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Volumn 287, Issue 42, 2012, Pages 35127-35138

MAP6-F is a temperature sensor that directly binds to and protects microtubules from cold-induced depolymerization

Author keywords

[No Author keywords available]

Indexed keywords

BODY TEMPERATURE; COLD SENSITIVITY; CONFORMATIONAL CHANGE; DYNAMIC STRUCTURE; IN-VITRO; IN-VIVO; MICROTUBULE NETWORKS; MICROTUBULES; PURIFIED PROTEIN; TEMPERATURE DECREASE; TEMPERATURE DEPENDENT;

EID: 84867422216     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.398339     Document Type: Article
Times cited : (42)

References (36)
  • 1
    • 41149156427 scopus 로고    scopus 로고
    • Tracking the ends: A dynamic protein network controls the fate of microtubule tips
    • DOI 10.1038/nrm2369, PII NRM2369
    • Akhmanova, A., and Steinmetz, M. O. (2008) Tracking the ends: a dynamic protein network controls the fate of microtubule tips. Nat. Rev. Mol. Cell Biol. 9, 309-322 (Pubitemid 351430849)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.4 , pp. 309-322
    • Akhmanova, A.1    Steinmetz, M.O.2
  • 2
    • 68049084655 scopus 로고    scopus 로고
    • Growth, fluctuation and switching at microtubule plus ends
    • Howard, J., and Hyman, A. A. (2009) Growth, fluctuation and switching at microtubule plus ends. Nat. Rev. Mol. Cell Biol. 10, 569-574
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 569-574
    • Howard, J.1    Hyman, A.A.2
  • 3
    • 33644853818 scopus 로고    scopus 로고
    • Structural intermediates in microtubule assembly and disassembly: How and why?
    • DOI 10.1016/j.ceb.2006.02.009, PII S0955067406000226, Cell Regulation
    • Nogales, E., and Wang, H. W. (2006) Structural intermediates in microtubule assembly and disassembly: how and why? Curr. Opin Cell Biol. 18, 179-184 (Pubitemid 43375886)
    • (2006) Current Opinion in Cell Biology , vol.18 , Issue.2 , pp. 179-184
    • Nogales, E.1    Wang, H.-W.2
  • 4
    • 70350571135 scopus 로고    scopus 로고
    • On and around microtubules: An overview
    • Wade, R. H. (2009) On and around microtubules: an overview. Mol Biotechnol 43, 177-191
    • (2009) Mol Biotechnol , vol.43 , pp. 177-191
    • Wade, R.H.1
  • 5
    • 0017334810 scopus 로고
    • In vitro reconstitution of calf brain microtubules: effects of solution variables
    • Lee, J. C., and Timasheff, S. N. (1977) In vitro reconstitution of calf brain microtubules: effects of solution variables. Biochemistry 16, 1754-1764 (Pubitemid 8081481)
    • (1977) Biochemistry , vol.16 , Issue.8 , pp. 1754-1764
    • Lee, J.C.1    Timasheff, S.N.2
  • 6
    • 0016813649 scopus 로고
    • Ionic and nucleotide requirements for microtubule polymerization in vitro
    • Olmsted, J. B., and Borisy, G. G. (1975) Ionic and nucleotide requirements for microtubule polymerization in vitro. Biochemistry 14, 2996-3005
    • (1975) Biochemistry , vol.14 , pp. 2996-3005
    • Olmsted, J.B.1    Borisy, G.G.2
  • 7
    • 0019459110 scopus 로고
    • Microtubule assembly and disassembly at alkaline pH
    • DOI 10.1083/jcb.89.1.45
    • Regula, C. S., Pfeiffer, J. R., and Berlin, R. D. (1981) Microtubule assembly and disassembly at alkaline pH. J. Cell Biol. 89, 45-53 (Pubitemid 11066129)
    • (1981) Journal of Cell Biology , vol.89 , Issue.1 , pp. 45-53
    • Regula, C.S.1    Pfeiffer, J.R.2    Berlin, R.D.3
  • 8
    • 0025823655 scopus 로고
    • The effect of solution composition on microtubule dynamic instability
    • Schilstra, M. J., Bayley, P. M., and Martin, S. R. (1991) The effect of solution composition on microtubule dynamic instability. Biochem. J. 277, 839-847
    • (1991) Biochem. J. , vol.277 , pp. 839-847
    • Schilstra, M.J.1    Bayley, P.M.2    Martin, S.R.3
  • 10
    • 0034708365 scopus 로고    scopus 로고
    • Expression of cold-adapted β-tubulins confer cold-tolerance to human cellular microtubules
    • DOI 10.1006/bbrc.2000.2362
    • Modig, C., Wallin, M., and Olsson, P. E. (2000) Expression of cold-adapted β-tubulins confer cold-tolerance to human cellular microtubules. Biochem. Biophys. Res. Commun. 269, 787-791 (Pubitemid 30440378)
    • (2000) Biochemical and Biophysical Research Communications , vol.269 , Issue.3 , pp. 787-791
    • Modig, C.1    Wallin, M.2    Olsson, P.-E.3
  • 11
    • 0031280519 scopus 로고    scopus 로고
    • Microtubule assembly in cold-adapted organisms: Functional properties and structural adaptations of tubulins from antarctic fishes
    • Detrich, H. W., 3rd. (1997) Microtubule assembly in cold-adapted organisms: functional properties and structural adaptations of tubulins from antarctic fishes. Comp. Biochem. Physiol. A. Physiol. 118, 501-513
    • (1997) Comp. Biochem. Physiol. A. Physiol. , vol.118 , pp. 501-513
    • Detrich III, H.W.1
  • 12
    • 0034711208 scopus 로고    scopus 로고
    • Cold adaptation of microtubule assembly and dynamics. Structural interpretation of primary sequence changes present in the α- and β-tubulins of antarctic fishes
    • DOI 10.1074/jbc.M005699200
    • Detrich, H. W., 3rd, Parker, S. K., Williams, R. C., Jr., Nogales, E., and Downing, K. H. (2000) Cold adaptation of microtubule assembly and dynamics. Structural interpretation of primary sequence changes present in the α- and β-tubulins of Antarctic fishes. J. Biol. Chem. 275, 37038-37047 (Pubitemid 32002120)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.47 , pp. 37038-37047
    • Detrich III, H.W.1    Parker, S.K.2    Williams Jr., R.C.3    Nogales, E.4    Downing, K.H.5
  • 13
    • 0023688586 scopus 로고
    • Reduction of metabolism during hibernation and daily torpor in mammals and birds: Temperature effect or physiological inhibition?
    • Geiser, F. (1988) Reduction of metabolism during hibernation and daily torpor in mammals and birds: temperature effect or physiological inhibition? J. Comp Physiol. B. 158, 25-37
    • (1988) J. Comp Physiol. B. , vol.158 , pp. 25-37
    • Geiser, F.1
  • 14
    • 3543017385 scopus 로고    scopus 로고
    • Natural hypometabolism during hibernation and daily torpor in mammals
    • DOI 10.1016/j.resp.2004.03.014, PII S1569904804000746
    • Heldmaier, G., Ortmann, S., and Elvert, R. (2004) Natural hypometabolism during hibernation and daily torpor in mammals. Respir. Physiol. Neurobiol. 141, 317-329 (Pubitemid 39013417)
    • (2004) Respiratory Physiology and Neurobiology , vol.141 , Issue.3 , pp. 317-329
    • Heldmaier, G.1    Ortmann, S.2    Elvert, R.3
  • 17
    • 0142126750 scopus 로고    scopus 로고
    • STOP Proteins
    • DOI 10.1021/bi0352163
    • Bosc, C., Andrieux, A., and Job, D. (2003) STOP proteins. Biochemistry 42, 12125-12132 (Pubitemid 37296488)
    • (2003) Biochemistry , vol.42 , Issue.42 , pp. 12125-12132
    • Bosc, C.1    Andrieux, A.2    Job, D.3
  • 18
    • 0038700687 scopus 로고    scopus 로고
    • Overlap of promoter and coding sequences in the mouse STOP gene (Mtap6)
    • DOI 10.1016/S0888-7543(03)00053-3
    • Aguezzoul, M., Andrieux, A., and Denarier, E. (2003) Overlap of promoter and coding sequences in the mouse STOP gene (Mtap6). Genomics 81, 623-627 (Pubitemid 36627505)
    • (2003) Genomics , vol.81 , Issue.6 , pp. 623-627
    • Aguezzoul, M.1    Andrieux, A.2    Denarier, E.3
  • 20
    • 0032514256 scopus 로고    scopus 로고
    • STOP proteins are responsible for the high degree of microtubule stabilization observed in neuronal cells
    • DOI 10.1083/jcb.142.1.167
    • Guillaud, L., Bosc, C., Fourest-Lieuvin, A., Denarier, E., Pirollet, F., Lafanechère, L., and Job, D. (1998) STOP proteins are responsible for the high degree of microtubule stabilization observed in neuronal cells. J. Cell Biol. 142, 167-179 (Pubitemid 28341148)
    • (1998) Journal of Cell Biology , vol.142 , Issue.1 , pp. 167-179
    • Guillaud, L.1    Bosc, C.2    Fourest-Lieuvin, A.3    Denarier, E.4    Pirollet, F.5    Lafanechere, L.6    Job, D.7
  • 21
    • 78650649948 scopus 로고    scopus 로고
    • Cold exposure reveals two populations of microtubules in pulmonary endothelia
    • Ochoa, C. D., Stevens, T., and Balczon, R. (2011) Cold exposure reveals two populations of microtubules in pulmonary endothelia. Am. J. Physiol. Lung Cell Mol. Physiol. 300, L132-L138
    • (2011) Am. J. Physiol. Lung Cell Mol. Physiol. , vol.300
    • Ochoa, C.D.1    Stevens, T.2    Balczon, R.3
  • 22
    • 0035903126 scopus 로고    scopus 로고
    • Identification of novel bifunctional calmodulin-binding and microtubule-stabilizing motifs in STOP proteins
    • Bosc, C., Frank, R., Denarier, E., Ronjat, M., Schweitzer, A., Wehland, J., and Job, D. (2001) Identification of novel bifunctional calmodulin-binding and microtubule-stabilizing motifs in STOP proteins. J. Biol. Chem. 276, 30904-30913
    • (2001) J. Biol. Chem. , vol.276 , pp. 30904-30913
    • Bosc, C.1    Frank, R.2    Denarier, E.3    Ronjat, M.4    Schweitzer, A.5    Wehland, J.6    Job, D.7
  • 23
    • 0028223232 scopus 로고
    • Intrinsic microtubule stability in interphase cells
    • Lieuvin, A., Labbé, J. C., Dorée, M., and Job, D. (1994) Intrinsic microtubule stability in interphase cells. J. Cell Biol. 124, 985-996 (Pubitemid 24109400)
    • (1994) Journal of Cell Biology , vol.124 , Issue.6 , pp. 985-996
    • Lieuvin, A.1    Labbe, J.-C.2    Doree, M.3    Job, D.4
  • 25
    • 84863205849 scopus 로고    scopus 로고
    • NIH Image to ImageJ: 25 Years of image analysis
    • Schneider, C. A., Rasband, W. S., and Eliceiri, K. W. (2012) NIH Image to ImageJ: 25 years of image analysis. Nat. Methods 9, 671-675
    • (2012) Nat. Methods , vol.9 , pp. 671-675
    • Schneider, C.A.1    Rasband, W.S.2    Eliceiri, K.W.3
  • 27
    • 0027501381 scopus 로고
    • Circular dichroic analysis of denatured proteins: Inclusion of denatured proteins in the reference set
    • DOI 10.1006/abio.1993.1450
    • Venyaminov, S. Y., Baikalov, I. A., Shen, Z. M., Wu, C. S., and Yang, J. T. (1993) Circular dichroic analysis of denatured proteins: inclusion of denatured proteins in the reference set. Anal. Biochem. 214, 17-24 (Pubitemid 23300347)
    • (1993) Analytical Biochemistry , vol.214 , Issue.1 , pp. 17-24
    • Venyaminov, S.Y.1    Baikalov, I.A.2    Shen, Z.M.3    Wu, C.-S.C.4    Yang, J.T.5
  • 28
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield, N., and Fasman, G. D. (1969) Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 8, 4108-4116
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.1    Fasman, G.D.2
  • 29
    • 0034658077 scopus 로고    scopus 로고
    • Structural transitions at microtubule ends correlate with their dynamic properties in Xenopus egg extracts
    • DOI 10.1083/jcb.149.4.767
    • Arnal, I., Karsenti, E., and Hyman, A. A. (2000) Structural transitions at microtubule ends correlate with their dynamic properties in Xenopus egg extracts. J. Cell Biol. 149, 767-774 (Pubitemid 30327229)
    • (2000) Journal of Cell Biology , vol.149 , Issue.4 , pp. 767-774
    • Arnal, I.1    Karsenti, E.2    Hyman, A.A.3
  • 30
    • 0029041404 scopus 로고
    • Structure of growing microtubule ends: Two-dimensional sheets close into tubes at variable rates
    • Chrétien, D., Fuller, S. D., and Karsenti, E. (1995) Structure of growing microtubule ends: two-dimensional sheets close into tubes at variable rates. J. Cell Biol. 129, 1311-1328
    • (1995) J. Cell Biol. , vol.129 , pp. 1311-1328
    • Chrétien, D.1    Fuller, S.D.2    Karsenti, E.3
  • 31
    • 2942657327 scopus 로고    scopus 로고
    • Mechanism of microtubule stabilization by doublecortin
    • DOI 10.1016/j.molcel.2004.06.009, PII S1097276504003296
    • Moores, C. A., Perderiset, M., Francis, F., Chelly, J., Houdusse, A., and Milligan, R. A. (2004) Mechanism of microtubule stabilization by doublecortin. Mol. Cell 14, 833-839 (Pubitemid 38780856)
    • (2004) Molecular Cell , vol.14 , Issue.6 , pp. 833-839
    • Moores, C.A.1    Perderiset, M.2    Francis, F.3    Chelly, J.4    Houdusse, A.5    Milligan, R.A.6
  • 33
    • 0023935365 scopus 로고
    • Heat-stable microtubule protein MAP-1 binds to microtubules and induces microtubule assembly
    • Vera, J. C., Rivas, C. I., and Maccioni, R. B. (1988) Heat-stable microtubule protein MAP-1 binds to microtubules and induces microtubule assembly. FEBS Lett. 232, 159-162
    • (1988) FEBS Lett. , vol.232 , pp. 159-162
    • Vera, J.C.1    Rivas, C.I.2    Maccioni, R.B.3
  • 35
    • 21644446496 scopus 로고    scopus 로고
    • Sites of tau important for aggregation populate β-structure and bind to microtubules and polyanions
    • DOI 10.1074/jbc.M501565200
    • Mukrasch, M. D., Biernat, J., von Bergen, M., Griesinger, C., Mandelkow, E., and Zweckstetter, M. (2005) Sites of tau important for aggregation populate {beta}-structure and bind to microtubules and polyanions. J. Biol. Chem. 280, 24978-24986 (Pubitemid 40934590)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.26 , pp. 24978-24986
    • Mukrasch, M.D.1    Biernat, J.2    Von Bergen, M.3    Griesinger, C.4    Mandelkow, E.5    Zweckstetter, M.6
  • 36
    • 0344737588 scopus 로고    scopus 로고
    • Stable Tubule only Polypeptides (STOP) Proteins Co-Aggregate with Spheroid Neurofilaments in Amyotrophic Lateral Sclerosis
    • Letournel, F., Bocquet, A., Dubas, F., Barthelaix, A., and Eyer, J. (2003) Stable tubule only polypeptides (STOP) proteins co-aggregate with spheroid neurofilaments in amyotrophic lateral sclerosis. J. Neuropathol. Exp. Neurol. 62, 1211-1219 (Pubitemid 37494190)
    • (2003) Journal of Neuropathology and Experimental Neurology , vol.62 , Issue.12 , pp. 1211-1219
    • Letournel, F.1    Bocquet, A.2    Dubas, F.3    Barthelaix, A.4    Eyer, J.5


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