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Volumn 134, Issue 3, 1996, Pages 675-687

Xenopus nonmuscle myosin heavy chain isoforms have different subcellular localizations and enzymatic activities

Author keywords

[No Author keywords available]

Indexed keywords

MYOSIN HEAVY CHAIN;

EID: 0029782819     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.134.3.675     Document Type: Article
Times cited : (143)

References (47)
  • 1
    • 0018638822 scopus 로고
    • Analysis of actin and microfilament associated proteins in the mitotic spindle and cleavage furrow of PtK2 cells by immunofluorescence
    • Aubin, J.E., W. Weber, and M. Osborn. 1979. Analysis of actin and microfilament associated proteins in the mitotic spindle and cleavage furrow of PtK2 cells by immunofluorescence. Exp. Cell Res. 124:93-109.
    • (1979) Exp. Cell Res. , vol.124 , pp. 93-109
    • Aubin, J.E.1    Weber, W.2    Osborn, M.3
  • 2
    • 0342996932 scopus 로고
    • Acanthamoeba castellanii: A model system for correlative biochemical and cell biological studies
    • Academic Press, Aarhus, Denmark, J.E. Celis, editor
    • Baines, I.C., and E.D. Korn. 1994. Acanthamoeba castellanii: a model system for correlative biochemical and cell biological studies. In Cell Biology: A Laboratory Handbook. Academic Press, Aarhus, Denmark, J.E. Celis, editor, pp. 405-411.
    • (1994) Cell Biology: A Laboratory Handbook , pp. 405-411
    • Baines, I.C.1    Korn, E.D.2
  • 3
    • 0029148548 scopus 로고
    • Quantification and localization of phosphorylated myosin I isoforms in Acanthamoeba castellanii
    • Baines, I.C., A. Corigliano-Murphy, and E.D. Korn. 1995. Quantification and localization of phosphorylated myosin I isoforms in Acanthamoeba castellanii. J. Cell Biol. 130:591-603.
    • (1995) J. Cell Biol. , vol.130 , pp. 591-603
    • Baines, I.C.1    Corigliano-Murphy, A.2    Korn, E.D.3
  • 4
    • 0027530939 scopus 로고
    • Cloning of the cDNA encoding a myosin heavy chain B isoform of Xenopus nonmuscle myosin with an insert in the head region
    • Bhatia-Dey, N., R.S. Adelstein, and I.B. Dawid. 1993. Cloning of the cDNA encoding a myosin heavy chain B isoform of Xenopus nonmuscle myosin with an insert in the head region. Proc. Natl. Acad. Sci. USA. 90: 2856-2859.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2856-2859
    • Bhatia-Dey, N.1    Adelstein, R.S.2    Dawid, I.B.3
  • 5
    • 0026757844 scopus 로고
    • Localization of myosin-IIB at the leading edge of growth cones from rat dorsal-root ganglionic cells
    • Cheng, T. P.O., N. Murakami, and M. Elzinga. 1992. Localization of myosin-IIB at the leading edge of growth cones from rat dorsal-root ganglionic cells. FEBS Lett. 311:91-94.
    • (1992) FEBS Lett. , vol.311 , pp. 91-94
    • Cheng, T.P.O.1    Murakami, N.2    Elzinga, M.3
  • 6
    • 0025291420 scopus 로고
    • Alternative myosin hinge regions are utilized in a tissue-specific fashion that correlates with muscle contraction speed
    • Collier, V.L., W.A. Kronert, P.T. O'Donnell, K.A. Edwards, and S.I. Bernstein. 1990. Alternative myosin hinge regions are utilized in a tissue-specific fashion that correlates with muscle contraction speed. Genes Dev. 6: 885-895.
    • (1990) Genes Dev. , vol.6 , pp. 885-895
    • Collier, V.L.1    Kronert, W.A.2    O'Donnell, P.T.3    Edwards, K.A.4    Bernstein, S.I.5
  • 7
    • 0027523460 scopus 로고
    • Relative distribution of actin, myosin I, and myosin II during the wound healing response of fibroblasts
    • Conrad, P.A., K.A. Giuliano, G. Fisher, K. Collins, P.T. Matsudaira, and D.L. Taylor. 1993. Relative distribution of actin, myosin I, and myosin II during the wound healing response of fibroblasts. J. Cell Biol. 120:1381-1391.
    • (1993) J. Cell Biol. , vol.120 , pp. 1381-1391
    • Conrad, P.A.1    Giuliano, K.A.2    Fisher, G.3    Collins, K.4    Matsudaira, P.T.5    Taylor, D.L.6
  • 8
    • 0024513698 scopus 로고
    • Molecular genetic characterization of a developmentally regulated human perinatal myosin heavy chain
    • Feghali, R., and L.A. Leinwand. 1989. Molecular genetic characterization of a developmentally regulated human perinatal myosin heavy chain. J. Cell Biol. 108:1791-1797.
    • (1989) J. Cell Biol. , vol.108 , pp. 1791-1797
    • Feghali, R.1    Leinwand, L.A.2
  • 9
    • 0017109215 scopus 로고
    • Fluorescent antibody localization of myosin in the cytoplasm, cleavage furrow and mitotic spindle of human cells
    • Fujiwara, K., and T.D. Pollard. 1976. Fluorescent antibody localization of myosin in the cytoplasm, cleavage furrow and mitotic spindle of human cells. J. Cell Biol. 71:848-875.
    • (1976) J. Cell Biol. , vol.71 , pp. 848-875
    • Fujiwara, K.1    Pollard, T.D.2
  • 10
    • 0024956931 scopus 로고
    • Myosin I is located at the leading edges of locomoting Dictyostelium amoeba
    • Fukui, Y., T.J. Lynch, H. Brzeska, and E.D. Korn. 1989. Myosin I is located at the leading edges of locomoting Dictyostelium amoeba. Nature (Lond.). 341:328-331.
    • (1989) Nature (Lond.) , vol.341 , pp. 328-331
    • Fukui, Y.1    Lynch, T.J.2    Brzeska, H.3    Korn, E.D.4
  • 11
    • 0025192475 scopus 로고
    • Structure and function of the cytoskeleton of a Dictyostelium myosin-defective mutant
    • Fukui, Y., A. De Lozanne, and J. A. Spudich. 1990. Structure and function of the cytoskeleton of a Dictyostelium myosin-defective mutant. J. Cell Biol. 110:367-378.
    • (1990) J. Cell Biol. , vol.110 , pp. 367-378
    • Fukui, Y.1    De Lozanne, A.2    Spudich, J.A.3
  • 12
    • 0027712834 scopus 로고
    • Confocal immunofluorescence microscopy of microtubules in amphibian oocytes and eggs
    • Gard, D.L. 1993. Confocal immunofluorescence microscopy of microtubules in amphibian oocytes and eggs. Methods Cell Biol. 38:241-264.
    • (1993) Methods Cell Biol. , vol.38 , pp. 241-264
    • Gard, D.L.1
  • 13
    • 0025371941 scopus 로고
    • Centrosome duplication continues in cyclohexamide-treated Xenopus blastulae in the absence of a detectable cell cycle
    • Gard, D.L., S. Hafezi, T. Zhang, and S.J. Doxsey. 1990. Centrosome duplication continues in cyclohexamide-treated Xenopus blastulae in the absence of a detectable cell cycle. J. Cell Biol. 110:2033-2042.
    • (1990) J. Cell Biol. , vol.110 , pp. 2033-2042
    • Gard, D.L.1    Hafezi, S.2    Zhang, T.3    Doxsey, S.J.4
  • 14
    • 0025136293 scopus 로고
    • Formation, transport, contraction, and disassembly of stress fibers in fibroblasts
    • Giuliano, K.A., and D.L. Taylor. 1990. Formation, transport, contraction, and disassembly of stress fibers in fibroblasts. Cell Motil. Cytoskeleton. 16:14-21.
    • (1990) Cell Motil. Cytoskeleton , vol.16 , pp. 14-21
    • Giuliano, K.A.1    Taylor, D.L.2
  • 15
    • 0001068154 scopus 로고
    • Biochemistry of the contractile process in smooth muscle
    • L.R. Johnson, editor. Raven Press, New York
    • Hartshorne, D.J. 1987. Biochemistry of the contractile process in smooth muscle. In Physiology of the Gastrointestinal Tract. L.R. Johnson, editor. Raven Press, New York. pp. 423-482.
    • (1987) Physiology of the Gastrointestinal Tract , pp. 423-482
    • Hartshorne, D.J.1
  • 16
    • 0026700379 scopus 로고
    • Role of the COOH-terminal nonhelical tailpiece in the assembly of a vertebrate nonmuscle myosin rod
    • Hodge, T.P., R. Cross, and J. Kendrick Jones. 1992. Role of the COOH-terminal nonhelical tailpiece in the assembly of a vertebrate nonmuscle myosin rod. J. Cell Biol. 118:1085-1095.
    • (1992) J. Cell Biol. , vol.118 , pp. 1085-1095
    • Hodge, T.P.1    Cross, R.2    Kendrick Jones, J.3
  • 17
    • 0024438147 scopus 로고
    • Two distinct nonmuscle myosin heavy chain mRNAs are differently expressed in various chicken tissues
    • Katsuragawa, Y., M. Yanagisawa, A. Inoue, and T. Masaki. 1989. Two distinct nonmuscle myosin heavy chain mRNAs are differently expressed in various chicken tissues. Eur. J. Biochem. 184:611-616.
    • (1989) Eur. J. Biochem. , vol.184 , pp. 611-616
    • Katsuragawa, Y.1    Yanagisawa, M.2    Inoue, A.3    Masaki, T.4
  • 18
    • 0026029783 scopus 로고
    • Chicken nonmuscle myosin heavy chains: Differential expression of two mRNAs and evidence for two different polypeptides
    • Kawamoto, S., and R.S. Adelstein. 1991 Chicken nonmuscle myosin heavy chains: differential expression of two mRNAs and evidence for two different polypeptides. J. Cell Biol. 112:915-924.
    • (1991) J. Cell Biol. , vol.112 , pp. 915-924
    • Kawamoto, S.1    Adelstein, R.S.2
  • 19
    • 0025092579 scopus 로고
    • The 204-kDa smooth muscle myosin heavy chain is phosphorylated in intact cells by casein kinase II on a serine near the carboxyl-terminus
    • Kelley, C.A., and R.S. Adelstein. 1990. The 204-kDa smooth muscle myosin heavy chain is phosphorylated in intact cells by casein kinase II on a serine near the carboxyl-terminus. J. Biol. Chem. 265:17876-17882.
    • (1990) J. Biol. Chem. , vol.265 , pp. 17876-17882
    • Kelley, C.A.1    Adelstein, R.S.2
  • 21
    • 0027258646 scopus 로고
    • An insert of seven amino acids confers functional differences between smooth muscle myosins from the intestines and vasculature
    • Kelley, C.A., M. Takahashi, J.H. Yu, and R.S. Adelstein. 1993. An insert of seven amino acids confers functional differences between smooth muscle myosins from the intestines and vasculature. J. Biol. Chem. 268:12848-12854.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12848-12854
    • Kelley, C.A.1    Takahashi, M.2    Yu, J.H.3    Adelstein, R.S.4
  • 23
    • 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 (Lond.). 227:680-685.
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: A physically integrated molecular process
    • Lauffenburger, D.A., and A.F. Horwitz. 1996. Cell migration: a physically integrated molecular process. Cell. 84:359-368.
    • (1996) Cell , vol.84 , pp. 359-368
    • Lauffenburger, D.A.1    Horwitz, A.F.2
  • 25
    • 0024362253 scopus 로고
    • Antigen-induced secretion of histamine and the phosphorylation of myosin by protein kinase C in rat basophilic leukemia cells
    • Ludowyke, R.I., I. Peleg, M.A. Beaven, and R.S. Adelstein. 1989. Antigen-induced secretion of histamine and the phosphorylation of myosin by protein kinase C in rat basophilic leukemia cells. J Biol Chem. 264:12492-12501.
    • (1989) J Biol Chem. , vol.264 , pp. 12492-12501
    • Ludowyke, R.I.1    Peleg, I.2    Beaven, M.A.3    Adelstein, R.S.4
  • 26
    • 0027999246 scopus 로고
    • Differential localization of myosin II isozymes in human cultured cells and blood cells
    • Maupin, P., C.L. Phillips, R.S. Adelstein, and T.D. Pollard. 1994. Differential localization of myosin II isozymes in human cultured cells and blood cells. J. Cell Sci. 107:3077-3090.
    • (1994) J. Cell Sci. , vol.107 , pp. 3077-3090
    • Maupin, P.1    Phillips, C.L.2    Adelstein, R.S.3    Pollard, T.D.4
  • 27
    • 0026557199 scopus 로고
    • Myosin II distribution in neurons is consistent with a role in growth cone motility but not synaptic vesicle mobilization
    • Miller, M., E. Bower, P. Levitt, D. Li, and P.D. Chantler. 1992. Myosin II distribution in neurons is consistent with a role in growth cone motility but not synaptic vesicle mobilization. Neuron. 8:25-44.
    • (1992) Neuron , vol.8 , pp. 25-44
    • Miller, M.1    Bower, E.2    Levitt, P.3    Li, D.4    Chantler, P.D.5
  • 28
    • 0030049170 scopus 로고    scopus 로고
    • Actin-based cell motility and cell locomotion
    • Mitchison, T.J., and L.P. Cramer. 1996. Actin-based cell motility and cell locomotion. Cell. 84:371-379.
    • (1996) Cell , vol.84 , pp. 371-379
    • Mitchison, T.J.1    Cramer, L.P.2
  • 29
    • 0026652360 scopus 로고
    • Immunohistochemical studies on the distribution of cellular myosin II isoforms in brain and aorta
    • Murakami, N., and M. Elzinga. 1992. Immunohistochemical studies on the distribution of cellular myosin II isoforms in brain and aorta. Cell Motil. Cytoskeleton. 22:281-295.
    • (1992) Cell Motil. Cytoskeleton , vol.22 , pp. 281-295
    • Murakami, N.1    Elzinga, M.2
  • 30
    • 0024436810 scopus 로고
    • Capping of surface receptors and concomitant cortical tension are generated by conventional myosin
    • Pasternak, C., J.A. Spudich, and E.L. Elson. 1989. Capping of surface receptors and concomitant cortical tension are generated by conventional myosin. Nature (Lond.). 341:549-551.
    • (1989) Nature (Lond.) , vol.341 , pp. 549-551
    • Pasternak, C.1    Spudich, J.A.2    Elson, E.L.3
  • 32
    • 0021685350 scopus 로고
    • Characterization of a developmentally regulated perinatal myosin heavy-chain gene expressed in skeletal muscle
    • Periasamy, M., D.F. Wieczorek, and B. Nadal-Ginard. 1984. Characterization of a developmentally regulated perinatal myosin heavy-chain gene expressed in skeletal muscle. J. Biol. Chem. 259:13573-13578.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13573-13578
    • Periasamy, M.1    Wieczorek, D.F.2    Nadal-Ginard, B.3
  • 33
    • 0015834603 scopus 로고
    • Acanthamoeba myosin. I. Isolation from Acanthamoeba castellanii of an enzyme similar to muscle myosin
    • Pollard, T.D., and E.D. Korn. 1973. Acanthamoeba myosin. I. Isolation from Acanthamoeba castellanii of an enzyme similar to muscle myosin. J. Biol. Chem. 248:4682-4690.
    • (1973) J. Biol. Chem. , vol.248 , pp. 4682-4690
    • Pollard, T.D.1    Korn, E.D.2
  • 35
    • 0029586312 scopus 로고
    • Localization of myosin IIA and B isoforms in cultured neurons
    • Rochlin, M.W., K. Itoh, R.S. Adelstein, and P.C. Bridgman. 1995. Localization of myosin IIA and B isoforms in cultured neurons. J. Cell Sci. 108: 3661-3670.
    • (1995) J. Cell Sci. , vol.108 , pp. 3661-3670
    • Rochlin, M.W.1    Itoh, K.2    Adelstein, R.S.3    Bridgman, P.C.4
  • 36
    • 0029561337 scopus 로고
    • Chimeric substitutions of the actin-binding loop activate dephosphorylated but not phosphorylated smooth muscle heavy meromyosin
    • Rovner, A.S., Y. Freyzon, and K.M. Trybus. 1995. Chimeric substitutions of the actin-binding loop activate dephosphorylated but not phosphorylated smooth muscle heavy meromyosin. J. Biol. Chem. 270:30260-30263.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30260-30263
    • Rovner, A.S.1    Freyzon, Y.2    Trybus, K.M.3
  • 37
    • 0025174075 scopus 로고
    • Human nonmuscle myosin heavy chain mRNA: Generation of diversity through alternative polyadenylation
    • Saez, C.G., J.C. Myers, T.B. Shows, and L.A. Leinwand. 1990. Human nonmuscle myosin heavy chain mRNA: generation of diversity through alternative polyadenylation. Proc. Natl. Acad. Sci. USA. 87 :1164-1168.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1164-1168
    • Saez, C.G.1    Myers, J.C.2    Shows, T.B.3    Leinwand, L.A.4
  • 38
    • 0024433443 scopus 로고
    • Analysis of cell division using fluorescently labeled actin and myosin in living PtK2 cells
    • Sanger, J.M., B. Mittal, J.S. Dome, and J.W. Sanger. 1989. Analysis of cell division using fluorescently labeled actin and myosin in living PtK2 cells. Cell Motil. Cytoskeleton. 14:201-219.
    • (1989) Cell Motil. Cytoskeleton , vol.14 , pp. 201-219
    • Sanger, J.M.1    Mittal, B.2    Dome, J.S.3    Sanger, J.W.4
  • 44
    • 0028075752 scopus 로고
    • How molecular motors work
    • Spudich, J.A. 1994. How molecular motors work. Nature (Lond.). 372:515-518.
    • (1994) Nature (Lond.) , vol.372 , pp. 515-518
    • Spudich, J.A.1
  • 45
    • 0026774648 scopus 로고
    • Evidence for inserted sequences on the head region of nonmuscle myosin specific to the nervous system
    • Takahashi, M., S. Kawamoto, and R.S. Adelstein. 1992. Evidence for inserted sequences on the head region of nonmuscle myosin specific to the nervous system. J. Biol. Chem. 267:17864-17871.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17864-17871
    • Takahashi, M.1    Kawamoto, S.2    Adelstein, R.S.3
  • 46
    • 0028354078 scopus 로고
    • Enzymatic activities correlate with chimaeric substitutions at the actin-binding face of myosin
    • Uyeda T.Q.P., K.M. Ruppel, and J.A Spudich. 1994. Enzymatic activities correlate with chimaeric substitutions at the actin-binding face of myosin. Nature (Lond.). 368:567-569.
    • (1994) Nature (Lond.) , vol.368 , pp. 567-569
    • Uyeda, T.Q.P.1    Ruppel, K.M.2    Spudich, J.A.3
  • 47
    • 0023484279 scopus 로고
    • Myosin structure and function in cell motility
    • Warrick, H.M., and J. A. Spudich. 1987. Myosin structure and function in cell motility. Annu. Rev. Cell Biol. 3:379-421.
    • (1987) Annu. Rev. Cell Biol. , vol.3 , pp. 379-421
    • Warrick, H.M.1    Spudich, J.A.2


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