, J.T.3
  • 5
    • 0027055575 scopus 로고
    • Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase
    • Kornberg L, Earp HS, Parsons JT, Schaller M, Juliano RL. Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase. J Biol Chem 267:23439-23442, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 23439-23442
    • Kornberg, L.1    Earp, H.S.2    Parsons, J.T.3    Schaller, M.4    Juliano, R.L.5
  • 6
    • 0026497659 scopus 로고
    • Integrin-dependent phosphorylation and activation of the protein tyrosine kinase pp125FAK in platelets
    • Lipfert L, Haimovich B, Schaller MD, Cobb BS, Parsons JT, Brugge JS. Integrin-dependent phosphorylation and activation of the protein tyrosine kinase pp125FAK in platelets. J Cell Biol 119:905-912, 1992.
    • (1992) J Cell Biol , vol.119 , pp. 905-912
    • Lipfert, L.1    Haimovich, B.2    Schaller, M.D.3    Cobb, B.S.4    Parsons, J.T.5    Brugge, J.S.6
  • 8
    • 0029010351 scopus 로고
    • Stimulation of human monocytes with macrophage colony-stimulating factor induces a Grb2-mediated association of the focal adhesion kinase pp125FAK and dynamin
    • Kharbanda S, Saleem A, Yuan Z, Emoto Y, Prasad KV, Kufe D. Stimulation of human monocytes with macrophage colony-stimulating factor induces a Grb2-mediated association of the focal adhesion kinase pp125FAK and dynamin. Proc Natl Acad Sci USA 92:6132-6136, 1995.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 6132-6136
    • Kharbanda, S.1    Saleem, A.2    Yuan, Z.3    Emoto, Y.4    Prasad, K.V.5    Kufe, D.6
  • 9
    • 0028049088 scopus 로고
    • Platelet-derived growth factor modulation of focal adhesion kinase (p125FAK) and paxillin tyrosine phosphorylation in Swiss 3T3 cells. Bell-shaped dose response and cross-talk with bombesin
    • Rankin S, Rozengurt E. Platelet-derived growth factor modulation of focal adhesion kinase (p125FAK) and paxillin tyrosine phosphorylation in Swiss 3T3 cells. Bell-shaped dose response and cross-talk with bombesin. J Biol Chem 269:704-710, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 704-710
    • Rankin, S.1    Rozengurt, E.2
  • 10
    • 0029947181 scopus 로고    scopus 로고
    • Requirement for phosphatidylinositol 3′-kinase activity in platelet-derived growth factor-stimulated tyrosine phosphorylation of p 125 focal adhesion kinase and paxillin
    • Rankin S, Hooshmand RR, Claesson WL, Rozengurt E. Requirement for phosphatidylinositol 3′-kinase activity in platelet-derived growth factor-stimulated tyrosine phosphorylation of p 125 focal adhesion kinase and paxillin. J Biol Chem 271:7829-7834, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 7829-7834
    • Rankin, S.1    Hooshmand, R.R.2    Claesson, W.L.3    Rozengurt, E.4
  • 11
    • 0027153594 scopus 로고
    • Bombesin stimulation of p125 focal adhesion kinase tyrosine phosphorylation. Role of protein kinase C, Ca2+ mobilization, and the actin cytoskeleton
    • Sinnett SJ, Zachary I, Valverde AM, Rozengurt E. Bombesin stimulation of p125 focal adhesion kinase tyrosine phosphorylation. Role of protein kinase C, Ca2+ mobilization, and the actin cytoskeleton. J Biol Chem 268:14261-14268, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 14261-14268
    • Sinnett, S.J.1    Zachary, I.2    Valverde, A.M.3    Rozengurt, E.4
  • 13
    • 0026674919 scopus 로고
    • Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin
    • Hanks SK, Calalb MB, Harper MC, Patel SK. Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin. Proc Natl Acad Sci USA 89:8487-8491, 1992.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 8487-8491
    • Hanks, S.K.1    Calalb, M.B.2    Harper, M.C.3    Patel, S.K.4
  • 14
    • 0028783271 scopus 로고
    • Mesodermal defect in late phase of gastrulation by a targeted mutation of focal adhesion kinase, FAK
    • Furuta Y, Ilic D, Kanazawa S, Takeda N, Yamamoto T, Aizawa S. Mesodermal defect in late phase of gastrulation by a targeted mutation of focal adhesion kinase, FAK. Oncogene 11:1989-1995, 1995.
    • (1995) Oncogene , vol.11 , pp. 1989-1995
    • Furuta, Y.1    Ilic, D.2    Kanazawa, S.3    Takeda, N.4    Yamamoto, T.5    Aizawa, S.6
  • 16
    • 0027448821 scopus 로고
    • Expression of focal adhesion kinase gene and invasive cancer
    • Weiner TM, Liu ET, Craven RJ, Cance WG. Expression of focal adhesion kinase gene and invasive cancer. Lancet 342: 1024-1025, 1993.
    • (1993) Lancet , vol.342 , pp. 1024-1025
    • Weiner, T.M.1    Liu, E.T.2    Craven, R.J.3    Cance, W.G.4
  • 19
    • 0026759309 scopus 로고
    • Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation
    • Guan JL, Shalloway D. Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation. Nature 358:690-692, 1992.
    • (1992) Nature , vol.358 , pp. 690-692
    • Guan, J.L.1    Shalloway, D.2
  • 20
    • 0029092674 scopus 로고
    • Focal adhesion kinase (p125FAK) expression correlates with motility of human melanoma cell lines
    • Akasaka T, Van LR, Yoshinaga IG, Mihm MJ, Byers HR. Focal adhesion kinase (p125FAK) expression correlates with motility of human melanoma cell lines. J Invest Dermatol 105:104-108, 1995.
    • (1995) J Invest Dermatol , vol.105 , pp. 104-108
    • Akasaka, T.1    Van, L.R.2    Yoshinaga, I.G.3    Mihm, M.J.4    Byers, H.R.5
  • 21
    • 0029739950 scopus 로고    scopus 로고
    • Control of adhesion-dependent cell survival by focal adhesion kinase
    • Frisch SM, Vuori K, Ruoslahti E, Chan HP. Control of adhesion-dependent cell survival by focal adhesion kinase. J Cell Biol 134:793-799, 1996.
    • (1996) J Cell Biol , vol.134 , pp. 793-799
    • Frisch, S.M.1    Vuori, K.2    Ruoslahti, E.3    Chan, H.P.4
  • 23
    • 0024467122 scopus 로고
    • Irreversible inhibition of v-src tyrosine kinase activity by herbimycin a and its abrogation by sulfhydryl compounds
    • Uehara Y, Fukazawa H, Murakami Y, Mizuno S. Irreversible inhibition of v-src tyrosine kinase activity by herbimycin A and its abrogation by sulfhydryl compounds. Biochem Biophys Res Commun 163:803-809, 1989.
    • (1989) Biochem Biophys Res Commun , vol.163 , pp. 803-809
    • Uehara, Y.1    Fukazawa, H.2    Murakami, Y.3    Mizuno, S.4
  • 24
    • 0028834626 scopus 로고
    • Inhibition of the association with nuclear matrix of pRB, p70 and p40 proteins along with the specific suppression of c-MYC expression by geldanamycin, an inhibitor of Src tyrosine kinase
    • Yamaki H, Nakajima M, Seimiya H, Saya H, Sugita M, Tsuruo T. Inhibition of the association with nuclear matrix of pRB, p70 and p40 proteins along with the specific suppression of c-MYC expression by geldanamycin, an inhibitor of Src tyrosine kinase. J Antibiot (Tokyo) 48:1021-1026, 1995.
    • (1995) J Antibiot (Tokyo) , vol.48 , pp. 1021-1026
    • Yamaki, H.1    Nakajima, M.2    Seimiya, H.3    Saya, H.4    Sugita, M.5    Tsuruo, T.6
  • 25
    • 0028064940 scopus 로고
    • Inhibition of heat shock protein HSP90-pp60v-src hetero-protein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation
    • Whitesell L, Mimnaugh EG, De CB, Myers CE, Neckers LM. Inhibition of heat shock protein HSP90-pp60v-src hetero-protein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation. Proc Natl Acad Sci USA 91:8324-8328, 1994.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    De, C.B.3    Myers, C.E.4    Neckers, L.M.5
  • 27
    • 0028786332 scopus 로고
    • Disruption of the Raf-1-hsp90 molecular complex results in destabilization of Raf-1 and loss of Raf-1-Ras association
    • Schulte T, Blagosklonny M, Ingui C, Neckers L. Disruption of the Raf-1-hsp90 molecular complex results in destabilization of Raf-1 and loss of Raf-1-Ras association. J Biol Chem 270:24585-24588, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 24585-24588
    • Schulte, T.1    Blagosklonny, M.2    Ingui, C.3    Neckers, L.4
  • 28
    • 0029670034 scopus 로고    scopus 로고
    • p185erbB2 binds to GRP94 in vivo. Dissociation of the p185erbB2/GRP94 heterocomplex by benzoquinone ansamycins precedes depletion of p185erbB2
    • Chavany C, Mimnaugh E, Miller P, Bitton R, Nguyen P, Trepel J, Whitesell L, Schnur R, Moyer J, Neckers L. p185erbB2 binds to GRP94 in vivo. Dissociation of the p185erbB2/GRP94 heterocomplex by benzoquinone ansamycins precedes depletion of p185erbB2. J Biol Chem 271: 4974-4977, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 4974-4977
    • Chavany, C.1    Mimnaugh, E.2    Miller, P.3    Bitton, R.4    Nguyen, P.5    Trepel, J.6    Whitesell, L.7    Schnur, R.8    Moyer, J.9    Neckers, L.10
  • 29
    • 0028828273 scopus 로고
    • Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent
    • Smith D, Whitesell L, Nair S, Chen S, Prapapanich V, Rimerman R. Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent. Mol Cell Biol 15:6804-6812, 1995.
    • (1995) Mol Cell Biol , vol.15 , pp. 6804-6812
    • Smith, D.1    Whitesell, L.2    Nair, S.3    Chen, S.4    Prapapanich, V.5    Rimerman, R.6
  • 31
    • 0029973294 scopus 로고    scopus 로고
    • Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells
    • Whitesell L, Cook P. Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells. Mol Endocrinol 10:705-712, 1996.
    • (1996) Mol Endocrinol , vol.10 , pp. 705-712
    • Whitesell, L.1    Cook, P.2
  • 33
    • 0029008487 scopus 로고
    • Herbimycin a induces the 20 S proteasome- And ubiquitin- dependent degradation of receptor tyrosine kinases
    • Sepp-Lorenzino L, Ma Z, Lebwohl DE, Vinitsky A, Rosen N. Herbimycin A induces the 20 S proteasome- and ubiquitin- dependent degradation of receptor tyrosine kinases. J Biol Chem 270:16580-16587, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 16580-16587
    • Sepp-Lorenzino, L.1    Ma, Z.2    De Lebwohl3    Vinitsky, A.4    Rosen, N.5
  • 34
    • 0029812759 scopus 로고    scopus 로고
    • c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin
    • c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin. J Biol Chem 271:22796-22801, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 22796-22801
    • Mimnaugh, E.1    Chavany, C.2    Neckers, L.3
  • 35
    • 0030878952 scopus 로고    scopus 로고
    • Geldanamycin-stimulated destabilization of mutated p53 is mediated by the proteasome in vivo
    • Whitesell L, Suthphin P, An W, Schulte T, Blagosklonny M, Neckers L. Geldanamycin-stimulated destabilization of mutated p53 is mediated by the proteasome in vivo. Oncogene 14:2809-2816, 1997.
    • (1997) Oncogene , vol.14 , pp. 2809-2816
    • Whitesell, L.1    Suthphin, P.2    An, W.3    Schulte, T.4    Blagosklonny, M.5    Neckers, L.6
  • 36
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany G, Standaert RF, Lane WAS, Choi S, Corey EJ, Schreiber SL. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 268:726-731, 1995.
    • (1995) Science , vol.268 , pp. 726-731
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.A.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 39
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature(London) 227:680-685, 1970.
    • (1970) Nature(London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 41
    • 0024593798 scopus 로고
    • Inhibition of calpain in intact platelets by the thiol protease inhibitor E-64d
    • McGowan EB, Becker E, Detwiler TC. Inhibition of calpain in intact platelets by the thiol protease inhibitor E-64d. Biochem Biophys Res Commun 158:432-435, 1989.
    • (1989) Biochem Biophys Res Commun , vol.158 , pp. 432-435
    • McGowan, E.B.1    Becker, E.2    Detwiler, T.C.3
  • 42
    • 0026742378 scopus 로고
    • Inhibition of cysteine proteinases in lysosomes and whole cells
    • Wilcox D, Mason RW. Inhibition of cysteine proteinases in lysosomes and whole cells. Biochem J 285:495-502, 1992.
    • (1992) Biochem J , vol.285 , pp. 495-502
    • Wilcox, D.1    Mason, R.W.2
  • 43
    • 0028293250 scopus 로고
    • Comparison of the effect of calpain inhibitors on two extralysosomal Proteinases: The multicatalytic proteinase complex and m-calpain
    • Figueiredo-Pereira ME, Banik N, Wilk S. Comparison of the effect of calpain inhibitors on two extralysosomal Proteinases: The multicatalytic proteinase complex and m-calpain. J Neurochem 62:1989-1994, 1994.
    • (1994) J Neurochem , vol.62 , pp. 1989-1994
    • Figueiredo-Pereira, M.E.1    Banik, N.2    Wilk, S.3
  • 45
    • 0029890020 scopus 로고    scopus 로고
    • Targeted proteolysis of the focal adhesion kinase pp125 FAK during c-MYC-induced apoptosis is suppressed by integrin signalling
    • Crouch DH, Fincham VJ, Frame MC. Targeted proteolysis of the focal adhesion kinase pp125 FAK during c-MYC-induced apoptosis is suppressed by integrin signalling. Oncogene 12:2689-2696, 1996.
    • (1996) Oncogene , vol.12 , pp. 2689-2696
    • Crouch, D.H.1    Fincham, V.J.2    Frame, M.C.3
  • 46
    • 0028988989 scopus 로고
    • V-Src-induced degradation of focal adhesion kinase during morphological transformation of chicken embryo fibroblasts
    • published erratum appears in Oncogene 11:2185, 1995
    • Fincham VJ, Wyke JA, Frame MC. v-Src-induced degradation of focal adhesion kinase during morphological transformation of chicken embryo fibroblasts [published erratum appears in Oncogene 11:2185, 1995]. Oncogene 10:2247-2252, 1995.
    • (1995) Oncogene , vol.10 , pp. 2247-2252
    • Fincham, V.J.1    Wyke, J.A.2    Frame, M.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.