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Volumn 270, Issue 24, 2003, Pages 4962-4972

A 49 kDa microtubule cross-linking protein from Artemia franciscana is a coenzyme A-transferase

Author keywords

Artemia franciscana; CoA transferase; Microtubule cross linking protein

Indexed keywords

4 HYDROXYBUTYRATE COENZYME A TRANSFERASE; COENZYME A TRANSFERASE; COMPLEMENTARY DNA; GENE PRODUCT; GLUTACONATE COENZYME A TRANSFERASE; OLIGONUCLEOTIDE; PROTEIN CG7920; PROTEIN P49; UNCLASSIFIED DRUG;

EID: 0346880108     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03898.x     Document Type: Article
Times cited : (10)

References (42)
  • 2
    • 0036010599 scopus 로고    scopus 로고
    • Toward reconstitution of in vivo microtubule dynamics in vitro
    • Andersen, S.S.L. & Wittmann, T. (2002) Toward reconstitution of in vivo microtubule dynamics in vitro. Bioessays 24, 305-307.
    • (2002) Bioessays , vol.24 , pp. 305-307
    • Andersen, S.S.L.1    Wittmann, T.2
  • 3
    • 0037452096 scopus 로고    scopus 로고
    • Dynamics and mechanics of the microtubule plus end
    • Howard, J. & Hyman, A.A. (2003) Dynamics and mechanics of the microtubule plus end. Nature 422, 753-758.
    • (2003) Nature , vol.422 , pp. 753-758
    • Howard, J.1    Hyman, A.A.2
  • 4
    • 0037219233 scopus 로고    scopus 로고
    • The two a-tubulin isotypes in budding yeast have opposing effects on microtubule dynamics in vitro
    • Bode, C.J., Gupta, M.L. Jr, Suprenant, K.A. & Himes, R.H. (2003) The two a-tubulin isotypes in budding yeast have opposing effects on microtubule dynamics in vitro. EMBO Rep. 4, 94-99.
    • (2003) EMBO Rep. , vol.4 , pp. 94-99
    • Bode, C.J.1    Gupta Jr., M.L.2    Suprenant, K.A.3    Himes, R.H.4
  • 5
    • 0037413708 scopus 로고    scopus 로고
    • Repeat motifs of tau bind to the insides of microtubules in the absence of taxol
    • Kar, S., Fan, J., Smith, M.J., Goedert, M. & Amos, L.A. (2003) Repeat motifs of tau bind to the insides of microtubules in the absence of taxol. EMBO J. 22, 70-77.
    • (2003) EMBO J. , vol.22 , pp. 70-77
    • Kar, S.1    Fan, J.2    Smith, M.J.3    Goedert, M.4    Amos, L.A.5
  • 6
    • 0037414777 scopus 로고    scopus 로고
    • Overexpression of full-length but not N-terminal truncated isoform of microtubule-associated protein (MAP) IB accelerates apoptosis of cultured cortical neurons
    • Uchida, Y. (2003) Overexpression of full-length but not N-terminal truncated isoform of microtubule-associated protein (MAP) IB accelerates apoptosis of cultured cortical neurons. J. Biol. Chem. 278, 366-371.
    • (2003) J. Biol. Chem. , vol.278 , pp. 366-371
    • Uchida, Y.1
  • 7
    • 0037172666 scopus 로고    scopus 로고
    • MAP4 counteracts microtubule catastrophe promotion but not tubulin-sequestering activity in intact cells
    • Holmfeldt, P., Brattsand, G. & Gullberg, M. (2002) MAP4 counteracts microtubule catastrophe promotion but not tubulin-sequestering activity in intact cells. Curr. Biol. 12, 1034-1039.
    • (2002) Curr. Biol. , vol.12 , pp. 1034-1039
    • Holmfeldt, P.1    Brattsand, G.2    Gullberg, M.3
  • 8
    • 0037166943 scopus 로고    scopus 로고
    • MAP2 and tau bind longitudinally along the outer ridges of microtubule protofilaments
    • Al-Bassam, J., Ozer, R.S., Safer, D., Halpain, S. & Milligan, R.A. (2002) MAP2 and tau bind longitudinally along the outer ridges of microtubule protofilaments. J. Cell Biol. 157, 1187-1196.
    • (2002) J. Cell Biol. , vol.157 , pp. 1187-1196
    • Al-Bassam, J.1    Ozer, R.S.2    Safer, D.3    Halpain, S.4    Milligan, R.A.5
  • 9
    • 0033972532 scopus 로고    scopus 로고
    • Kinesins and microtubules: Their structures and motor mechanisms
    • Sablin, E.P. (2000) Kinesins and microtubules: their structures and motor mechanisms. Curr. Opin. Cell Biol. 12, 35-41.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 35-41
    • Sablin, E.P.1
  • 10
    • 0034618565 scopus 로고    scopus 로고
    • Microtubule motors in mitosis
    • Sharp, D.J., Rogers, G.C. & Scholey, J.M. (2000) Microtubule motors in mitosis. Nature 407, 41-47.
    • (2000) Nature , vol.407 , pp. 41-47
    • Sharp, D.J.1    Rogers, G.C.2    Scholey, J.M.3
  • 11
    • 0036678201 scopus 로고    scopus 로고
    • The microtubule-destabilizing kinesin XKCM1 regulates microtubule dynamic instability in cells
    • Kline-Smith, S.L. & Walczak, C.E. (2002) The microtubule- destabilizing kinesin XKCM1 regulates microtubule dynamic instability in cells. Mol. Biol. Cell 13, 2718-2731.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2718-2731
    • Kline-Smith, S.L.1    Walczak, C.E.2
  • 13
    • 0037416151 scopus 로고    scopus 로고
    • HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo
    • Zhang, Y., Li, N., Caron, C., Matthias, G., Hess, D., Khochbin, S. & Matthias, P. (2003) HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo. EMBO J. 22, 1168-1179.
    • (2003) EMBO J. , vol.22 , pp. 1168-1179
    • Zhang, Y.1    Li, N.2    Caron, C.3    Matthias, G.4    Hess, D.5    Khochbin, S.6    Matthias, P.7
  • 14
    • 0034100185 scopus 로고    scopus 로고
    • The glycolytic enzyme enolase is present in sperm tail and displays nucleotide-dependent association with microtubules
    • Gitlits, V.M., Toh, B.H., Loveland, K.L. & Sentry, J.W. (2000) The glycolytic enzyme enolase is present in sperm tail and displays nucleotide-dependent association with microtubules. Eur. J. Cell Biol. 79, 104-111.
    • (2000) Eur. J. Cell Biol. , vol.79 , pp. 104-111
    • Gitlits, V.M.1    Toh, B.H.2    Loveland, K.L.3    Sentry, J.W.4
  • 15
    • 0025083511 scopus 로고
    • Analysis of the binding of glyceraldehyde-3-phosphate dehydrogenase to microtubules, the mechanism of bundle formation and the linkage effect
    • Somers, M., Engelborghs, Y. & Baert, J. (1990) Analysis of the binding of glyceraldehyde-3-phosphate dehydrogenase to microtubules, the mechanism of bundle formation and the linkage effect. Eur. J. Biochem. 193, 437-444.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 437-444
    • Somers, M.1    Engelborghs, Y.2    Baert, J.3
  • 16
    • 0035842895 scopus 로고    scopus 로고
    • A novel p21-activated kinase binds the actin and microtubule networks and induces microtubule stabilization
    • Cau, J., Faure, S., Comps, M., Delsert, C. & Morin, N. (2001) A novel p21-activated kinase binds the actin and microtubule networks and induces microtubule stabilization. J. Cell Biol. 155, 1029-1042.
    • (2001) J. Cell Biol. , vol.155 , pp. 1029-1042
    • Cau, J.1    Faure, S.2    Comps, M.3    Delsert, C.4    Morin, N.5
  • 17
    • 0035895915 scopus 로고    scopus 로고
    • Characterization of p190Rho-GEF, a RhoA-specific guanine nucleotide exchange factor that interacts with microtubules
    • van Horck, F.P.G., Ahmadian, M.R., Haeusler, L.C., Moolenaar, W.H. & Kranenburg, O. (2001) Characterization of p190Rho-GEF, a RhoA-specific guanine nucleotide exchange factor that interacts with microtubules. J. Biol. Chem. 276, 4948-4956.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4948-4956
    • Van Horck, F.P.G.1    Ahmadian, M.R.2    Haeusler, L.C.3    Moolenaar, W.H.4    Kranenburg, O.5
  • 18
    • 0024660212 scopus 로고
    • Cross-linking of microtubules by microtubule-associated proteins (MAPs) from the brine shrimp Artemia
    • Campbell, E.J., MacKinlay, S.A. & MacRae, T.H. (1989) Cross-linking of microtubules by microtubule-associated proteins (MAPs) from the brine shrimp Artemia. J. Cell Sci. 93, 29-39.
    • (1989) J. Cell Sci. , vol.93 , pp. 29-39
    • Campbell, E.J.1    MacKinlay, S.A.2    MacRae, T.H.3
  • 19
    • 0026936628 scopus 로고
    • A novel 49-kilodalton protein from Artemia cross-links microtubules in vitro
    • Zhang, J. & MacRae, T.H. (1992) A novel 49-kilodalton protein from Artemia cross-links microtubules in vitro. Biochem. Cell Biol. 70, 1055-1063.
    • (1992) Biochem. Cell Biol. , vol.70 , pp. 1055-1063
    • Zhang, J.1    MacRae, T.H.2
  • 20
    • 0028101327 scopus 로고
    • Nucleotide dependence and cytoplasmic localization of a 49-kDa microtubule cross-linking protein from the brine shrimp Artemia
    • Zhang, J. & MacRae, T.H. (1994) Nucleotide dependence and cytoplasmic localization of a 49-kDa microtubule cross-linking protein from the brine shrimp Artemia. J. Biol. Chem. 269, 3053-3062.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3053-3062
    • Zhang, J.1    MacRae, T.H.2
  • 21
    • 0028908154 scopus 로고
    • Influence of phosphorylation on isoform composition and function of a microtubule-associated protein from developing Artemia
    • Zhang, J. & MacRae, T.H. (1995) Influence of phosphorylation on isoform composition and function of a microtubule-associated protein from developing Artemia. Biochem. J. 307, 419-424.
    • (1995) Biochem. J. , vol.307 , pp. 419-424
    • Zhang, J.1    MacRae, T.H.2
  • 22
    • 0025370112 scopus 로고
    • Tubulin isoforms in the brine shrimp, Artemia: Primary gene products and their posttranslational modification
    • Langdon, C.M., Bagshaw, J.C. & MacRae, T.H. (1990) Tubulin isoforms in the brine shrimp, Artemia: primary gene products and their posttranslational modification. Eur. J. Cell Biol. 52, 17-26.
    • (1990) Eur. J. Cell Biol. , vol.52 , pp. 17-26
    • Langdon, C.M.1    Bagshaw, J.C.2    MacRae, T.H.3
  • 23
    • 0037975662 scopus 로고    scopus 로고
    • Understanding tubulin-taxol interactions: Mutations that impart taxol binding to yeast tubulin
    • Gupta, M.L. Jr, Bode, C.J., Georg, G.I. & Himes, R.H. (2003) Understanding tubulin-taxol interactions: mutations that impart taxol binding to yeast tubulin. Proc. Natl Acad. Sci. USA 100, 6394-6397.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 6394-6397
    • Gupta Jr., M.L.1    Bode, C.J.2    Georg, G.I.3    Himes, R.H.4
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0041525250 scopus 로고    scopus 로고
    • A small heat shock/α-crystallin protein from encysted Artemia embryos suppresses tubulin denaturation
    • Day, R.M., Gupta, J.S. & MacRae, T.H. (2003) A small heat shock/α-crystallin protein from encysted Artemia embryos suppresses tubulin denaturation. Cell Stress Chaperones 8, 183-193.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 183-193
    • Day, R.M.1    Gupta, J.S.2    MacRae, T.H.3
  • 27
    • 0033849869 scopus 로고    scopus 로고
    • Fermentation of 4-aminobutyrate by Clostridium aminobutyricum: Cloning of two genes involved in the formation and dehydration of 4-hydroxybutyryl-CoA
    • Gerhardt, A., Çinkaya, I., Linder, D., Huisman, G. & Buckel, W. (2000) Fermentation of 4-aminobutyrate by Clostridium aminobutyricum: cloning of two genes involved in the formation and dehydration of 4-hydroxybutyryl-CoA. Arch. Microbiol. 174, 189-199.
    • (2000) Arch. Microbiol. , vol.174 , pp. 189-199
    • Gerhardt, A.1    Çinkaya, I.2    Linder, D.3    Huisman, G.4    Buckel, W.5
  • 30
    • 0030771126 scopus 로고    scopus 로고
    • The PROSITE database, its status in 1997
    • Bairoch, A., Bucher, P. & Hofman, K. (1997) The PROSITE database, its status in 1997. Nucleic Acids Res. 25, 217-221.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 217-221
    • Bairoch, A.1    Bucher, P.2    Hofman, K.3
  • 32
    • 0030203863 scopus 로고    scopus 로고
    • TREEVIEW: An application to display phylogenetic trees on personal computers
    • Page, R.D. (1996) TREEVIEW: an application to display phylogenetic trees on personal computers. Comput. Appl. Biosci. 12, 357-358.
    • (1996) Comput. Appl. Biosci. , vol.12 , pp. 357-358
    • Page, R.D.1
  • 33
    • 0025780688 scopus 로고
    • Purification and properties of 4-hydroxybutyrate coenzyme a transferase from Clostridium aminobutyricum
    • Scherf, U. & Buckel, W. (1991) Purification and properties of 4-hydroxybutyrate coenzyme A transferase from Clostridium aminobutyricum. Appl. Environ. Microbiol. 57, 2699-2702.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 2699-2702
    • Scherf, U.1    Buckel, W.2
  • 34
    • 0028075976 scopus 로고
    • Location of the 2 genes encoding glutaconate coenzyme-A-transferase at the beginning of the hydroxyglutarate operon in Acidaminococcus fermentans
    • Mack, M., Bendrat, K., Zelder, O., Eckel, E., Linder, D. & Buckel, W. (1994) Location of the 2 genes encoding glutaconate coenzyme-A-transferase at the beginning of the hydroxyglutarate operon in Acidaminococcus fermentans. Eur. J. Biochem. 226, 41-51.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 41-51
    • Mack, M.1    Bendrat, K.2    Zelder, O.3    Eckel, E.4    Linder, D.5    Buckel, W.6
  • 35
    • 0036151093 scopus 로고    scopus 로고
    • Propionate CoA-transferase from Clostridium propionicum: Cloning of the gene and identification of glutamate 324 at the active site
    • Selmer, T., Willanzheimer, A. & Hetzel, M. (2002) Propionate CoA-transferase from Clostridium propionicum: cloning of the gene and identification of glutamate 324 at the active site. Eur. J. Biochem. 269, 372-380.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 372-380
    • Selmer, T.1    Willanzheimer, A.2    Hetzel, M.3
  • 36
    • 0031569327 scopus 로고    scopus 로고
    • Glutaconate CoA-transferase from Acidaminococcus fermentans: The crystal structure reveals homology with other CoA-transferases
    • Jacob, U., Mack, M., Clausen, T., Huber, R., Buckel, W. & Messerschmidt, A. (1997) Glutaconate CoA-transferase from Acidaminococcus fermentans: the crystal structure reveals homology with other CoA-transferases. Structure 5, 415-426.
    • (1997) Structure , vol.5 , pp. 415-426
    • Jacob, U.1    Mack, M.2    Clausen, T.3    Huber, R.4    Buckel, W.5    Messerschmidt, A.6
  • 37
    • 0019401061 scopus 로고
    • Glutaconate CoA-transferase from Acidaminococcus fermentans
    • Buckel, W., Dorn, U. & Semmer, R. (1981) Glutaconate CoA-transferase from Acidaminococcus fermentans. Eur. J. Biochem. 118, 315-321.
    • (1981) Eur. J. Biochem. , vol.118 , pp. 315-321
    • Buckel, W.1    Dorn, U.2    Semmer, R.3
  • 38
    • 0037195125 scopus 로고    scopus 로고
    • Tubulin is the endogenous inhibitor of the glyceraldehyde 3-phosphate dehydrogenase isoform that catalyzes membrane fusion: Implications for the coordinated regulation of glycolysis and membrane fusion
    • Glaser, P.E., Han, X. & Gross, R.W. (2002) Tubulin is the endogenous inhibitor of the glyceraldehyde 3-phosphate dehydrogenase isoform that catalyzes membrane fusion: implications for the coordinated regulation of glycolysis and membrane fusion. Proc. Natl Acad. Sci. USA 99, 14104-14109.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 14104-14109
    • Glaser, P.E.1    Han, X.2    Gross, R.W.3
  • 39
    • 0036479109 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase Ciota/γ and plays a role in microtubule dynamics in the early secretory pathway
    • Tisdale, E.J. (2002) Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase Ciota/γ and plays a role in microtubule dynamics in the early secretory pathway. J. Biol. Chem. 277, 3334-3341.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3334-3341
    • Tisdale, E.J.1
  • 40
    • 0035976817 scopus 로고    scopus 로고
    • Tubulin and microtubule are potential targets for brain hexokinase binding
    • Wágner, G., Kovács, J., Löw, P., Orosz, F. & Ovádi, J. (2001) Tubulin and microtubule are potential targets for brain hexokinase binding. FEBS Lett. 509, 81-84.
    • (2001) FEBS Lett. , vol.509 , pp. 81-84
    • Wágner, G.1    Kovács, J.2    Löw, P.3    Orosz, F.4    Ovádi, J.5
  • 42
    • 0036723365 scopus 로고    scopus 로고
    • Microtubule-dependent subcellular redistribution of the transcriptional coactivator p/CIP
    • Qutob, M.S., Bhattacharjee, R.N., Pollari, E., Yee, S.P. & Torchia, J. (2002) Microtubule-dependent subcellular redistribution of the transcriptional coactivator p/CIP. Mol. Cell Biol. 22, 6611-6626.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 6611-6626
    • Qutob, M.S.1    Bhattacharjee, R.N.2    Pollari, E.3    Yee, S.P.4    Torchia, J.5


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