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Volumn 108, Issue 5, 2009, Pages 1289-1299

The basal flux of Akt in the mitochondria is mediated by heat shock protein 90

Author keywords

Akt; Glycogen synthase kinase 3 ; Heat shock protein 90; Insulin like growth factor 1; Mitochondria; Phosphatidylinositol 3 kinase

Indexed keywords

GELDANAMYCIN; HEAT SHOCK PROTEIN 90; NOVOBIOCIN; PROTEIN KINASE B;

EID: 59449096843     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2009.05878.x     Document Type: Article
Times cited : (32)

References (41)
  • 2
    • 0031127305 scopus 로고    scopus 로고
    • Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Bα
    • Alessi D. R., James S. R., Downes C. P., Holmes A. B., Gaffney P. R., Reese C. B. Cohen P. (1997) Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Bα. Curr. Biol. 7, 261 269.
    • (1997) Curr. Biol. , vol.7 , pp. 261-269
    • Alessi, D.R.1    James, S.R.2    Downes, C.P.3    Holmes, A.B.4    Gaffney, P.R.5    Reese, C.B.6    Cohen, P.7
  • 4
    • 0037131187 scopus 로고    scopus 로고
    • Akt forms an intracellular complex with heat shock protein 90 (HSP90) and Cdc37and is destabilized by inhibitors of HSP90 function
    • Basso A. D., Solit D. B., Chiosis G., Giri B., Tsichlis P. Rosen N. (2002) Akt forms an intracellular complex with heat shock protein 90 (HSP90) and Cdc37and is destabilized by inhibitors of HSP90 function. J. Biol. Chem. 277, 39858 39866.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39858-39866
    • Basso, A.D.1    Solit, D.B.2    Chiosis, G.3    Giri, B.4    Tsichlis, P.5    Rosen, N.6
  • 5
    • 34548495803 scopus 로고    scopus 로고
    • Multiple 40-kDa heat-shock protein chaperones function in TOM70-dependent mitochondrial import
    • Bhangoo M. K., Tzankov S., Fan A. C., Dejgaard K., Thomas D. Y. Young J. C. (2007) Multiple 40-kDa heat-shock protein chaperones function in TOM70-dependent mitochondrial import. Mol. Biol. Cell 18, 3414 3428.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3414-3428
    • Bhangoo, M.K.1    Tzankov, S.2    Fan, A.C.3    Dejgaard, K.4    Thomas, D.Y.5    Young, J.C.6
  • 6
    • 0346434149 scopus 로고    scopus 로고
    • Rapid accumulation of Akt in mitochondria following phosphatidylinositol 3-kinase activation
    • Bijur G. N. Jope R. S. (2003) Rapid accumulation of Akt in mitochondria following phosphatidylinositol 3-kinase activation. J. Neurochem. 87, 1427 1435.
    • (2003) J. Neurochem. , vol.87 , pp. 1427-1435
    • Bijur, G.N.1    Jope, R.S.2
  • 7
    • 0034647674 scopus 로고    scopus 로고
    • Translocation of Akt/PKB to the nucleus of osteoblast-like MC3T3-E1 cells exposed to proliferative growth factors
    • Borgatti P., Martelli A. M., Bellacosa A., Casto R., Massari L., Capitani S. Neri L. M. (2000) Translocation of Akt/PKB to the nucleus of osteoblast-like MC3T3-E1 cells exposed to proliferative growth factors. FEBS Lett. 477, 27 32.
    • (2000) FEBS Lett. , vol.477 , pp. 27-32
    • Borgatti, P.1    Martelli, A.M.2    Bellacosa, A.3    Casto, R.4    Massari, L.5    Capitani, S.6    Neri, L.M.7
  • 9
    • 33744953241 scopus 로고    scopus 로고
    • The role of the DIF motif of the DnaJ (HSP40) co-chaperone in the regulation of the DnaK (HSP70) chaperone cycle
    • Cajo G. C., Horne B. E., Kelley W. L., Schwager F., Georgopoulos C. Genevaux P. (2006) The role of the DIF motif of the DnaJ (HSP40) co-chaperone in the regulation of the DnaK (HSP70) chaperone cycle. J. Biol. Chem. 281, 12436 12444.
    • (2006) J. Biol. Chem. , vol.281 , pp. 12436-12444
    • Cajo, G.C.1    Horne, B.E.2    Kelley, W.L.3    Schwager, F.4    Georgopoulos, C.5    Genevaux, P.6
  • 11
    • 33845964416 scopus 로고    scopus 로고
    • HSP90 functions in the targeting and outer membrane translocation steps of TOM70-mediated mitochondrial import
    • Fan A. C., Bhangoo M. K. Young J. C. (2006) HSP90 functions in the targeting and outer membrane translocation steps of TOM70-mediated mitochondrial import. J. Biol. Chem. 281, 33313 33324.
    • (2006) J. Biol. Chem. , vol.281 , pp. 33313-33324
    • Fan, A.C.1    Bhangoo, M.K.2    Young, J.C.3
  • 13
    • 0037155901 scopus 로고    scopus 로고
    • Involvement of HSP90 in signaling and stability of 3-phosphoinositide- dependent kinase-1
    • Fujita N., Sato S., Ishida A. Tsuruo T. (2002) Involvement of HSP90 in signaling and stability of 3-phosphoinositide-dependent kinase-1. J. Biol. Chem. 277, 10346 10353.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10346-10353
    • Fujita, N.1    Sato, S.2    Ishida, A.3    Tsuruo, T.4
  • 14
    • 0037566814 scopus 로고    scopus 로고
    • Tom40, the import channel of the mitochondrial outer membrane, plays an active role in sorting imported proteins
    • Gabriel K., Egan B. Lithgow T. (2003) Tom40, the import channel of the mitochondrial outer membrane, plays an active role in sorting imported proteins. EMBO J. 22, 2380 2386.
    • (2003) EMBO J. , vol.22 , pp. 2380-2386
    • Gabriel, K.1    Egan, B.2    Lithgow, T.3
  • 15
    • 0037200043 scopus 로고    scopus 로고
    • The turn motif is a phosphorylation switch that regulates the binding of HSP70 to protein kinase C
    • Gao T. Newton A. C. (2002) The turn motif is a phosphorylation switch that regulates the binding of HSP70 to protein kinase C. J. Biol. Chem. 277, 31585 31592.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31585-31592
    • Gao, T.1    Newton, A.C.2
  • 16
    • 0033739682 scopus 로고    scopus 로고
    • Membrane potential-driven protein import into mitochondria. the sorting sequence of cytochrome b(2) modulates the Δψ-dependence of translocation of the matrix-targeting sequence
    • Geissler A., Krimmer T., Bömer U., Guiard B., Rassow J. Pfanner N. (2000) Membrane potential-driven protein import into mitochondria. The sorting sequence of cytochrome b(2) modulates the Δψ-dependence of translocation of the matrix-targeting sequence. Mol. Biol. Cell 11, 3977 3991.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3977-3991
    • Geissler, A.1    Krimmer, T.2    Bömer, U.3    Guiard, B.4    Rassow, J.5    Pfanner, N.6
  • 17
    • 0037636369 scopus 로고    scopus 로고
    • Mitochondrial membrane potential regulates matrix configuration and cytochrome c release during apoptosis
    • Gottlieb E., Armour S. M., Harris M. H. Thompson C. B. (2003) Mitochondrial membrane potential regulates matrix configuration and cytochrome c release during apoptosis. Cell Death Differ. 10, 709 717.
    • (2003) Cell Death Differ. , vol.10 , pp. 709-717
    • Gottlieb, E.1    Armour, S.M.2    Harris, M.H.3    Thompson, C.B.4
  • 18
    • 0013936320 scopus 로고
    • Ultrastructural bases for metabolically linked mechanical activity in mitochondria. I. Reversible ultrastructural changes with change in metabolic steady state in isolated liver mitochondria
    • Hackenbrock C. R. (1966) Ultrastructural bases for metabolically linked mechanical activity in mitochondria. I. Reversible ultrastructural changes with change in metabolic steady state in isolated liver mitochondria. J. Cell Biol. 30, 269 297.
    • (1966) J. Cell Biol. , vol.30 , pp. 269-297
    • Hackenbrock, C.R.1
  • 19
    • 0014286720 scopus 로고
    • Ultrastructural bases for metabolically linked mechanical activity in mitochondria. II. Electron transport-linked ultrastructural transformations in mitochondria
    • Hackenbrock C. R. (1968) Ultrastructural bases for metabolically linked mechanical activity in mitochondria. II. Electron transport-linked ultrastructural transformations in mitochondria. J. Cell Biol. 37, 345 369.
    • (1968) J. Cell Biol. , vol.37 , pp. 345-369
    • Hackenbrock, C.R.1
  • 21
    • 35348887850 scopus 로고    scopus 로고
    • Regulation of tumor cell mitochondrial homeostasis by an organelle-specific HSP90 chaperone network
    • Kang B. H., Plescia J., Dohi T., Rosa J., Doxsey S. J. Altieri D. C. (2007) Regulation of tumor cell mitochondrial homeostasis by an organelle-specific HSP90 chaperone network. Cell 131, 257 270.
    • (2007) Cell , vol.131 , pp. 257-270
    • Kang, B.H.1    Plescia, J.2    Dohi, T.3    Rosa, J.4    Doxsey, S.J.5    Altieri, D.C.6
  • 22
    • 0031408095 scopus 로고    scopus 로고
    • The Tim54p-Tim22p complex mediates insertion of proteins into the mitochondrial inner membrane
    • Kerscher O., Holder J., Srinivasan M., Leung R. S. Jensen R. E. (1997) The Tim54p-Tim22p complex mediates insertion of proteins into the mitochondrial inner membrane. J. Cell Biol. 139, 1663 1675.
    • (1997) J. Cell Biol. , vol.139 , pp. 1663-1675
    • Kerscher, O.1    Holder, J.2    Srinivasan, M.3    Leung, R.S.4    Jensen, R.E.5
  • 23
    • 0037454761 scopus 로고    scopus 로고
    • Geldanamycin decreases Raf-1 and Akt levels and induces apoptosis in neuroblastomas
    • Kim S., Kang J., Hu W., Evers B. M. Chung D. H. (2003) Geldanamycin decreases Raf-1 and Akt levels and induces apoptosis in neuroblastomas. Int. J. Cancer 103, 352 359.
    • (2003) Int. J. Cancer , vol.103 , pp. 352-359
    • Kim, S.1    Kang, J.2    Hu, W.3    Evers, B.M.4    Chung, D.H.5
  • 24
    • 0030752305 scopus 로고    scopus 로고
    • Binding of mitochondrial precursor proteins to the cytoplasmic domains of the import receptors TOM70 and TOM20 is determined by cytoplasmic chaperones
    • Komiya T., Rospert S., Schatz G. Mihara K. (1997) Binding of mitochondrial precursor proteins to the cytoplasmic domains of the import receptors TOM70 and TOM20 is determined by cytoplasmic chaperones. EMBO J. 16, 4267 4275.
    • (1997) EMBO J. , vol.16 , pp. 4267-4275
    • Komiya, T.1    Rospert, S.2    Schatz, G.3    Mihara, K.4
  • 25
    • 36349034613 scopus 로고    scopus 로고
    • Cooperation of translocase complexes in mitochondrial protein import
    • Kutik S., Guiard B., Meyer H. E., Wiedemann N. Pfanner N. (2007) Cooperation of translocase complexes in mitochondrial protein import. J. Cell Biol. 179, 585 591.
    • (2007) J. Cell Biol. , vol.179 , pp. 585-591
    • Kutik, S.1    Guiard, B.2    Meyer, H.E.3    Wiedemann, N.4    Pfanner, N.5
  • 26
    • 0141796313 scopus 로고    scopus 로고
    • Mesenchymal stem cells modified with Akt prevent remodeling and restore performance of infarcted hearts
    • Mangi A. A., Noiseux N., Kong D., He H., Rezvani M., Ingwall J. S. Dzau V. J. (2003) Mesenchymal stem cells modified with Akt prevent remodeling and restore performance of infarcted hearts. Nat. Med. 9, 1195 1201.
    • (2003) Nat. Med. , vol.9 , pp. 1195-1201
    • Mangi, A.A.1    Noiseux, N.2    Kong, D.3    He, H.4    Rezvani, M.5    Ingwall, J.S.6    Dzau, V.J.7
  • 27
    • 0034711270 scopus 로고    scopus 로고
    • The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone
    • Marcu M. G., Chadli A., Bouhouche I., Catelli M. Neckers L. M. (2000a) The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone. J. Biol. Chem. 275, 37181 37186.
    • (2000) J. Biol. Chem. , vol.275 , pp. 37181-37186
    • Marcu, M.G.1    Chadli, A.2    Bouhouche, I.3    Catelli, M.4    Neckers, L.M.5
  • 28
    • 0034594644 scopus 로고    scopus 로고
    • Novobiocin and related coumarins and depletion of heat shock protein 90-dependent signaling proteins
    • Marcu M. G., Schulte T. W. Neckers L. (2000b) Novobiocin and related coumarins and depletion of heat shock protein 90-dependent signaling proteins. J. Natl Cancer Inst. 92, 242 248.
    • (2000) J. Natl Cancer Inst. , vol.92 , pp. 242-248
    • Marcu, M.G.1    Schulte, T.W.2    Neckers, L.3
  • 29
    • 0025953614 scopus 로고
    • Role of an energized inner membrane in mitochondrial protein import. Δψ drives the movement of presequences
    • Martin J., Mahlke K. Pfanner N. (1991) Role of an energized inner membrane in mitochondrial protein import. Δψ drives the movement of presequences. J. Biol. Chem. 266, 18051 18057.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18051-18057
    • Martin, J.1    Mahlke, K.2    Pfanner, N.3
  • 30
    • 4444310056 scopus 로고    scopus 로고
    • Heat shock protein-90 dampens and directs signaling stimulated by insulin-like growth factor-1 and insulin
    • Meares G. P., Zmijewska A. A. Jope R. S. (2004) Heat shock protein-90 dampens and directs signaling stimulated by insulin-like growth factor-1 and insulin. FEBS Lett. 574, 181 186.
    • (2004) FEBS Lett. , vol.574 , pp. 181-186
    • Meares, G.P.1    Zmijewska, A.A.2    Jope, R.S.3
  • 31
    • 1842451978 scopus 로고    scopus 로고
    • Transgenic mouse overexpressing the Akt reduced the volume of infarct area after middle cerebral artery occlusion
    • Ohba N., Kiryu-Seo S., Maeda M., Muraoka M., Ishii M. Kiyama H. (2004) Transgenic mouse overexpressing the Akt reduced the volume of infarct area after middle cerebral artery occlusion. Neurosci. Lett. 359, 159 162.
    • (2004) Neurosci. Lett. , vol.359 , pp. 159-162
    • Ohba, N.1    Kiryu-Seo, S.2    Maeda, M.3    Muraoka, M.4    Ishii, M.5    Kiyama, H.6
  • 32
    • 0032541344 scopus 로고    scopus 로고
    • ATP binding and hydrolysis are essential to the function of the HSP90 molecular chaperone in vivo
    • Panaretou B., Prodromou C., Roe S. M., O'Brien R., Ladbury J. E., Piper P. W. Pearl L. H. (1998) ATP binding and hydrolysis are essential to the function of the HSP90 molecular chaperone in vivo. EMBO J. 17, 4829 4836.
    • (1998) EMBO J. , vol.17 , pp. 4829-4836
    • Panaretou, B.1    Prodromou, C.2    Roe, S.M.3    O'Brien, R.4    Ladbury, J.E.5    Piper, P.W.6    Pearl, L.H.7
  • 33
    • 0025008104 scopus 로고
    • Energy requirements for unfolding and membrane translocation of precursor proteins during import into mitochondria
    • Pfanner N., Rassow J., Guiard B., Söllner T., Hartl F. U. Neupert W. (1990) Energy requirements for unfolding and membrane translocation of precursor proteins during import into mitochondria. J. Biol. Chem. 265, 16324 16329.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16324-16329
    • Pfanner, N.1    Rassow, J.2    Guiard, B.3    Söllner, T.4    Hartl, F.U.5    Neupert, W.6
  • 34
    • 34247549679 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and its involvement in cell death and in disease pathogenesis
    • Rasola A. Bernardi P. (2000) The mitochondrial permeability transition pore and its involvement in cell death and in disease pathogenesis. Apoptosis 12, 815 833.
    • (2000) Apoptosis , vol.12 , pp. 815-833
    • Rasola, A.1    Bernardi, P.2
  • 35
    • 0034718540 scopus 로고    scopus 로고
    • Modulation of Akt kinase activity by binding to HSP90
    • Sato S., Fujita N. Tsuruo T. (2000) Modulation of Akt kinase activity by binding to HSP90. Proc. Natl Acad. Sci. USA 97, 10832 10837.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 10832-10837
    • Sato, S.1    Fujita, N.2    Tsuruo, T.3
  • 36
    • 0028064940 scopus 로고
    • Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation
    • Whitesell L., Mimnaugh E. G., De Costa B., Myers C. E. Neckers L. M. (1994) Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation. Proc. Natl Acad. Sci. USA 91, 8324 8328.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    De Costa, B.3    Myers, C.E.4    Neckers, L.M.5
  • 37
    • 0345707575 scopus 로고    scopus 로고
    • The heat shock protein 90 inhibitor geldanamycin and the ErbB inhibitor ZD1839 promote rapid PP1 phosphatase-dependent inactivation of Akt in ErbB2 overexpressing breast cancer cells
    • Xu W., Yuan X., Jung Y. J., Yang Y., Basso A., Rosen N., Chung E. J., Trepel J. Neckers L. (2003) The heat shock protein 90 inhibitor geldanamycin and the ErbB inhibitor ZD1839 promote rapid PP1 phosphatase-dependent inactivation of Akt in ErbB2 overexpressing breast cancer cells. Cancer Res. 63, 7777 7784.
    • (2003) Cancer Res. , vol.63 , pp. 7777-7784
    • Xu, W.1    Yuan, X.2    Jung, Y.J.3    Yang, Y.4    Basso, A.5    Rosen, N.6    Chung, E.J.7    Trepel, J.8    Neckers, L.9
  • 38
    • 1642379534 scopus 로고    scopus 로고
    • Mitochondrial import receptors TOM20 and TOM22 have chaperone-like activity
    • Yano M., Terada K. Mori M. (2004) Mitochondrial import receptors TOM20 and TOM22 have chaperone-like activity. J. Biol. Chem. 279, 10808 10813.
    • (2004) J. Biol. Chem. , vol.279 , pp. 10808-10813
    • Yano, M.1    Terada, K.2    Mori, M.3
  • 39
    • 0037428164 scopus 로고    scopus 로고
    • Molecular chaperones HSP90 and HSP70 deliver preproteins to the mitochondrial import receptor TOM70
    • Young J. C., Hoogenraad N. J. Hartl F. U. (2003) Molecular chaperones HSP90 and HSP70 deliver preproteins to the mitochondrial import receptor TOM70. Cell 112, 41 50.
    • (2003) Cell , vol.112 , pp. 41-50
    • Young, J.C.1    Hoogenraad, N.J.2    Hartl, F.U.3
  • 41
    • 3042656869 scopus 로고    scopus 로고
    • Novobiocin induces a distinct conformation of HSP90 and alters HSP90-cochaperone-client interactions
    • Yun B. G., Huang W., Leach N., Hartson S. D. Matts R. L. (2004) Novobiocin induces a distinct conformation of HSP90 and alters HSP90-cochaperone-client interactions. Biochemistry 43, 8217 8229.
    • (2004) Biochemistry , vol.43 , pp. 8217-8229
    • Yun, B.G.1    Huang, W.2    Leach, N.3    Hartson, S.D.4    Matts, R.L.5


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