메뉴 건너뛰기




Volumn 112, Issue 3, 1996, Pages 1079-1087

Evidence for opposing effects of calmodulin on cortical microtubules

Author keywords

[No Author keywords available]

Indexed keywords

DAUCUS CAROTA;

EID: 0029728952     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.112.3.1079     Document Type: Article
Times cited : (45)

References (48)
  • 1
    • 0010569906 scopus 로고
    • Calmodulin and calcium-binding proteins
    • PK Stumpf, ed, Academic Press, New York
    • Allan E, Hepler PK (1989) Calmodulin and calcium-binding proteins. In PK Stumpf, ed, The Biochemistry of Plants. Academic Press, New York, pp 455-484
    • (1989) The Biochemistry of Plants , pp. 455-484
    • Allan, E.1    Hepler, P.K.2
  • 3
    • 0025961398 scopus 로고
    • Purification and characterization of a brain-specific protein kinase C substrate, neurogranin (p17)
    • Baudier J, Deloulme JC, Van Dorsselaer A, Black D, Matthes HWD (1991) Purification and characterization of a brain-specific protein kinase C substrate, neurogranin (p17). J Biol Chem 266: 229-237
    • (1991) J Biol Chem , vol.266 , pp. 229-237
    • Baudier, J.1    Deloulme, J.C.2    Van Dorsselaer, A.3    Black, D.4    Matthes, H.W.D.5
  • 4
    • 0026659117 scopus 로고
    • Regulation of expression of calmodulin and calmodulin-related genes by environmental stimuli in plants
    • Braam J (1992) Regulation of expression of calmodulin and calmodulin-related genes by environmental stimuli in plants. Cell Calcium 13: 457-463
    • (1992) Cell Calcium , vol.13 , pp. 457-463
    • Braam, J.1
  • 5
    • 0025162096 scopus 로고
    • Rain-, wind-, and touch-induced expression of calmodulin and calmodulin-related genes in Arabidopsis
    • Braam J, Davis RW (1990) Rain-, wind-, and touch-induced expression of calmodulin and calmodulin-related genes in Arabidopsis. Cell 60: 357-364
    • (1990) Cell , vol.60 , pp. 357-364
    • Braam, J.1    Davis, R.W.2
  • 6
    • 0002424966 scopus 로고
    • Regulation of cytoplasmic calcium in plants
    • Bush DS (1993) Regulation of cytoplasmic calcium in plants. Plant Physiol 103: 7-13
    • (1993) Plant Physiol , vol.103 , pp. 7-13
    • Bush, D.S.1
  • 7
    • 0028855262 scopus 로고
    • Calcium regulation in plant cells and its role in signaling
    • Bush DS (1995) Calcium regulation in plant cells and its role in signaling. Annu Rev Plant Physiol Plant Mol Biol 46: 95-122
    • (1995) Annu Rev Plant Physiol Plant Mol Biol , vol.46 , pp. 95-122
    • Bush, D.S.1
  • 9
    • 0025992588 scopus 로고
    • Calcium/calmodulin affects microtubule stability in lysed protoplasts
    • Cyr RJ (1991a) Calcium/calmodulin affects microtubule stability in lysed protoplasts. J Cell Sci 100: 311-317
    • (1991) J Cell Sci , vol.100 , pp. 311-317
    • Cyr, R.J.1
  • 10
    • 0011866429 scopus 로고
    • Microtubule-associated proteins in higher plants
    • CW Lloyd, ed, Academic Press, San Diego, CA
    • Cyr RJ (1991b) Microtubule-associated proteins in higher plants. In CW Lloyd, ed, The Cytoskeletal Basis of Plant Growth and Form. Academic Press, San Diego, CA, pp 57-67
    • (1991) The Cytoskeletal Basis of Plant Growth and Form , pp. 57-67
    • Cyr, R.J.1
  • 11
    • 34249974738 scopus 로고
    • Microtubule-binding proteins from carrot. I. Initial characterization and microtubule bundling
    • Cyr RJ, Palevitz BA (1989) Microtubule-binding proteins from carrot. I. Initial characterization and microtubule bundling. Planta 177: 245-260
    • (1989) Planta , vol.177 , pp. 245-260
    • Cyr, R.J.1    Palevitz, B.A.2
  • 12
    • 0028954596 scopus 로고
    • Organization of cortical microtubules in plant cells
    • Cyr RJ, Palevitz BA (1995) Organization of cortical microtubules in plant cells. Curr Opin Cell Biol 7: 65-71
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 65-71
    • Cyr, R.J.1    Palevitz, B.A.2
  • 13
    • 0027951751 scopus 로고
    • Beyond translation: Elongation factor-1α and the cytoskeleton
    • Durso NA, Cyr RJ (1994a) Beyond translation: elongation factor-1α and the cytoskeleton. Protoplasma 180: 99-105
    • (1994) Protoplasma , vol.180 , pp. 99-105
    • Durso, N.A.1    Cyr, R.J.2
  • 14
    • 0028445306 scopus 로고
    • A calmodulin-sensitive interaction between microtubules and a higher plant homolog of elongation factor-1α
    • Durso NA, Cyr RJ (1994b) A calmodulin-sensitive interaction between microtubules and a higher plant homolog of elongation factor-1α. Plant Cell 6: 893-905
    • (1994) Plant Cell , vol.6 , pp. 893-905
    • Durso, N.A.1    Cyr, R.J.2
  • 15
    • 0030019097 scopus 로고    scopus 로고
    • In situ immunocytochemical evidence that a homolog of protein translation elongation factor EF-1α is associated with microtubules in carrot cells
    • Durso NA, Leslie JD, Cyr RJ (1996) In situ immunocytochemical evidence that a homolog of protein translation elongation factor EF-1α is associated with microtubules in carrot cells. Protoplasma 190: 141-150
    • (1996) Protoplasma , vol.190 , pp. 141-150
    • Durso, N.A.1    Leslie, J.D.2    Cyr, R.J.3
  • 16
    • 0027132676 scopus 로고
    • Calcium levels affect the ability to immunolocalize calmodulin to cortical microtubules
    • Fisher D, Cyr R (1993) Calcium levels affect the ability to immunolocalize calmodulin to cortical microtubules. Plant Physiol 103: 543-551
    • (1993) Plant Physiol , vol.103 , pp. 543-551
    • Fisher, D.1    Cyr, R.2
  • 17
    • 0028100469 scopus 로고
    • Mutational and biophysical studies suggest RC3/neurogranin regulates calmodulin availability
    • Gerendasy DD, Herron SR, Watson JB, Sutcliffe JG (1994) Mutational and biophysical studies suggest RC3/neurogranin regulates calmodulin availability. J Biol Chem 269: 22420-22426
    • (1994) J Biol Chem , vol.269 , pp. 22420-22426
    • Gerendasy, D.D.1    Herron, S.R.2    Watson, J.B.3    Sutcliffe, J.G.4
  • 18
    • 12044250989 scopus 로고
    • Role of calcium in signal transduction in Commelina guard cells
    • Gilroy S, Fricker MD, Read ND, Trewavas AJ (1991) Role of calcium in signal transduction in Commelina guard cells. Plant Cell 3: 333-344
    • (1991) Plant Cell , vol.3 , pp. 333-344
    • Gilroy, S.1    Fricker, M.D.2    Read, N.D.3    Trewavas, A.J.4
  • 19
    • 0023103656 scopus 로고
    • The measurements of intracellular calcium levels in protoplasts from higher plant cells
    • Gilroy S, Hughes WA, Trewavas AJ (1987) The measurements of intracellular calcium levels in protoplasts from higher plant cells. FEBS Lett 212: 133-137
    • (1987) FEBS Lett , vol.212 , pp. 133-137
    • Gilroy, S.1    Hughes, W.A.2    Trewavas, A.J.3
  • 21
    • 0020493109 scopus 로고
    • 2+-induced hydrophobic site on calmodulin: Application for purification of calmodulin by phenyl-Sepharose affinity chromatography
    • 2+-induced hydrophobic site on calmodulin: application for purification of calmodulin by phenyl-Sepharose affinity chromatography. Biochem Biophys Res Commun 104: 830-836
    • (1982) Biochem Biophys Res Commun , vol.104 , pp. 830-836
    • Gopalakrishna, R.1    Anderson, W.B.2
  • 23
    • 0001819040 scopus 로고
    • A calcium-dependent but calmodulin-independent protein kinase from soybean
    • Harmon AC, Putnam-Evans C, Cormier MS (1987) A calcium-dependent but calmodulin-independent protein kinase from soybean. Plant Physiol 83: 830-837
    • (1987) Plant Physiol , vol.83 , pp. 830-837
    • Harmon, A.C.1    Putnam-Evans, C.2    Cormier, M.S.3
  • 24
    • 0019792916 scopus 로고
    • Rapid disassembly of cold-stable microtubules by calmodulin
    • Job D, Fischer EH, Margolis RL (1981) Rapid disassembly of cold-stable microtubules by calmodulin. Proc Natl Acad Sci USA 78: 4679-4682
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 4679-4682
    • Job, D.1    Fischer, E.H.2    Margolis, R.L.3
  • 27
    • 0001110303 scopus 로고
    • 2+-induced fragmentation of actin filaments in pollen tubes
    • 2+-induced fragmentation of actin filaments in pollen tubes. Protoplasma 141: 177-179
    • (1987) Protoplasma , vol.141 , pp. 177-179
    • Kohno, T.1    Shimmen, T.2
  • 28
    • 0022235642 scopus 로고
    • Calmodulin inhibits interaction of actin with MAP2 and tau, two major microtubule-associated proteins
    • Kotani S, Nishida E, Kumagai H, Sakai H (1985) Calmodulin inhibits interaction of actin with MAP2 and tau, two major microtubule-associated proteins. J Biol Chem 260: 10779-10783
    • (1985) J Biol Chem , vol.260 , pp. 10779-10783
    • Kotani, S.1    Nishida, E.2    Kumagai, H.3    Sakai, H.4
  • 29
    • 0021357249 scopus 로고
    • Calmodulin binds to both microtubule-associated protein 2 and τ proteins
    • Lee Y, Wolff J (1984) Calmodulin binds to both microtubule-associated protein 2 and τ proteins. J Biol Chem 259: 1226-1230
    • (1984) J Biol Chem , vol.259 , pp. 1226-1230
    • Lee, Y.1    Wolff, J.2
  • 30
    • 1542788134 scopus 로고
    • Control of microtubule assembly-disassembly by calcium-dependent regulator protein
    • Marcum JM, Dedman JR, Brinkley BR, Means AR (1978) Control of microtubule assembly-disassembly by calcium-dependent regulator protein. Proc Natl Acad Sci USA 75: 3771-3775
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 3771-3775
    • Marcum, J.M.1    Dedman, J.R.2    Brinkley, B.R.3    Means, A.R.4
  • 31
    • 0022497883 scopus 로고
    • Purification and assay of a 145-kDa protein (STOP145) with microtubule-stabilizing and motility behavior
    • Margolis RL, Rauch CT, Job D (1986) Purification and assay of a 145-kDa protein (STOP145) with microtubule-stabilizing and motility behavior. Proc Natl Acad Sci USA 83: 639-643
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 639-643
    • Margolis, R.L.1    Rauch, C.T.2    Job, D.3
  • 32
    • 0026495206 scopus 로고
    • 2+-calmodulin regulated effectors of microtubule stability in neuronal tissues
    • 2+-calmodulin regulated effectors of microtubule stability in neuronal tissues. Biochim Biophys Acta 1160: 113-119
    • (1992) Biochim Biophys Acta , vol.1160 , pp. 113-119
    • Pirollet, F.1    Margolis, R.L.2    Job, D.3
  • 35
    • 11944252555 scopus 로고
    • Calcium-modulated proteins: Targets of intracellular calcium signals in higher plants
    • Roberts DM, Harmon AC (1992) Calcium-modulated proteins: targets of intracellular calcium signals in higher plants. Annu Rev Plant Physiol Plant Mol Biol 43: 375-414
    • (1992) Annu Rev Plant Physiol Plant Mol Biol , vol.43 , pp. 375-414
    • Roberts, D.M.1    Harmon, A.C.2
  • 36
    • 0026975054 scopus 로고
    • Higher plant microtubule-associated proteins (MAPs): A survey
    • Schellenbaum P, Vantard M, Lambert A (1992) Higher plant microtubule-associated proteins (MAPs): a survey. Biol Cell 76: 359-364
    • (1992) Biol Cell , vol.76 , pp. 359-364
    • Schellenbaum, P.1    Vantard, M.2    Lambert, A.3
  • 37
    • 0027134235 scopus 로고
    • Regulation by gibberellins of the orientation of cortical microtubules in plant cells
    • Shibaoka H (1993) Regulation by gibberellins of the orientation of cortical microtubules in plant cells. Aust J Plant Physiol 20: 461-470
    • (1993) Aust J Plant Physiol , vol.20 , pp. 461-470
    • Shibaoka, H.1
  • 39
    • 0024508661 scopus 로고
    • Axonal growth-associated proteins
    • Skene JHP (1989) Axonal growth-associated proteins. Annu Rev Neurosci 12: 127-156
    • (1989) Annu Rev Neurosci , vol.12 , pp. 127-156
    • Skene, J.H.P.1
  • 40
    • 0024244677 scopus 로고
    • Calmodulin stabilization of kinetochore microtubule structure to the effect of nocodazole
    • Sweet SC, Rogers CM, Welsh MJ (1988) Calmodulin stabilization of kinetochore microtubule structure to the effect of nocodazole. J Cell Biol 107: 2243-2251
    • (1988) J Cell Biol , vol.107 , pp. 2243-2251
    • Sweet, S.C.1    Rogers, C.M.2    Welsh, M.J.3
  • 43
    • 0028408958 scopus 로고
    • Taking a long, hard look at calmodulin's warm embrace
    • Török K, Whitaker M (1994) Taking a long, hard look at calmodulin's warm embrace. Bioessays 16: 221-224
    • (1994) Bioessays , vol.16 , pp. 221-224
    • Török, K.1    Whitaker, M.2
  • 44
    • 0025245420 scopus 로고
    • Calcium channels, stores, and oscillations
    • Tsien RW, Tsien RY (1990) Calcium channels, stores, and oscillations. Annu Rev Cell Biol 6: 715-760
    • (1990) Annu Rev Cell Biol , vol.6 , pp. 715-760
    • Tsien, R.W.1    Tsien, R.Y.2
  • 45
    • 0022111816 scopus 로고
    • Characterization and immunocytochemical distribution of calmodulin in higher plant endosperm cells: Localization in the mitotic apparatus
    • Vantard M, Lambert A-M, De Mey J, Picquot P, Van Eldik LJ (1985) Characterization and immunocytochemical distribution of calmodulin in higher plant endosperm cells: localization in the mitotic apparatus. J Cell Biol 101: 488-499
    • (1985) J Cell Biol , vol.101 , pp. 488-499
    • Vantard, M.1    Lambert, A.-M.2    De Mey, J.3    Picquot, P.4    Van Eldik, L.J.5
  • 46
    • 0018746497 scopus 로고
    • Tubulin and calmodulin: Effects of microtubule and microfilament inhibitors on localization in the mitotic apparatus
    • Welsh MJ, Dedman JR, Brinkley BR, Means AR (1979) Tubulin and calmodulin: effects of microtubule and microfilament inhibitors on localization in the mitotic apparatus. J Cell Biol 81: 624-634
    • (1979) J Cell Biol , vol.81 , pp. 624-634
    • Welsh, M.J.1    Dedman, J.R.2    Brinkley, B.R.3    Means, A.R.4
  • 47
    • 0000484778 scopus 로고
    • Double immunofluorescence labeling of calmodulin and tubulin in dividing plant cells
    • Wick SM, Muto S, Duniec J (1985) Double immunofluorescence labeling of calmodulin and tubulin in dividing plant cells. Protoplasma 126: 198-206
    • (1985) Protoplasma , vol.126 , pp. 198-206
    • Wick, S.M.1    Muto, S.2    Duniec, J.3
  • 48
    • 0002760238 scopus 로고
    • Structure and evolution of the calmodulin family of calcium regulatory proteins
    • P Cohen, CB Klee, eds, Elsevier, Amsterdam
    • Wylie DC, Vanaman TC (1988) Structure and evolution of the calmodulin family of calcium regulatory proteins. In P Cohen, CB Klee, eds, Calmodulin, Vol 5: Molecular Aspects of Cellular Regulation. Elsevier, Amsterdam, pp 1-15
    • (1988) Calmodulin, Vol 5: Molecular Aspects of Cellular Regulation , vol.5 , pp. 1-15
    • Wylie, D.C.1    Vanaman, T.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.