메뉴 건너뛰기




Volumn 1784, Issue 12, 2008, Pages 2045-2051

Nucleotide-dependent self-assembly of Nucleoside Diphosphate Kinase (NDPK) in vitro

Author keywords

Filament; NDPK; Polymerization; Self assembly

Indexed keywords

GUANOSINE TRIPHOSPHATE; HISTIDINE; NUCLEOSIDE DIPHOSPHATE KINASE; NUCLEOTIDE; POLYMER;

EID: 54549122356     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.07.011     Document Type: Article
Times cited : (8)

References (43)
  • 1
    • 0017873959 scopus 로고
    • Nucleoside diphosphokinase from human erythrocytes
    • Agarwal R.P., Robison B., and Parks R.E. Nucleoside diphosphokinase from human erythrocytes. Methods Enzymol. 51 (1978) 376-386
    • (1978) Methods Enzymol. , vol.51 , pp. 376-386
    • Agarwal, R.P.1    Robison, B.2    Parks, R.E.3
  • 2
    • 0029970190 scopus 로고    scopus 로고
    • Differential gene expression in tumor metastasis: Nm23
    • Freije J.M., MacDonald N.J., and Steeg P.S. Differential gene expression in tumor metastasis: Nm23. Curr. Top. Microbio. Immuno. 213 Pt 2 (1996) 215-232
    • (1996) Curr. Top. Microbio. Immuno. , vol.213 , Issue.PART 2 , pp. 215-232
    • Freije, J.M.1    MacDonald, N.J.2    Steeg, P.S.3
  • 3
    • 0031600391 scopus 로고    scopus 로고
    • Nm23 and tumour metastasis: basic and translational advances
    • Freije J.M., MacDonald N.J., and Steeg P.S. Nm23 and tumour metastasis: basic and translational advances. Biochem. Soc. Symp. 63 (1998) 261-271
    • (1998) Biochem. Soc. Symp. , vol.63 , pp. 261-271
    • Freije, J.M.1    MacDonald, N.J.2    Steeg, P.S.3
  • 4
    • 0037870267 scopus 로고    scopus 로고
    • Nucleoside diphosphate kinases in mammalian signal transduction systems: recent development and perspective
    • Kimura N., Shimada N., Ishijima Y., Fukuda M., Takagi Y., and Ishikawa N. Nucleoside diphosphate kinases in mammalian signal transduction systems: recent development and perspective. J. Bioenerg. Biomembr. 35 (2003) 41-47
    • (2003) J. Bioenerg. Biomembr. , vol.35 , pp. 41-47
    • Kimura, N.1    Shimada, N.2    Ishijima, Y.3    Fukuda, M.4    Takagi, Y.5    Ishikawa, N.6
  • 5
    • 0027193360 scopus 로고
    • Inhibition of cell motility after nm23 transfection of human and murine tumor cells
    • Kantor J.D., McCormick B., Steeg P.S., and Zetter B.R. Inhibition of cell motility after nm23 transfection of human and murine tumor cells. Cancer Res. 53 (1993) 1971-1973
    • (1993) Cancer Res. , vol.53 , pp. 1971-1973
    • Kantor, J.D.1    McCormick, B.2    Steeg, P.S.3    Zetter, B.R.4
  • 6
    • 0031041899 scopus 로고    scopus 로고
    • Site-directed mutation of Nm23-H1. Mutations lacking motility suppressive capacity upon transfection are deficient in histidine-dependent protein phosphotransferase pathways in vitro
    • Freije J.M., Blay P., MacDonald N.J., Manrow R.E., and Steeg P.S. Site-directed mutation of Nm23-H1. Mutations lacking motility suppressive capacity upon transfection are deficient in histidine-dependent protein phosphotransferase pathways in vitro. J. Biol. Chem. 272 (1997) 5525-5532
    • (1997) J. Biol. Chem. , vol.272 , pp. 5525-5532
    • Freije, J.M.1    Blay, P.2    MacDonald, N.J.3    Manrow, R.E.4    Steeg, P.S.5
  • 7
    • 40349106023 scopus 로고    scopus 로고
    • Awd, the homolog of metastasis suppressor gene Nm23, regulates Drosophila epithelial cell invasion
    • Nallamothu G., Woolworth J.A., Dammai V., and Hsu T. Awd, the homolog of metastasis suppressor gene Nm23, regulates Drosophila epithelial cell invasion. Mol. Cell. Biol. 28 (2008) 1964-1973
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 1964-1973
    • Nallamothu, G.1    Woolworth, J.A.2    Dammai, V.3    Hsu, T.4
  • 8
    • 0344442763 scopus 로고    scopus 로고
    • Drosophila awd, the homolog of human nm23, regulates FGF receptor levels and functions synergistically with shi/dynamin during tracheal development
    • Dammai V., Adryan B., Lavenburg K.R., and Hsu T. Drosophila awd, the homolog of human nm23, regulates FGF receptor levels and functions synergistically with shi/dynamin during tracheal development. Genes Dev. 17 (2003) 2812-2824
    • (2003) Genes Dev. , vol.17 , pp. 2812-2824
    • Dammai, V.1    Adryan, B.2    Lavenburg, K.R.3    Hsu, T.4
  • 10
    • 0038546525 scopus 로고    scopus 로고
    • Regulation of dynamin by nucleoside diphosphate kinase
    • Narayanan R., and Ramaswami M. Regulation of dynamin by nucleoside diphosphate kinase. J. Bioenerg. Biomembr. 35 (2003) 49-55
    • (2003) J. Bioenerg. Biomembr. , vol.35 , pp. 49-55
    • Narayanan, R.1    Ramaswami, M.2
  • 11
    • 0036701910 scopus 로고    scopus 로고
    • Dynamin and endocytosis
    • Sever S. Dynamin and endocytosis. Curr. Opin. Cell Biol. 14 (2002) 463-467
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 463-467
    • Sever, S.1
  • 12
    • 0036902709 scopus 로고    scopus 로고
    • ARF6-GTP recruits Nm23-H1 to facilitate dynamin-mediated endocytosis during adherens junctions disassembly
    • Palacios F., Schweitzer J.K., Boshans R.L., and D'Souza-Schorey C. ARF6-GTP recruits Nm23-H1 to facilitate dynamin-mediated endocytosis during adherens junctions disassembly. Nat. Cell Biol. 4 (2002) 929-936
    • (2002) Nat. Cell Biol. , vol.4 , pp. 929-936
    • Palacios, F.1    Schweitzer, J.K.2    Boshans, R.L.3    D'Souza-Schorey, C.4
  • 13
    • 0021142850 scopus 로고
    • The microtubule-associated nucleoside diphosphate kinase
    • Nickerson J.A., and Wells W.W. The microtubule-associated nucleoside diphosphate kinase. J. Biol. Chem. 259 (1984) 11297-11304
    • (1984) J. Biol. Chem. , vol.259 , pp. 11297-11304
    • Nickerson, J.A.1    Wells, W.W.2
  • 14
    • 0018522038 scopus 로고
    • Tubulin-associated nucleoside diphosphokinase
    • Jacobs M., and Huitorel P. Tubulin-associated nucleoside diphosphokinase. Eur. J. Biochem. / FEBS 99 (1979) 613-622
    • (1979) Eur. J. Biochem. / FEBS , vol.99 , pp. 613-622
    • Jacobs, M.1    Huitorel, P.2
  • 15
    • 0017643539 scopus 로고
    • Nucleotide binding and phosphorylation in microtubule assembly in vitro
    • Penningroth S.M., and Kirschner M.W. Nucleotide binding and phosphorylation in microtubule assembly in vitro. J. Mol. Biol. 115 (1977) 643-673
    • (1977) J. Mol. Biol. , vol.115 , pp. 643-673
    • Penningroth, S.M.1    Kirschner, M.W.2
  • 16
    • 0022410912 scopus 로고
    • Microtubules and nucleoside diphosphate kinase. Nucleoside diphosphate kinase binds to co-purifying contaminants rather than to microtubule proteins
    • Islam K., and Burns R.G. Microtubules and nucleoside diphosphate kinase. Nucleoside diphosphate kinase binds to co-purifying contaminants rather than to microtubule proteins. Biochem. J. 232 (1985) 651-656
    • (1985) Biochem. J. , vol.232 , pp. 651-656
    • Islam, K.1    Burns, R.G.2
  • 17
    • 0026326968 scopus 로고
    • Activation of a small GTP-binding protein by nucleoside diphosphate kinase
    • Randazzo P.A., Northup J.K., and Kahn R.A. Activation of a small GTP-binding protein by nucleoside diphosphate kinase. Science 254 (1991) 850-853
    • (1991) Science , vol.254 , pp. 850-853
    • Randazzo, P.A.1    Northup, J.K.2    Kahn, R.A.3
  • 18
    • 0026759873 scopus 로고
    • Nucleoside diphosphate kinase: conclusions withdrawn
    • Randazzo P.A., Kahn R.A., and Northup J.K. Nucleoside diphosphate kinase: conclusions withdrawn. Science 257 (1992) 862
    • (1992) Science , vol.257 , pp. 862
    • Randazzo, P.A.1    Kahn, R.A.2    Northup, J.K.3
  • 19
    • 0033805226 scopus 로고    scopus 로고
    • NM23/nucleoside diphosphate kinase and signal transduction
    • Otero A.S. NM23/nucleoside diphosphate kinase and signal transduction. J. Bioenerg. Biomembr. 32 (2000) 269-275
    • (2000) J. Bioenerg. Biomembr. , vol.32 , pp. 269-275
    • Otero, A.S.1
  • 20
    • 0026713312 scopus 로고
    • Regulatory GTP-binding proteins (ADP-ribosylation factor, Gt, and RAS) are not activated directly by nucleoside diphosphate kinase
    • Randazzo P.A., Northup J.K., and Kahn R.A. Regulatory GTP-binding proteins (ADP-ribosylation factor, Gt, and RAS) are not activated directly by nucleoside diphosphate kinase. J. Biol. Chem. 267 (1992) 18182-18189
    • (1992) J. Biol. Chem. , vol.267 , pp. 18182-18189
    • Randazzo, P.A.1    Northup, J.K.2    Kahn, R.A.3
  • 22
    • 3142709440 scopus 로고    scopus 로고
    • Lbc proto-oncogene product binds to and could be negatively regulated by metastasis suppressor nm23-H2
    • Iwashita S., Fujii M., Mukai H., Ono Y., and Miyamoto M. Lbc proto-oncogene product binds to and could be negatively regulated by metastasis suppressor nm23-H2. Biochem. Biophys. Res. Commun. 320 (2004) 1063-1068
    • (2004) Biochem. Biophys. Res. Commun. , vol.320 , pp. 1063-1068
    • Iwashita, S.1    Fujii, M.2    Mukai, H.3    Ono, Y.4    Miyamoto, M.5
  • 24
    • 0037036371 scopus 로고    scopus 로고
    • Integrin cytoplasmic domain-associated protein 1alpha (ICAP-1alpha ) interacts directly with the metastasis suppressor nm23-H2, and both proteins are targeted to newly formed cell adhesion sites upon integrin engagement
    • Fournier H.N., Dupe-Manet S., Bouvard D., Lacombe M.L., Marie C., Block M.R., and Albiges-Rizo C. Integrin cytoplasmic domain-associated protein 1alpha (ICAP-1alpha ) interacts directly with the metastasis suppressor nm23-H2, and both proteins are targeted to newly formed cell adhesion sites upon integrin engagement. J. Biol. Chem. 277 (2002) 20895-20902
    • (2002) J. Biol. Chem. , vol.277 , pp. 20895-20902
    • Fournier, H.N.1    Dupe-Manet, S.2    Bouvard, D.3    Lacombe, M.L.4    Marie, C.5    Block, M.R.6    Albiges-Rizo, C.7
  • 25
    • 0037166288 scopus 로고    scopus 로고
    • Interactions of phocein with nucleoside-diphosphate kinase, Eps15, and Dynamin I
    • Baillat G., Gaillard S., Castets F., and Monneron A. Interactions of phocein with nucleoside-diphosphate kinase, Eps15, and Dynamin I. J. Biol. Chem. 277 (2002) 18961-18966
    • (2002) J. Biol. Chem. , vol.277 , pp. 18961-18966
    • Baillat, G.1    Gaillard, S.2    Castets, F.3    Monneron, A.4
  • 26
    • 0037452537 scopus 로고    scopus 로고
    • A molecular motor or a regulator? Dynamin's in a class of its own
    • Song B.D., and Schmid S.L. A molecular motor or a regulator? Dynamin's in a class of its own. Biochemistry 42 (2003) 1369-1376
    • (2003) Biochemistry , vol.42 , pp. 1369-1376
    • Song, B.D.1    Schmid, S.L.2
  • 29
    • 12844249950 scopus 로고    scopus 로고
    • Nm23H2 facilitates Coat Protein II assembly and endoplasmic reticulum export in mammalian cells
    • Kapetanovich L., Baughman C., and Lee T.H. Nm23H2 facilitates Coat Protein II assembly and endoplasmic reticulum export in mammalian cells. Mol. Biol. Cell 16 (2005) 835-848
    • (2005) Mol. Biol. Cell , vol.16 , pp. 835-848
    • Kapetanovich, L.1    Baughman, C.2    Lee, T.H.3
  • 30
    • 0037150118 scopus 로고    scopus 로고
    • Structure-based mutational and functional analysis identify human NM23-H2 as a multifunctional enzyme
    • Postel E.H., Abramczyk B.A., Gursky S.K., and Xu Y. Structure-based mutational and functional analysis identify human NM23-H2 as a multifunctional enzyme. Biochemistry 41 (2002) 6330-6337
    • (2002) Biochemistry , vol.41 , pp. 6330-6337
    • Postel, E.H.1    Abramczyk, B.A.2    Gursky, S.K.3    Xu, Y.4
  • 31
    • 0033795931 scopus 로고    scopus 로고
    • The catalytic mechanism of nucleoside diphosphate kinases
    • Lascu I., and Gonin P. The catalytic mechanism of nucleoside diphosphate kinases. J. Bioenerg. Biomembr. 32 (2000) 237-246
    • (2000) J. Bioenerg. Biomembr. , vol.32 , pp. 237-246
    • Lascu, I.1    Gonin, P.2
  • 34
    • 0016796444 scopus 로고
    • The reconstitution of microtubules from purified calf brain tubulin
    • Lee J.C., and Timasheff S.N. The reconstitution of microtubules from purified calf brain tubulin. Biochemistry 14 (1975) 5183-5187
    • (1975) Biochemistry , vol.14 , pp. 5183-5187
    • Lee, J.C.1    Timasheff, S.N.2
  • 35
    • 0016813649 scopus 로고
    • Ionic and nucleotide requirements for microtubule polymerization in vitro
    • Olmsted J.B., and Borisy G.G. Ionic and nucleotide requirements for microtubule polymerization in vitro. Biochemistry 14 (1975) 2996-3005
    • (1975) Biochemistry , vol.14 , pp. 2996-3005
    • Olmsted, J.B.1    Borisy, G.G.2
  • 36
    • 0017201915 scopus 로고
    • Tubulin-nucleotide interactions during the polymerization and depolymerization of microtubules
    • Weisenberg R.C., Deery W.J., and Dickinson P.J. Tubulin-nucleotide interactions during the polymerization and depolymerization of microtubules. Biochemistry 15 (1976) 4248-4254
    • (1976) Biochemistry , vol.15 , pp. 4248-4254
    • Weisenberg, R.C.1    Deery, W.J.2    Dickinson, P.J.3
  • 37
    • 0032518656 scopus 로고    scopus 로고
    • Dynamic assembly of FtsZ regulated by GTP hydrolysis
    • Mukherjee A., and Lutkenhaus J. Dynamic assembly of FtsZ regulated by GTP hydrolysis. EMBO J. 17 (1998) 462-469
    • (1998) EMBO J. , vol.17 , pp. 462-469
    • Mukherjee, A.1    Lutkenhaus, J.2
  • 39
    • 0029154302 scopus 로고
    • Mechanism of phosphate transfer by nucleoside diphosphate kinase: X-ray structures of the phosphohistidine intermediate of the enzymes from Drosophila and Dictyostelium
    • Morera S., Chiadmi M., LeBras G., Lascu I., and Janin J. Mechanism of phosphate transfer by nucleoside diphosphate kinase: X-ray structures of the phosphohistidine intermediate of the enzymes from Drosophila and Dictyostelium. Biochemistry 34 (1995) 11062-11070
    • (1995) Biochemistry , vol.34 , pp. 11062-11070
    • Morera, S.1    Chiadmi, M.2    LeBras, G.3    Lascu, I.4    Janin, J.5
  • 40
    • 0025612249 scopus 로고
    • A Drosophila gene that is homologous to a mammalian gene associated with tumor metastasis codes for a nucleoside diphosphate kinase
    • Biggs J., Hersperger E., Steeg P.S., Liotta L.A., and Shearn A. A Drosophila gene that is homologous to a mammalian gene associated with tumor metastasis codes for a nucleoside diphosphate kinase. Cell 63 (1990) 933-940
    • (1990) Cell , vol.63 , pp. 933-940
    • Biggs, J.1    Hersperger, E.2    Steeg, P.S.3    Liotta, L.A.4    Shearn, A.5
  • 42
    • 0030965158 scopus 로고    scopus 로고
    • Copurification of vimentin, energy metabolism enzymes, and a MER5 homolog with nucleoside diphosphate kinase. Identification of tissue-specific interactions
    • Otero A.S. Copurification of vimentin, energy metabolism enzymes, and a MER5 homolog with nucleoside diphosphate kinase. Identification of tissue-specific interactions. J. Biol. Chem. 272 (1997) 14690-14694
    • (1997) J. Biol. Chem. , vol.272 , pp. 14690-14694
    • Otero, A.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.