메뉴 건너뛰기




Volumn 280, Issue 1, 2002, Pages 45-54

Unique behavior of a Dictyostelium homologue of TRAP-1, coupling with differentiation of D. discoideum cells

Author keywords

Actin; Development; Dictyostelium; HSP90; Mitochondria; TRAP1

Indexed keywords

F ACTIN; HEAT SHOCK PROTEIN 90; PHALLOIDIN; PROTEIN ANTIBODY; PROTOZOAL PROTEIN; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED PROTEIN 1; UNCLASSIFIED DRUG;

EID: 0036035152     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.2002.5620     Document Type: Article
Times cited : (23)

References (32)
  • 1
    • 0031873752 scopus 로고    scopus 로고
    • The 90-kDa molecular chaperone family: Structure, function, and clinical applications. A comprehensive review
    • Csermely, P., Schnaider, T., Soti, C., Prohaszka, Z., and Nardai, G. (1998). The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review. Pharmacol. Ther. 79, 129-168.
    • (1998) Pharmacol. Ther. , vol.79 , pp. 129-168
    • Csermely, P.1    Schnaider, T.2    Soti, C.3    Prohaszka, Z.4    Nardai, G.5
  • 2
    • 0032569851 scopus 로고    scopus 로고
    • Hsp90 as a capacitor for morphological evolution
    • Rutherford, S. L, and Lindquist, S. (1998). Hsp90 as a capacitor for morphological evolution. Nature 396, 336-342.
    • (1998) Nature , vol.396 , pp. 336-342
    • Rutherford, S.L.1    Lindquist, S.2
  • 3
    • 0028954475 scopus 로고
    • Identification of a protein with homology to hsp90 that binds the type 1 tumor necrosis factor receptor
    • Song, H. Y., Dunbar, J. D., Zhang, Y. X., Guo, D., and Donner, D. B. (1995). Identification of a protein with homology to hsp90 that binds the type 1 tumor necrosis factor receptor. J. Biol. Chem. 270, 3574-3581.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3574-3581
    • Song, H.Y.1    Dunbar, J.D.2    Zhang, Y.X.3    Guo, D.4    Donner, D.B.5
  • 4
    • 0029760873 scopus 로고    scopus 로고
    • A new member of the hsp90 family of molecular chaperones interacts with the retinoblastoma protein during mitosis and after heat shock
    • Chen, C. F., Chen, Y., Dai, K., Chen, P. L., Riley, D. J., and Lee, W. H. (1996). A new member of the hsp90 family of molecular chaperones interacts with the retinoblastoma protein during mitosis and after heat shock. Mol. Cell. Biol. 16, 4691-4699.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4691-4699
    • Chen, C.F.1    Chen, Y.2    Dai, K.3    Chen, P.L.4    Riley, D.J.5    Lee, W.H.6
  • 5
    • 0032718876 scopus 로고    scopus 로고
    • A direct interaction between EXT proteins and glycosyltransferases is defective in hereditary multiple exostoses
    • Simmons, A. D., Musy, M. M., Lopes, C. S., Hwang, L. Y., Yang, Y., and Lovett, M. (1999). A direct interaction between EXT proteins and glycosyltransferases is defective in hereditary multiple exostoses. Hum. Mol. Genet. 8, 2155-2164.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 2155-2164
    • Simmons, A.D.1    Musy, M.M.2    Lopes, C.S.3    Hwang, L.Y.4    Yang, Y.5    Lovett, M.6
  • 6
    • 0034724389 scopus 로고    scopus 로고
    • Expression analysis with oligonucleotide microarrays reveals that MYC regulates genes involved in growth, cell cycle, signaling, and adhesion
    • Golub, T. R. (2000). Expression analysis with oligonucleotide microarrays reveals that MYC regulates genes involved in growth, cell cycle, signaling, and adhesion. Proc. Natl. Acad. Sci. USA 97, 3260-3265.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3260-3265
    • Golub, T.R.1
  • 7
    • 0034633963 scopus 로고    scopus 로고
    • Immunoelectron microscopy provides evidence that tumor necrosis factor receptor-associated protein 1 (TRAP-1) is a mitochondrial protein which also localizes at specific extramitochondrial sites
    • Cechetto, J. D., and Gupta, R. S. (2000). Immunoelectron microscopy provides evidence that tumor necrosis factor receptor-associated protein 1 (TRAP-1) is a mitochondrial protein which also localizes at specific extramitochondrial sites. Exp. Cell Res. 260, 30-39.
    • (2000) Exp. Cell Res. , vol.260 , pp. 30-39
    • Cechetto, J.D.1    Gupta, R.S.2
  • 8
    • 0024388197 scopus 로고
    • Transition of starving Dictyostelium cells to differentiation phase at a particular position of the cell cycle
    • Maeda, Y., Ohmori, T., Abe, T., Abe, F., and Amagai, A. (1989). Transition of starving Dictyostelium cells to differentiation phase at a particular position of the cell cycle. Differentiation 41, 169-175.
    • (1989) Differentiation , vol.41 , pp. 169-175
    • Maeda, Y.1    Ohmori, T.2    Abe, T.3    Abe, F.4    Amagai, A.5
  • 9
    • 84957380101 scopus 로고
    • Evidence for the formation of cell aggregates by chemotaxis in the development of the cellular slime mold Dictyostelium discoideum
    • Bonner, J. T. (1947). Evidence for the formation of cell aggregates by chemotaxis in the development of the cellular slime mold Dictyostelium discoideum. J. Exp. Zool. 106, 1-26.
    • (1947) J. Exp. Zool. , vol.106 , pp. 1-26
    • Bonner, J.T.1
  • 10
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith, D. B., and Johnson, K. S. (1988). Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67, 31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 11
    • 0015197418 scopus 로고
    • Isolation and characterization of a prespore specific structure of the cellular slime mold. Dictyostelium discoideum
    • Ikeda, T., and Takeuchi, I. (1971). Isolation and characterization of a prespore specific structure of the cellular slime mold, Dictyostelium discoideum. Dev. Growth Differ. 13, 221-229.
    • (1971) Dev. Growth Differ. , vol.13 , pp. 221-229
    • Ikeda, T.1    Takeuchi, I.2
  • 12
    • 0021438842 scopus 로고
    • Chemoattractant-mediated changes in cytoskeletal actin of cellular slime moulds
    • McRobbie, S. J., and Newell, P. C. (1984). Chemoattractant-mediated changes in cytoskeletal actin of cellular slime moulds. J. Cell Sci. 68, 139-151.
    • (1984) J. Cell Sci. , vol.68 , pp. 139-151
    • McRobbie, S.J.1    Newell, P.C.2
  • 13
    • 0024688488 scopus 로고
    • Survey of amino-terminal proteolytic cleavage sites in mitochondrial precursor proteins: Leader peptides cleaved by two matrix proteases share a three-amino acid motif
    • Hendrick, J. P., Hodges, P. E., and Rosenberg, L. E. (1989). Survey of amino-terminal proteolytic cleavage sites in mitochondrial precursor proteins: Leader peptides cleaved by two matrix proteases share a three-amino acid motif. Proc. Natl. Acad. Sci. USA 86, 4056-4060.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4056-4060
    • Hendrick, J.P.1    Hodges, P.E.2    Rosenberg, L.E.3
  • 14
    • 0032972509 scopus 로고    scopus 로고
    • PSORT: A program for detecting sorting signals in proteins and predicting their subcellular localization
    • Nakai, K., and Horton, P. (1999). PSORT: a program for detecting sorting signals in proteins and predicting their subcellular localization. Trends Biochem. Sci. 24, 34-36.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 34-36
    • Nakai, K.1    Horton, P.2
  • 15
    • 0034603178 scopus 로고    scopus 로고
    • The hsp90-related protein TRAP1 is a mitochondrial protein with distinct functional properties
    • Felts, S. J., Owen, B. A., Nguyen, P., Trepel, J., Donner, D. B., and Toft, D. O. (2000). The hsp90-related protein TRAP1 is a mitochondrial protein with distinct functional properties. J. Biol. Chem. 275, 3305-3312.
    • (2000) J. Biol. Chem. , vol.275 , pp. 3305-3312
    • Felts, S.J.1    Owen, B.A.2    Nguyen, P.3    Trepel, J.4    Donner, D.B.5    Toft, D.O.6
  • 16
    • 0026092879 scopus 로고
    • Structure, expression, and regulation of members of the developmentally controlled V and H gene classes from Dictyostelium
    • Singleton, C. K., Delude, R. L., Ken, R., Manning, S. S., and McPherson, C. E. (1991). Structure, expression, and regulation of members of the developmentally controlled V and H gene classes from Dictyostelium. Dev. Genet. 12, 88-97.
    • (1991) Dev. Genet. , vol.12 , pp. 88-97
    • Singleton, C.K.1    Delude, R.L.2    Ken, R.3    Manning, S.S.4    McPherson, C.E.5
  • 17
    • 0031670169 scopus 로고    scopus 로고
    • Spatiotemporal dynamics of actin concentration during cytokinesis and locomotion in Dictyostelium
    • Yumura, S., and Fukui, Y. (1998). Spatiotemporal dynamics of actin concentration during cytokinesis and locomotion in Dictyostelium. J. Cell Sci. 111, 2097-2108.
    • (1998) J. Cell Sci. , vol.111 , pp. 2097-2108
    • Yumura, S.1    Fukui, Y.2
  • 18
    • 0034102883 scopus 로고    scopus 로고
    • The actin cytoskeleton of Dictyostelium: A story told by mutants
    • Noegel, A. A., and Schleicher, M. (2000). The actin cytoskeleton of Dictyostelium: A story told by mutants. J. Cell Sci. 113, 759-766.
    • (2000) J. Cell Sci. , vol.113 , pp. 759-766
    • Noegel, A.A.1    Schleicher, M.2
  • 19
    • 0034804337 scopus 로고    scopus 로고
    • Reduced protein diffusion rate by cytoskeleton in vegetative and polarized Dictyostelium cells
    • Potma, E. O., de Boeij, W. P., Bosgraaf, L, Roelofs, J., van Haastert, P. J., and Wiersma, D. A. (2001). Reduced protein diffusion rate by cytoskeleton in vegetative and polarized Dictyostelium cells. Biophys. J. 81, 2010-2019.
    • (2001) Biophys. J. , vol.81 , pp. 2010-2019
    • Potma, E.O.1    De Boeij, W.P.2    Bosgraaf, L.3    Roelofs, J.4    Van Haastert, P.J.5    Wiersma, D.A.6
  • 20
    • 0026576609 scopus 로고
    • A density-sensing factor controls development in Dictyostelium
    • Jain, R., Yuen, I. S., Taphouse, C. R., and Gomer, R. H. (1992). A density-sensing factor controls development in Dictyostelium. Genes Dev. 6, 390-400.
    • (1992) Genes Dev. , vol.6 , pp. 390-400
    • Jain, R.1    Yuen, I.S.2    Taphouse, C.R.3    Gomer, R.H.4
  • 21
    • 0033180415 scopus 로고    scopus 로고
    • A cell-counting factor regulating structure size in Dictyostelium
    • Brock, D. A., and Gomer, R. H. (1999). A cell-counting factor regulating structure size in Dictyostelium. Genes Dev. 13, 1960-1969.
    • (1999) Genes Dev. , vol.13 , pp. 1960-1969
    • Brock, D.A.1    Gomer, R.H.2
  • 22
    • 0033133729 scopus 로고    scopus 로고
    • Mitochondrial-matrix proteins at unexpected locations: Are they exported?
    • Soltys, B. J., and Gupta, R. S. (1999). Mitochondrial-matrix proteins at unexpected locations: Are they exported? Trends Biochem. Sci. 24, 174-177.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 174-177
    • Soltys, B.J.1    Gupta, R.S.2
  • 23
    • 0023789673 scopus 로고
    • The molecular mobility of alpha-actinin and actin in a reconstituted model of gelation
    • Simon, J. R., Furukawa, R. H., Ware, B. R., and Taylor, D. L. (1988). The molecular mobility of alpha-actinin and actin in a reconstituted model of gelation. Cell Motil. Cytoskeleton 11, 64-82.
    • (1988) Cell Motil. Cytoskeleton , vol.11 , pp. 64-82
    • Simon, J.R.1    Furukawa, R.H.2    Ware, B.R.3    Taylor, D.L.4
  • 24
    • 0026478716 scopus 로고
    • Structure of hisactophilin is similar to interleukin-1 beta and fibroblast growth factor
    • Habazettl, J., Gondol, D., Wiltscheck, R., Otlewski, J., Schleicher, M., and Holak, T. A. (1992). Structure of hisactophilin is similar to interleukin-1 beta and fibroblast growth factor. Nature 359, 855-858.
    • (1992) Nature , vol.359 , pp. 855-858
    • Habazettl, J.1    Gondol, D.2    Wiltscheck, R.3    Otlewski, J.4    Schleicher, M.5    Holak, T.A.6
  • 25
    • 0029020353 scopus 로고
    • pH regulation of the F-actin binding properties of Dictyostelium elongation factor 1 alpha
    • Edmonds, B. T., Murray, J., and Condeelis, J. (1995). pH regulation of the F-actin binding properties of Dictyostelium elongation factor 1 alpha. J. Biol. Chem. 270, 15222-15230.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15222-15230
    • Edmonds, B.T.1    Murray, J.2    Condeelis, J.3
  • 27
    • 0025778706 scopus 로고
    • Cytoplasmic 8 S glucocorticoid receptor binds to actin filaments through the 90-kDa heat shock protein moiety
    • Miyata, Y., and Yahara, I. (1991). Cytoplasmic 8 S glucocorticoid receptor binds to actin filaments through the 90-kDa heat shock protein moiety. J. Biol. Chem. 266, 8779-8783.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8779-8783
    • Miyata, Y.1    Yahara, I.2
  • 28
    • 0034019417 scopus 로고    scopus 로고
    • Alteration of the glucocorticoid receptor sub-cellular localization by non steroidal compounds
    • Prima, V., Depoix, C., Masselot, B., Formstecher, P., and Lefebvre, P. (2000). Alteration of the glucocorticoid receptor sub-cellular localization by non steroidal compounds. J. Steroid Biochem. Mol. Biol. 72, 1-12.
    • (2000) J. Steroid Biochem. Mol. Biol. , vol.72 , pp. 1-12
    • Prima, V.1    Depoix, C.2    Masselot, B.3    Formstecher, P.4    Lefebvre, P.5
  • 29
    • 0035213530 scopus 로고    scopus 로고
    • Bax and other pro-apoptotic Bcl-2 family "killer-proteins" and their victim the mitochondrion
    • Antonsson, B. (2001). Bax and other pro-apoptotic Bcl-2 family "killer-proteins" and their victim the mitochondrion. Cell Tissue Res. 306, 347-361.
    • (2001) Cell Tissue Res. , vol.306 , pp. 347-361
    • Antonsson, B.1
  • 31
    • 0032740301 scopus 로고    scopus 로고
    • Transient expression of a mitochondrial gene cluster including rps4 is essential for the phase-shift of Dictyostelium cells from growth to differentiation
    • Inazu, Y., Chae, S. C., and Maeda, Y. (1999). Transient expression of a mitochondrial gene cluster including rps4 is essential for the phase-shift of Dictyostelium cells from growth to differentiation. Dev. Genet. 25, 339-352.
    • (1999) Dev. Genet. , vol.25 , pp. 339-352
    • Inazu, Y.1    Chae, S.C.2    Maeda, Y.3
  • 32
    • 0035809177 scopus 로고    scopus 로고
    • Tortoise, a novel mitochondrial protein, is required for directional responses of Dictyostelium in chemotactic gradients
    • Van Es, S., Wessels, D., Soll, D. R., Borleis, J., and Devreotes, P. N. (2001). Tortoise, a novel mitochondrial protein, is required for directional responses of Dictyostelium in chemotactic gradients. J. Cell. Biol. 152, 621-632.
    • (2001) J. Cell. Biol. , vol.152 , pp. 621-632
    • Van Es, S.1    Wessels, D.2    Soll, D.R.3    Borleis, J.4    Devreotes, P.N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.