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Volumn 327, Issue 1, 2005, Pages 35-42

Identification of proteins binding the native tubulin dimer

Author keywords

Microtubules; Tubulin; Tubulin associated proteins

Indexed keywords

ALPHA TUBULIN; BINDING PROTEIN; DIMER; HEAT SHOCK PROTEIN; MICROTUBULE ASSOCIATED PROTEIN; MONOCLONAL ANTIBODY; TUBULIN;

EID: 11144228323     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.11.138     Document Type: Article
Times cited : (25)

References (48)
  • 2
    • 0030783012 scopus 로고    scopus 로고
    • Stathmin: A tubulin-sequestering protein which forms a ternary T2S complex with two tubulin molecules
    • L. Jourdain, P. Curmi, A. Sobel, D. Pantaloni, and M.F. Carlier Stathmin: a tubulin-sequestering protein which forms a ternary T2S complex with two tubulin molecules Biochemistry 36 1997 10817 108121
    • (1997) Biochemistry , vol.36 , pp. 10817-108121
    • Jourdain, L.1    Curmi, P.2    Sobel, A.3    Pantaloni, D.4    Carlier, M.F.5
  • 4
    • 0033081060 scopus 로고    scopus 로고
    • Identification of MINUS, a small polypeptide that functions as a microtubule nucleation suppressor
    • P. Fanara, B. Oback, K. Ashman, A. Podtelejnikov, and R. Brandt Identification of MINUS, a small polypeptide that functions as a microtubule nucleation suppressor EMBO J. 18 1999 565 577
    • (1999) EMBO J. , vol.18 , pp. 565-577
    • Fanara, P.1    Oback, B.2    Ashman, K.3    Podtelejnikov, A.4    Brandt, R.5
  • 5
    • 0030820735 scopus 로고    scopus 로고
    • Tubulin subunits exist in an activated conformational state generated and maintained by proteins cofactors
    • G. Tian, S.A. Lewis, B. Feierbach, T. Stearns, H. Rommelaere, C. Ampe, and N.J. Cowan Tubulin subunits exist in an activated conformational state generated and maintained by proteins cofactors J. Cell Biol. 138 1997 821 832
    • (1997) J. Cell Biol. , vol.138 , pp. 821-832
    • Tian, G.1    Lewis, S.A.2    Feierbach, B.3    Stearns, T.4    Rommelaere, H.5    Ampe, C.6    Cowan, N.J.7
  • 6
    • 0033588020 scopus 로고    scopus 로고
    • Tubulin folding cofactors as GTPase-activating proteins. GTP hydrolysis and the assembly of the alpha/beta-tubulin heterodimer
    • G. Tian, A. Bhamidipati, N.J. Cowan, and S.A. Lewis Tubulin folding cofactors as GTPase-activating proteins. GTP hydrolysis and the assembly of the alpha/beta-tubulin heterodimer J. Biol. Chem. 274 1999 24054 24058
    • (1999) J. Biol. Chem. , vol.274 , pp. 24054-24058
    • Tian, G.1    Bhamidipati, A.2    Cowan, N.J.3    Lewis, S.A.4
  • 7
    • 0034729382 scopus 로고    scopus 로고
    • ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin
    • A. Bhamidipati, S.A. Lewis, and N.J. Cowan ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin J. Cell Biol. 149 2000 1087 1096
    • (2000) J. Cell Biol. , vol.149 , pp. 1087-1096
    • Bhamidipati, A.1    Lewis, S.A.2    Cowan, N.J.3
  • 8
    • 0034658368 scopus 로고    scopus 로고
    • EB1 proteins regulate microtubule dynamics, cell polarity, and chromosome stability
    • J.S. Tirnauer, and B.E. Bierer EB1 proteins regulate microtubule dynamics, cell polarity, and chromosome stability J. Cell Biol. 149 2000 761 766
    • (2000) J. Cell Biol. , vol.149 , pp. 761-766
    • Tirnauer, J.S.1    Bierer, B.E.2
  • 9
    • 0038709397 scopus 로고    scopus 로고
    • The microtubule plus-end proteins EB1 and dynactin have differential effects on microtubule polymerization
    • L.A. Ligon, S.S. Shelly, M. Tokito, and E.L.F. Holzbaur The microtubule plus-end proteins EB1 and dynactin have differential effects on microtubule polymerization Mol. Biol. Cell. 14 2003 1405 1417
    • (2003) Mol. Biol. Cell. , vol.14 , pp. 1405-1417
    • Ligon, L.A.1    Shelly, S.S.2    Tokito, M.3    Holzbaur, E.L.F.4
  • 10
    • 0030668145 scopus 로고    scopus 로고
    • BIM1 encodes a microtubule-binding protein in yeast
    • K. Schwartz, K. Richards, and D. Bostein BIM1 encodes a microtubule-binding protein in yeast Mol. Biol. Cell. 8 1997 2677 2691
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 2677-2691
    • Schwartz, K.1    Richards, K.2    Bostein, D.3
  • 14
    • 0034677672 scopus 로고    scopus 로고
    • A reassessment of the factors affecting microtubule assembly and disassembly in vitro
    • N. Caudron, O. Valiron, Y. Usson, P. Valiron, and D. Job A reassessment of the factors affecting microtubule assembly and disassembly in vitro J. Mol. Biol. 297 2000 211 220
    • (2000) J. Mol. Biol. , vol.297 , pp. 211-220
    • Caudron, N.1    Valiron, O.2    Usson, Y.3    Valiron, P.4    Job, D.5
  • 15
    • 0024583552 scopus 로고
    • Complete separation of tyrosinated, detyrosinated, and nontyrosinatable brain tubulin subpopulations using affinity chromatography
    • L. Paturle, J. Wehland, R.L. Margolis, and D. Job Complete separation of tyrosinated, detyrosinated, and nontyrosinatable brain tubulin subpopulations using affinity chromatography Biochemistry 28 1989 2698 2704
    • (1989) Biochemistry , vol.28 , pp. 2698-2704
    • Paturle, L.1    Wehland, J.2    Margolis, R.L.3    Job, D.4
  • 16
    • 0021074286 scopus 로고
    • A rat monoclonal antibody reacting specifically with the tyrosinated form of alpha-tubulin. I. Biochemical characterization, effects on microtubule polymerization in vitro, and microtubule polymerization and organization in vivo
    • J. Wehland, M.C. Willigham, and J.V. Sandoval A rat monoclonal antibody reacting specifically with the tyrosinated form of alpha-tubulin. I. Biochemical characterization, effects on microtubule polymerization in vitro, and microtubule polymerization and organization in vivo J. Cell Biol. 97 1983 1467 1475
    • (1983) J. Cell Biol. , vol.97 , pp. 1467-1475
    • Wehland, J.1    Willigham, M.C.2    Sandoval, J.V.3
  • 19
    • 0021837781 scopus 로고
    • The small subunit of ribonucleotide reductase is encoded by one of the most abundant translationally regulated maternal RNAs in clam and sea urchin eggs
    • N.M. Standart, S.J. Bray, E.L. George, T. Hunt, and J.V. Ruderman The small subunit of ribonucleotide reductase is encoded by one of the most abundant translationally regulated maternal RNAs in clam and sea urchin eggs J. Cell Biol. 100 1985 1968 1976
    • (1985) J. Cell Biol. , vol.100 , pp. 1968-1976
    • Standart, N.M.1    Bray, S.J.2    George, E.L.3    Hunt, T.4    Ruderman, J.V.5
  • 20
    • 0036798432 scopus 로고    scopus 로고
    • EB1-microtubule interactions in Xenopus egg extracts: Role of EB1 in microtubule stabilization and mechanisms of targeting to microtubules
    • J.S. Tirnauer, S. Grego, E.D. Salmon, and T.J. Mitchison EB1-microtubule interactions in Xenopus egg extracts: role of EB1 in microtubule stabilization and mechanisms of targeting to microtubules Mol. Biol. Cell. 13 2002 3614 3626
    • (2002) Mol. Biol. Cell. , vol.13 , pp. 3614-3626
    • Tirnauer, J.S.1    Grego, S.2    Salmon, E.D.3    Mitchison, T.J.4
  • 21
    • 0030802287 scopus 로고    scopus 로고
    • Molecular chaperones and the cytoskeleton
    • P. Liang, and T.H. MacRae Molecular chaperones and the cytoskeleton J. Cell Sci. 110 1997 1431 1440
    • (1997) J. Cell Sci. , vol.110 , pp. 1431-1440
    • Liang, P.1    MacRae, T.H.2
  • 22
    • 0032491521 scopus 로고    scopus 로고
    • Loss of Hsp70-Hsp40 chaperone activity causes abnormal nuclear distribution and aberrant microtubule formation in M-phase of Saccharomyces cerevisiae
    • M. Oka, M. Nakai, T. Endo, C.R. Lim, Y. Kimata, and K. Kohno Loss of Hsp70-Hsp40 chaperone activity causes abnormal nuclear distribution and aberrant microtubule formation in M-phase of Saccharomyces cerevisiae J. Biol. Chem. 273 1998 29727 29737
    • (1998) J. Biol. Chem. , vol.273 , pp. 29727-29737
    • Oka, M.1    Nakai, M.2    Endo, T.3    Lim, C.R.4    Kimata, Y.5    Kohno, K.6
  • 23
    • 0029746254 scopus 로고    scopus 로고
    • Effect of nucleotides, peptides, and unfolded proteins on the self-association of the molecular chaperone HSC70
    • N. Benaroudj, F. Triniolles, and M.M. Ladjimi Effect of nucleotides, peptides, and unfolded proteins on the self-association of the molecular chaperone HSC70 J. Biol. Chem. 271 1996 18471 18476
    • (1996) J. Biol. Chem. , vol.271 , pp. 18471-18476
    • Benaroudj, N.1    Triniolles, F.2    Ladjimi, M.M.3
  • 25
  • 29
    • 0032979181 scopus 로고    scopus 로고
    • Stathmin interaction with HSC70 family proteins
    • V. Manceau, O. Gavet, P. Curmi, and A. Sobel Stathmin interaction with HSC70 family proteins Electrophoresis 20 1999 409 417
    • (1999) Electrophoresis , vol.20 , pp. 409-417
    • Manceau, V.1    Gavet, O.2    Curmi, P.3    Sobel, A.4
  • 31
    • 0036713310 scopus 로고    scopus 로고
    • The anaphase-promoting complex: It's not just for mitosis any more
    • J.W. Harper, J.L. Burton, and M.J. Solomon The anaphase-promoting complex: it's not just for mitosis any more Genes Dev. 165 2002 2179 2206
    • (2002) Genes Dev. , vol.165 , pp. 2179-2206
    • Harper, J.W.1    Burton, J.L.2    Solomon, M.J.3
  • 32
    • 0031055137 scopus 로고    scopus 로고
    • APC-mediated proteolysis of Ase1 and the morphogenesis of the mitotic spindle
    • Y.L. Juang, J. Huang, J.M. Peters, M.E. Mc Laughlin, C.Y. Tai, and D. Pellman APC-mediated proteolysis of Ase1 and the morphogenesis of the mitotic spindle Science 275 1997 1311 1314
    • (1997) Science , vol.275 , pp. 1311-1314
    • Juang, Y.L.1    Huang, J.2    Peters, J.M.3    Mc Laughlin, M.E.4    Tai, C.Y.5    Pellman, D.6
  • 33
    • 0345254320 scopus 로고    scopus 로고
    • Kip1, a kinesin-related motor protein is a substrate for APC-mediated proteolysis
    • D.M. Gordon, and D.M. Roof Kip1, a kinesin-related motor protein is a substrate for APC-mediated proteolysis Mol. Biol. Cell 8 Suppl. 1997 813
    • (1997) Mol. Biol. Cell , vol.8 , pp. 813
    • Gordon, D.M.1    Roof, D.M.2
  • 36
    • 0037774459 scopus 로고    scopus 로고
    • LRP130, a pentatricopeptide motif protein with a noncanonical RNA-binding domain, is bound in vivo to mitochondrial and nuclear RNAs
    • S. Mili, and S. Pinol-Roma LRP130, a pentatricopeptide motif protein with a noncanonical RNA-binding domain, is bound in vivo to mitochondrial and nuclear RNAs Mol. Cell. Biol. 23 2003 4972 4982
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4972-4982
    • Mili, S.1    Pinol-Roma, S.2
  • 37
    • 0032967476 scopus 로고    scopus 로고
    • RNA-cytoskeletal associations
    • R.P. Jansen RNA-cytoskeletal associations FASEB J. 13 1999 455 466
    • (1999) FASEB J. , vol.13 , pp. 455-466
    • Jansen, R.P.1
  • 38
    • 0021077837 scopus 로고
    • Distinct patterns of cytoplasmic protein phosphorylation related to regulation of synthesis and release of prolactin by GH cells
    • A. Sobel, and A.H. Tashjian Distinct patterns of cytoplasmic protein phosphorylation related to regulation of synthesis and release of prolactin by GH cells J. Biol. Chem. 258 1983 10312 10324
    • (1983) J. Biol. Chem. , vol.258 , pp. 10312-10324
    • Sobel, A.1    Tashjian, A.H.2
  • 39
    • 0030687570 scopus 로고    scopus 로고
    • The alpha and beta tubulin folding pathways
    • S.A. Lewis, G. Tian, and N.J. Cowan The alpha and beta tubulin folding pathways Trends Cell Biol. 7 1997 479 485
    • (1997) Trends Cell Biol. , vol.7 , pp. 479-485
    • Lewis, S.A.1    Tian, G.2    Cowan, N.J.3
  • 40
    • 0028823831 scopus 로고
    • Characterization of the cDNA and pattern expression of a new gene over-expressed in human hepatomas and colonic tumors
    • S. Charasse, M. Mazel, S. Taviaux, P. Berta, T. Chow, and C. Larroque Characterization of the cDNA and pattern expression of a new gene over-expressed in human hepatomas and colonic tumors Eur. J. Biochem. 234 1995 406 413
    • (1995) Eur. J. Biochem. , vol.234 , pp. 406-413
    • Charasse, S.1    Mazel, M.2    Taviaux, S.3    Berta, P.4    Chow, T.5    Larroque, C.6
  • 41
    • 0029885423 scopus 로고    scopus 로고
    • Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins HSP90 and HSP70
    • S. Chen, V. Prapapanich, R.A. Rimerman, B. Honoré, and D.F. Smith Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins HSP90 and HSP70 Mol. Endocrinol. 10 1996 682 693
    • (1996) Mol. Endocrinol. , vol.10 , pp. 682-693
    • Chen, S.1    Prapapanich, V.2    Rimerman, R.A.3    Honoré, B.4    Smith, D.F.5
  • 42
    • 1242269219 scopus 로고    scopus 로고
    • Mechanisms for regulation of Hsp70 function by Hsp40
    • C.Y. Fan, S. Lee, and D.M. Cyr Mechanisms for regulation of Hsp70 function by Hsp40 Cell Stress Chaperones 8 2003 309 316
    • (2003) Cell Stress Chaperones , vol.8 , pp. 309-316
    • Fan, C.Y.1    Lee, S.2    Cyr, D.M.3
  • 43
    • 0033534588 scopus 로고    scopus 로고
    • An evolutionary conserved family of Hsp70/Hsc70 molecular chaperone regulators
    • S. Takayama, Z. Xie, and J.C. Reed An evolutionary conserved family of Hsp70/Hsc70 molecular chaperone regulators J. Biol. Chem. 274 1999 781 786
    • (1999) J. Biol. Chem. , vol.274 , pp. 781-786
    • Takayama, S.1    Xie, Z.2    Reed, J.C.3
  • 44
    • 0026843954 scopus 로고
    • Mammalian stress response: Induction of the glucose-regulated protein family
    • A.S. Lee Mammalian stress response: induction of the glucose-regulated protein family Curr. Opin. Cell Biol. 4 1992 267 273
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 267-273
    • Lee, A.S.1
  • 45
    • 0031866430 scopus 로고    scopus 로고
    • Characterization of the Hsp110/SSE gene family response to hyperosmolality and other stresses
    • B.C. Santos, A. Chevaile, R. Kojima, and S.R. Gullans Characterization of the Hsp110/SSE gene family response to hyperosmolality and other stresses Am. J. Physiol. 274 1998 F1054 1061
    • (1998) Am. J. Physiol. , vol.274
    • Santos, B.C.1    Chevaile, A.2    Kojima, R.3    Gullans, S.R.4
  • 47
    • 0028232866 scopus 로고
    • Molecular cloning and expression of the gene for a major leucine-rich protein from human hepatoblastoma cells (HepG2)
    • J. Hou, F. Wang, and W.F. McKeehan Molecular cloning and expression of the gene for a major leucine-rich protein from human hepatoblastoma cells (HepG2) In Vitro Cell. Dev. Biol. Anim. A 30 1994 111 114
    • (1994) In Vitro Cell. Dev. Biol. Anim. a , vol.30 , pp. 111-114
    • Hou, J.1    Wang, F.2    McKeehan, W.F.3
  • 48
    • 11144224974 scopus 로고    scopus 로고
    • Importins and exportins: How to get in and out of the nucleus
    • K. Weis Importins and exportins: how to get in and out of the nucleus Trends Biochem. Sci. 136 1998 859 870
    • (1998) Trends Biochem. Sci. , vol.136 , pp. 859-870
    • Weis, K.1


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