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Volumn 244, Issue 3, 2000, Pages 153-166

Posttranslationally modified tubulins and microtubule organization in hemocytes of the brine shrimp, Artemia franciscana

Author keywords

Artemia; Crustacean; Hemocyte; Microtubule; Posttranslationally modified tubulin

Indexed keywords

CELL EXTRACT; TUBULIN;

EID: 0034083068     PISSN: 03622525     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4687(200006)244:3<153::AID-JMOR1>3.0.CO;2-T     Document Type: Article
Times cited : (8)

References (55)
  • 1
    • 0033007989 scopus 로고    scopus 로고
    • Balanced regulation of microtubule dynamics during the cell cycle: A contemporary view
    • Andersen SSL. 1999. Balanced regulation of microtubule dynamics during the cell cycle: a contemporary view. BioEssays 21: 53-60.
    • (1999) BioEssays , vol.21 , pp. 53-60
    • Andersen, S.S.L.1
  • 3
    • 0014735453 scopus 로고
    • Cellular aspects of blood clotting in the seastar and the hermit crab
    • Bang FB. 1970. Cellular aspects of blood clotting in the seastar and the hermit crab. J Reticuloendothel Soc 7:161-172.
    • (1970) J Reticuloendothel Soc , vol.7 , pp. 161-172
    • Bang, F.B.1
  • 4
    • 38249037676 scopus 로고
    • Light and electron microscopy of the hemocytes of Ligia oceanica (L.) (Crustacea: Isopoda)
    • Benjamin LR, James BL. 1987. Light and electron microscopy of the hemocytes of Ligia oceanica (L.) (Crustacea: Isopoda). J Invert Pathol 49:19-25.
    • (1987) J Invert Pathol , vol.49 , pp. 19-25
    • Benjamin, L.R.1    James, B.L.2
  • 5
    • 0023582253 scopus 로고
    • Control of microtubule nucleation and stability in Madin-Darby canine kidney cells: The occurrence of noncentrosomal, stable detyrosinated microtubules
    • Bré H, Kreis TE, Karsenti E. 1987. Control of microtubule nucleation and stability in Madin-Darby canine kidney cells: the occurrence of noncentrosomal, stable detyrosinated microtubules. J Cell Biol 105:1283-1296.
    • (1987) J Cell Biol , vol.105 , pp. 1283-1296
    • Bré, H.1    Kreis, T.E.2    Karsenti, E.3
  • 6
    • 0028924760 scopus 로고
    • Comparison of antibacterial activity in the hemocytes of different crustacean species
    • Chisholm JRS, Smith VJ. 1995. Comparison of antibacterial activity in the hemocytes of different crustacean species. Comp Biochem Physiol 110A:39-45.
    • (1995) Comp Biochem Physiol , vol.110 A , pp. 39-45
    • Chisholm, J.R.S.1    Smith, V.J.2
  • 7
    • 0342557926 scopus 로고
    • Marginal bands of lobster blood cells: Disappearance associated with changes in cell morphology
    • Cohen WD, Nemhauser I, Cohen MF. 1983. Marginal bands of lobster blood cells: disappearance associated with changes in cell morphology. Biol Bull 164:50-61.
    • (1983) Biol Bull , vol.164 , pp. 50-61
    • Cohen, W.D.1    Nemhauser, I.2    Cohen, M.F.3
  • 11
    • 2642626625 scopus 로고    scopus 로고
    • Dictyostelium γ-tubulin: Molecular characterization and ultrastructural localization
    • Euteneuer U, Gräf R, Kube-Granderath E, Schliwa M. 1998. Dictyostelium γ-tubulin: molecular characterization and ultrastructural localization. J Cell Sci 111:405-412.
    • (1998) J Cell Sci , vol.111 , pp. 405-412
    • Euteneuer, U.1    Gräf, R.2    Kube-Granderath, E.3    Schliwa, M.4
  • 12
    • 0023794840 scopus 로고
    • Selective stabilization of microtubules oriented toward the direction of cell migration
    • Gundersen GG, Bulinski JC. 1988. Selective stabilization of microtubules oriented toward the direction of cell migration. Proc Natl Acad Sci USA 85 5946-5950.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 5946-5950
    • Gundersen, G.G.1    Bulinski, J.C.2
  • 13
    • 38249022277 scopus 로고
    • Defense functions of granulocytes in the ridgeback prawn Sicyonia ingentis
    • Hose JE, Martin GG. 1989. Defense functions of granulocytes in the ridgeback prawn Sicyonia ingentis. J Invert Pathol 53:335-346.
    • (1989) J Invert Pathol , vol.53 , pp. 335-346
    • Hose, J.E.1    Martin, G.G.2
  • 15
    • 0002945967 scopus 로고
    • A decapod hemocyte classification scheme integrating morphology, cytochemistry, and function
    • Hose JE, Martin GG, Gerard AS. 1990. A decapod hemocyte classification scheme integrating morphology, cytochemistry, and function. Biol Bull 178:33-45.
    • (1990) Biol Bull , vol.178 , pp. 33-45
    • Hose, J.E.1    Martin, G.G.2    Gerard, A.S.3
  • 16
    • 0000771005 scopus 로고
    • Patterns of hemocyte production and release throughout the molt cycle in the penaeid shrimp Sicyonia ingentis
    • Hose JE, Martin GG, Tiu S, McKrell N. 1992. Patterns of hemocyte production and release throughout the molt cycle in the penaeid shrimp Sicyonia ingentis. Biol Bull 183:185-199.
    • (1992) Biol Bull , vol.183 , pp. 185-199
    • Hose, J.E.1    Martin, G.G.2    Tiu, S.3    McKrell, N.4
  • 17
    • 0030893287 scopus 로고    scopus 로고
    • Structurally similar Drosophila α-tubulins are functionally distinct in vivo
    • Hutchens JA, Hoyle HD, Turner FR, Raff EC. 1997. Structurally similar Drosophila α-tubulins are functionally distinct in vivo. Mol Biol Cell 8:481-500.
    • (1997) Mol Biol Cell , vol.8 , pp. 481-500
    • Hutchens, J.A.1    Hoyle, H.D.2    Turner, F.R.3    Raff, E.C.4
  • 18
    • 0031934614 scopus 로고    scopus 로고
    • New types of clotting factors and defense molecules found in horseshoe crab hemolymph: Their structures and functions
    • Iwanaga S, Kawabata S-i, Muta T. 1998. New types of clotting factors and defense molecules found in horseshoe crab hemolymph: their structures and functions. J Biochem (Tokyo) 123: 1-15.
    • (1998) J Biochem (Tokyo) , vol.123 , pp. 1-15
    • Iwanaga, S.1    Kawabata, S.-I.2    Muta, T.3
  • 19
    • 0032941748 scopus 로고    scopus 로고
    • Detyrosination of tubulin regulates the interaction of intermediate filaments with microtubules in vivo via a kinesin-dependent mechanism
    • Kreitzer G, Liao G, Gundersen GG. 1999. Detyrosination of tubulin regulates the interaction of intermediate filaments with microtubules in vivo via a kinesin-dependent mechanism. Mol Biol Cell 10:1105-1118.
    • (1999) Mol Biol Cell , vol.10 , pp. 1105-1118
    • Kreitzer, G.1    Liao, G.2    Gundersen, G.G.3
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 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
  • 21
    • 0030627521 scopus 로고    scopus 로고
    • Tubulin synthesis and assembly in differentiating neurons
    • Laferrière NB, MacRae TH, Brown DL. 1997. Tubulin synthesis and assembly in differentiating neurons. Biochem Cell Biol 75:103-117.
    • (1997) Biochem Cell Biol , vol.75 , pp. 103-117
    • Laferrière, N.B.1    MacRae, T.H.2    Brown, D.L.3
  • 22
    • 0025370112 scopus 로고
    • Tubulin isoforms in the brine shrimp, Artemia: Primary gene products and their posttranslational modification
    • Langdon CM, Bagshaw JC, MacRae TH. 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
    • 0026038630 scopus 로고
    • Posttranslationally modified tubulins in Artemia: Prelarval development in the absence of detyrosinated tubulin
    • Langdon CM, Freeman JA, MacRae TH. 1991. Posttranslationally modified tubulins in Artemia: prelarval development in the absence of detyrosinated tubulin. Dev Biol 148: 147-155.
    • (1991) Dev Biol , vol.148 , pp. 147-155
    • Langdon, C.M.1    Freeman, J.A.2    MacRae, T.H.3
  • 24
    • 0027361787 scopus 로고
    • Morphological and biochemical characterization of Procambarus clarki blood cells
    • Lanz H, Tsutsumi V, Aréchiga H. 1993. Morphological and biochemical characterization of Procambarus clarki blood cells. Dev Comp Immunol 17:389-397.
    • (1993) Dev Comp Immunol , vol.17 , pp. 389-397
    • Lanz, H.1    Tsutsumi, V.2    Aréchiga, H.3
  • 25
    • 0023389780 scopus 로고
    • Identification of an acetylation site of Chlamydomonas α-tubulin
    • LeDizet M, Piperno G. 1987. Identification of an acetylation site of Chlamydomonas α-tubulin. Proc Natl Acad Sci USA 84: 5720-5724.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5720-5724
    • LeDizet, M.1    Piperno, G.2
  • 26
    • 0031020927 scopus 로고    scopus 로고
    • Purification, structure and in vitro molecular-chaperone activity of Artemia p26, a small heat-shock/α-crystallin protein
    • Liang P, Amons R, MacRae TH, Clegg JS. 1997. Purification, structure and in vitro molecular-chaperone activity of Artemia p26, a small heat-shock/α-crystallin protein. Eur J Biochem 243:225-232.
    • (1997) Eur J Biochem , vol.243 , pp. 225-232
    • Liang, P.1    Amons, R.2    MacRae, T.H.3    Clegg, J.S.4
  • 27
    • 84982057489 scopus 로고
    • Studies on the blood and related tissues in Artemia (Crustacea, Anostraca)
    • Lockhead JH, Lockhead MS. 1941. Studies on the blood and related tissues in Artemia (Crustacea, Anostraca). J Morphol 68:593-632.
    • (1941) J Morphol , vol.68 , pp. 593-632
    • Lockhead, J.H.1    Lockhead, M.S.2
  • 29
    • 0030709242 scopus 로고    scopus 로고
    • Multiple forms of tubulin: Different gene products and covalent modifications
    • Ludueña RF. 1998. Multiple forms of tubulin: different gene products and covalent modifications. Int Rev Cytol 178:207-275.
    • (1998) Int Rev Cytol , vol.178 , pp. 207-275
    • Ludueña, R.F.1
  • 30
    • 0026936813 scopus 로고
    • Towards an understanding of microtubule function and cell organization: An overview
    • MacRae TH. 1992. Towards an understanding of microtubule function and cell organization: an overview. Biochem Cell Biol 70:835-841.
    • (1992) Biochem Cell Biol , vol.70 , pp. 835-841
    • MacRae, T.H.1
  • 31
    • 0031039519 scopus 로고    scopus 로고
    • Tubulin post-translational modifications. Enzymes and their mechanisms of action
    • MacRae TH. 1997. Tubulin post-translational modifications. Enzymes and their mechanisms of action. Eur J Biochem 244:265-278.
    • (1997) Eur J Biochem , vol.244 , pp. 265-278
    • MacRae, T.H.1
  • 32
    • 0021413722 scopus 로고
    • Developmental and comparative aspects of brine shrimp tubulin
    • MacRae TH, Ludueña RF. 1984. Developmental and comparative aspects of brine shrimp tubulin. Biochem J 219:137-148.
    • (1984) Biochem J , vol.219 , pp. 137-148
    • MacRae, T.H.1    Ludueña, R.F.2
  • 33
    • 0026019425 scopus 로고
    • Spatial distribution of post-translationally modified tubulins in polarized cells of developing Artemia
    • MacRae TH, Langdon CM, Freeman JA. 1991. Spatial distribution of post-translationally modified tubulins in polarized cells of developing Artemia. Cell Motil Cytoskel 18:189-203.
    • (1991) Cell Motil Cytoskel , vol.18 , pp. 189-203
    • MacRae, T.H.1    Langdon, C.M.2    Freeman, J.A.3
  • 34
    • 0000173661 scopus 로고
    • Vascular elements and blood (hemolymph)
    • Harrison FW, Humes AG, editors. New York: Wiley-Liss
    • Martin GG, Hose JE. 1992. Vascular elements and blood (hemolymph). In: Harrison FW, Humes AG, editors. Microscopic anatomy of invertebrates, vol. 10. New York: Wiley-Liss. p 117-146.
    • (1992) Microscopic Anatomy of Invertebrates , vol.10 , pp. 117-146
    • Martin, G.G.1    Hose, J.E.2
  • 35
    • 0025790041 scopus 로고
    • Localization and roles of coagulogen and transglutaminase in hemolymph coagulation in decapod crustaceans
    • Martin GG, Hose JE, Omori S, Chong C, Hoodbhoy T, McKrell N. 1991. Localization and roles of coagulogen and transglutaminase in hemolymph coagulation in decapod crustaceans. Comp Biochem Physiol 100B:517-522.
    • (1991) Comp Biochem Physiol , vol.100 B , pp. 517-522
    • Martin, G.G.1    Hose, J.E.2    Omori, S.3    Chong, C.4    Hoodbhoy, T.5    McKrell, N.6
  • 37
    • 0030044895 scopus 로고    scopus 로고
    • Clearance of bacteria injected into the hemolymph of the ridgeback prawn, Sicyonia ingentis (Crustacea: Decapoda): Role of hematopoietic tissue
    • Martin GG, Hose JE, Minka G, Rosenberg S. 1996. Clearance of bacteria injected into the hemolymph of the ridgeback prawn, Sicyonia ingentis (Crustacea: Decapoda): role of hematopoietic tissue. J Morphol 227:227-233.
    • (1996) J Morphol , vol.227 , pp. 227-233
    • Martin, G.G.1    Hose, J.E.2    Minka, G.3    Rosenberg, S.4
  • 38
    • 0032221966 scopus 로고    scopus 로고
    • In vitro nodule formation in the ridgeback prawn, Sicyonia ingentis, and the American lobster, Homarus americanus
    • Martin GG, Kay J, Poole D, Poole C. 1998. In vitro nodule formation in the ridgeback prawn, Sicyonia ingentis, and the American lobster, Homarus americanus. Invert Biol 117:155-168.
    • (1998) Invert Biol , vol.117 , pp. 155-168
    • Martin, G.G.1    Kay, J.2    Poole, D.3    Poole, C.4
  • 39
    • 0022452231 scopus 로고
    • The acetylation of alpha-tubulin and its relationship to the assembly and disassembly of microtubules
    • Maruta H, Greer K, Rosenbaum JL. 1986. The acetylation of alpha-tubulin and its relationship to the assembly and disassembly of microtubules. J Cell Biol 103:571-579.
    • (1986) J Cell Biol , vol.103 , pp. 571-579
    • Maruta, H.1    Greer, K.2    Rosenbaum, J.L.3
  • 40
    • 0031854868 scopus 로고    scopus 로고
    • Recruitment of the γ-tubulin ring complex to Drosophila salt-stripped centrosome scaffolds
    • Moritz M, Zheng Y, Alberts BM, Oegema K. 1998. Recruitment of the γ-tubulin ring complex to Drosophila salt-stripped centrosome scaffolds. J Cell Biol 142:775-786.
    • (1998) J Cell Biol , vol.142 , pp. 775-786
    • Moritz, M.1    Zheng, Y.2    Alberts, B.M.3    Oegema, K.4
  • 41
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the αβ tubulin dimer by electron crystallography
    • Nogales E, Wolf SG, Downing KH. 1998. Structure of the αβ tubulin dimer by electron crystallography. Nature 391:199-203.
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 44
    • 0024589503 scopus 로고
    • Identification of γ-tubulin, a new member of the tubulin superfamily encoded by mipA gene of Aspergillus nidulans
    • Oakley CE, Oakley BR. 1989. Identification of γ-tubulin, a new member of the tubulin superfamily encoded by mipA gene of Aspergillus nidulans. Nature 338:662-664.
    • (1989) Nature , vol.338 , pp. 662-664
    • Oakley, C.E.1    Oakley, B.R.2
  • 45
    • 0031050544 scopus 로고    scopus 로고
    • Centrosome-microtubule nucleation
    • Pereira G, Schiebel E. 1997. Centrosome-microtubule nucleation. J Cell Sci 110:295-300.
    • (1997) J Cell Sci , vol.110 , pp. 295-300
    • Pereira, G.1    Schiebel, E.2
  • 47
    • 0032030168 scopus 로고    scopus 로고
    • Assembly and colchicine binding characteristics of tubulin with maximally tyrosinated and detyrosinated α-tubulins
    • Skoufias DA, Wilson L. 1998. Assembly and colchicine binding characteristics of tubulin with maximally tyrosinated and detyrosinated α-tubulins. Arch Biochem Biophys 351:115-122.
    • (1998) Arch Biochem Biophys , vol.351 , pp. 115-122
    • Skoufias, D.A.1    Wilson, L.2
  • 48
    • 0033080404 scopus 로고    scopus 로고
    • Role of microtubules in the organization of the Golgi complex
    • Thyberg J, Moskalewski S. 1999. Role of microtubules in the organization of the Golgi complex. Exp Cell Res 246:263-279.
    • (1999) Exp Cell Res , vol.246 , pp. 263-279
    • Thyberg, J.1    Moskalewski, S.2
  • 49
    • 0002872361 scopus 로고
    • Hemocytes of penaeid and palaemonid shrimps: Morphology, cytochemistry, and hemograms
    • Tsing A, Arcier J-M, Brehélin M. 1989. Hemocytes of penaeid and palaemonid shrimps: morphology, cytochemistry, and hemograms. J Invert Path 53:64-77.
    • (1989) J Invert Path , vol.53 , pp. 64-77
    • Tsing, A.1    Arcier, J.-M.2    Brehélin, M.3
  • 50
    • 0031880573 scopus 로고    scopus 로고
    • Characterization of γ-tubulin in Artemia: Isoform composition and spatial distribution in polarized cells of the larval epidermis
    • Walling MA, Criel GRJ, MacRae TH. 1998. Characterization of γ-tubulin in Artemia: isoform composition and spatial distribution in polarized cells of the larval epidermis. Cell Motil Cytoskel 40:331-341.
    • (1998) Cell Motil Cytoskel , vol.40 , pp. 331-341
    • Walling, M.A.1    Criel, G.R.J.2    MacRae, T.H.3
  • 51
    • 0026636867 scopus 로고
    • Regulation of cytoplasmic carboxypeptidase activity during neural and muscle differentiation: Characterization using a microtubule-based assay
    • Webster DR, Modesti NM, Bulinski JC. 1992. Regulation of cytoplasmic carboxypeptidase activity during neural and muscle differentiation: characterization using a microtubule-based assay. Biochemistry 31:5849-5856.
    • (1992) Biochemistry , vol.31 , pp. 5849-5856
    • Webster, D.R.1    Modesti, N.M.2    Bulinski, J.C.3
  • 52
    • 0023406178 scopus 로고
    • Turnover of the carboxy-terminal tyrosine of α-tubulin and means of reaching elevated levels of detyrosination in living cells
    • Wehland J, Weber K. 1987. Turnover of the carboxy-terminal tyrosine of α-tubulin and means of reaching elevated levels of detyrosination in living cells. J Cell Sci 88:185-203.
    • (1987) J Cell Sci , vol.88 , pp. 185-203
    • Wehland, J.1    Weber, K.2
  • 53
    • 0031569552 scopus 로고    scopus 로고
    • Differential expression of two γ-tubulin isoforms during gametogenesis and development in Drosophila
    • Wilson PG, Zheng Y, Oakley CE, Oakley BR, Borisy GG, Fuller MT. 1997. Differential expression of two γ-tubulin isoforms during gametogenesis and development in Drosophila. Dev Biol 184:207-221.
    • (1997) Dev Biol , vol.184 , pp. 207-221
    • Wilson, P.G.1    Zheng, Y.2    Oakley, C.E.3    Oakley, B.R.4    Borisy, G.G.5    Fuller, M.T.6
  • 54
    • 0024369960 scopus 로고
    • Definition of individual components within the cytoskeleton of Trypanosoma brucei by a library of monoclonal antibodies
    • Woods A, Sherwin T, Sasse R, MacRae TH, Baines AJ, Gull K. 1989. Definition of individual components within the cytoskeleton of Trypanosoma brucei by a library of monoclonal antibodies. J Cell Sci 93:491-500.
    • (1989) J Cell Sci , vol.93 , pp. 491-500
    • Woods, A.1    Sherwin, T.2    Sasse, R.3    MacRae, T.H.4    Baines, A.J.5    Gull, K.6
  • 55
    • 0029363669 scopus 로고
    • Production and utilization of detyrosinated tubulin in developing Artemia larvae: Evidence for a tubulin-reactive carboxypeptidase
    • Xiang H, MacRae TH. 1995. Production and utilization of detyrosinated tubulin in developing Artemia larvae: evidence for a tubulin-reactive carboxypeptidase. Biochem Cell Biol 73:673-685.
    • (1995) Biochem Cell Biol , vol.73 , pp. 673-685
    • Xiang, H.1    MacRae, T.H.2


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