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Volumn 116, Issue 2, 1996, Pages 270-277

The ultrastructure of chicken gizzard vinculin as visualized by high-resolution electron microscopy

Author keywords

[No Author keywords available]

Indexed keywords

VINCULIN;

EID: 0343058961     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.1996.0042     Document Type: Article
Times cited : (74)

References (37)
  • 1
    • 0025824367 scopus 로고
    • Vinculin is essential for muscle function in the nematode
    • Barstead, R. J., and Waterston, R. H. (1991) Vinculin is essential for muscle function in the nematode, J. Cell. Biol. 114, 715-724.
    • (1991) J. Cell. Biol. , vol.114 , pp. 715-724
    • Barstead, R.J.1    Waterston, R.H.2
  • 2
    • 4243392875 scopus 로고
    • Electron spectroscopic imaging: An advanced technique for imaging and analysis in transmission electron microscopy
    • Mayer, F., (Ed.), Academic Press, New York
    • Bauer, J. (1988) Electron spectroscopic imaging: An advanced technique for imaging and analysis in transmission electron microscopy, in Mayer, F., (Ed.), Methods in Microbiology: Electron Microscopy in Microbiology, Vol. 20, pp. 113-146, Academic Press, New York.
    • (1988) Methods in Microbiology: Electron Microscopy in Microbiology , vol.20 , pp. 113-146
    • Bauer, J.1
  • 3
    • 0024405255 scopus 로고
    • Structural model of vinculin: Correlation of amino acid sequence with electron-microscopical shape
    • Beck, K. (1989) Structural model of vinculin: correlation of amino acid sequence with electron-microscopical shape, FEBS Lett. 249, 1-4.
    • (1989) FEBS Lett. , vol.249 , pp. 1-4
    • Beck, K.1
  • 4
    • 0024348567 scopus 로고
    • Identification of two distinct functional domains on vinculin involved in its association with focal contacts
    • Bendori, R., Salomon, D., and Geiger, B. (1989) Identification of two distinct functional domains on vinculin involved in its association with focal contacts, J. Cell. Biol. 108, 2383-2393.
    • (1989) J. Cell. Biol. , vol.108 , pp. 2383-2393
    • Bendori, R.1    Salomon, D.2    Geiger, B.3
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0026033216 scopus 로고
    • 12 α-Hydroxysteroid dehydrogenase I from Clostridium group P, strain C 48-50: Production, purification and characterization
    • Braun, M., Lünsdorf, H., and Bückmann, A. J. (1991) 12 α-Hydroxysteroid dehydrogenase I from Clostridium group P, strain C 48-50: Production, purification and characterization, Eur. J. Biochem. 196, 439-450.
    • (1991) Eur. J. Biochem. , vol.196 , pp. 439-450
    • Braun, M.1    Lünsdorf, H.2    Bückmann, A.J.3
  • 7
    • 0021214312 scopus 로고
    • An interaction between vinculin and talin
    • Burridge, K., and Mangeat, P. (1984) An interaction between vinculin and talin, Nature 308, 744-746.
    • (1984) Nature , vol.308 , pp. 744-746
    • Burridge, K.1    Mangeat, P.2
  • 8
    • 0024205182 scopus 로고
    • cDNA-derived sequence of chicken embryo vinculin
    • Coutu, M. D., and Craig, S. W. (1988) cDNA-derived sequence of chicken embryo vinculin, Proc. Nat. Acad. Sci. USA 85, 8535-8539.
    • (1988) Proc. Nat. Acad. Sci. USA , vol.85 , pp. 8535-8539
    • Coutu, M.D.1    Craig, S.W.2
  • 9
    • 0027399847 scopus 로고
    • Molecular shape of vinculin in aqueous solution
    • Eimer, W., Niermann, M., Eppe, M. A., and Jockusch, B. M. (1993) Molecular shape of vinculin in aqueous solution, J. Mol. Biol. 229, 146-152.
    • (1993) J. Mol. Biol. , vol.229 , pp. 146-152
    • Eimer, W.1    Niermann, M.2    Eppe, M.A.3    Jockusch, B.M.4
  • 10
    • 0019320755 scopus 로고
    • A rapid purification of a-actinin, and a 130,000-dalton protein from smooth muscle
    • Feramisco, J. R., and Burridge, K. (1980) A rapid purification of a-actinin, and a 130,000-dalton protein from smooth muscle, J. Biol. Chem. 255, 1194-1199.
    • (1980) J. Biol. Chem. , vol.255 , pp. 1194-1199
    • Feramisco, J.R.1    Burridge, K.2
  • 11
    • 0028174102 scopus 로고
    • α-Actinin and vinculin are PIP2-binding proteins involved in signaling by tyrosine kinase
    • Fukami, K., Endo, T., Imamura, M., and Takenawa, T. (1994) α-Actinin and vinculin are PIP2-binding proteins involved in signaling by tyrosine kinase, J. Biol. Chem. 269, 1518-1522.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1518-1522
    • Fukami, K.1    Endo, T.2    Imamura, M.3    Takenawa, T.4
  • 12
    • 0018692430 scopus 로고
    • A 130 kDa protein from chicken gizzard: Its localization at the termini of microfilament bundles in cultured chicken cells
    • Geiger, B. (1979) A 130 kDa protein from chicken gizzard: Its localization at the termini of microfilament bundles in cultured chicken cells, Cell 18, 193-205.
    • (1979) Cell , vol.18 , pp. 193-205
    • Geiger, B.1
  • 14
    • 0023389031 scopus 로고
    • Metavinculin and vinculin from mammalian smooth muscle:Bulk isolation and characterization
    • Gimona, M., Fürst, D. O., and Small, J. V. (1987) Metavinculin and vinculin from mammalian smooth muscle:bulk isolation and characterization, J. Muscle Res. Cell Motil. 8, 329-341.
    • (1987) J. Muscle Res. Cell Motil. , vol.8 , pp. 329-341
    • Gimona, M.1    Fürst, D.O.2    Small, J.V.3
  • 15
    • 0028067413 scopus 로고
    • Native talin is a dumbbell-shaped homodimer when it interacts with actin
    • Goldmann, W. H., Bremer, A., Haner, M., Aebi, U., and Isenberg, G. (1994) Native talin is a dumbbell-shaped homodimer when it interacts with actin, J. Struct. Biol. 112, 3-10.
    • (1994) J. Struct. Biol. , vol.112 , pp. 3-10
    • Goldmann, W.H.1    Bremer, A.2    Haner, M.3    Aebi, U.4    Isenberg, G.5
  • 16
    • 0024278676 scopus 로고
    • Substructure and higher structure of chicken smooth muscle a-actinin molecule
    • Imamura, M., Endo, T., Kuroda, M., Tanaka, T., and Masaki, T. (1988) Substructure and higher structure of chicken smooth muscle a-actinin molecule, J. Biol. Chem. 263, 7800-7805.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7800-7805
    • Imamura, M.1    Endo, T.2    Kuroda, M.3    Tanaka, T.4    Masaki, T.5
  • 17
    • 0019973479 scopus 로고
    • Structural aspects of vinculin-actin interactions
    • Isenberg, G., Leonard, K., and Jockusch, B. M. (1982) Structural aspects of vinculin-actin interactions, J Mol. Biol. 158, 231-249.
    • (1982) J Mol. Biol. , vol.158 , pp. 231-249
    • Isenberg, G.1    Leonard, K.2    Jockusch, B.M.3
  • 19
    • 0028318397 scopus 로고
    • An intramolecular association between the head and tail domains of vinculin modulates talin binding
    • Johnson, R. P., and Craig, S. W. (1994) An intramolecular association between the head and tail domains of vinculin modulates talin binding, J. Biol. Chem. 269, 12611-12619.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12611-12619
    • Johnson, R.P.1    Craig, S.W.2
  • 20
    • 0028836195 scopus 로고
    • F-actin binding site masked by the intramolecular association of vinculin head and tail domains
    • Johnson, R. P., and Craig, S. W. (1995a) F-actin binding site masked by the intramolecular association of vinculin head and tail domains, Nature 373, 261-264.
    • (1995) Nature , vol.373 , pp. 261-264
    • Johnson, R.P.1    Craig, S.W.2
  • 21
    • 0029009673 scopus 로고
    • The carboxy-terminal tail domain of vinculin contains a cryptic binding site for acidic phospholipids
    • Johnson, R. P., and Craig, S. W. (1995b) The carboxy-terminal tail domain of vinculin contains a cryptic binding site for acidic phospholipids, Biochem. Biophys. Res. Commun. 210, 159-164.
    • (1995) Biochem. Biophys. Res. Commun. , vol.210 , pp. 159-164
    • Johnson, R.P.1    Craig, S.W.2
  • 22
    • 0027943345 scopus 로고
    • Intramolecular interactions in vinculin control α-actinin binding to the vinculin head
    • Kroemker, M., Rüdiger, A. H., Jockusch, B. M., and Rüdiger, M. (1994) Intramolecular interactions in vinculin control α-actinin binding to the vinculin head, FEBS Lett. 355, 259-262.
    • (1994) FEBS Lett. , vol.355 , pp. 259-262
    • Kroemker, M.1    Rüdiger, A.H.2    Jockusch, B.M.3    Rüdiger, M.4
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophages T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophages T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0022891198 scopus 로고
    • A rapid method for preparing perforated supporting foils for the thin carbon films used in high resolution transmission electron microscopy
    • Lünsdorf, H., and Spiess, E. (1986) A rapid method for preparing perforated supporting foils for the thin carbon films used in high resolution transmission electron microscopy, J. Microsc. 144, 211-213.
    • (1986) J. Microsc. , vol.144 , pp. 211-213
    • Lünsdorf, H.1    Spiess, E.2
  • 25
    • 0028358979 scopus 로고
    • Identification of the vinculin-binding site in the cytoskeletal protein α-actinin
    • McGregor, A., Blanchard, A. D., Rowe, A. J., and Critchley, D. R. (1994) Identification of the vinculin-binding site in the cytoskeletal protein α-actinin, J. Biochem. 301, 225-233.
    • (1994) J. Biochem. , vol.301 , pp. 225-233
    • McGregor, A.1    Blanchard, A.D.2    Rowe, A.J.3    Critchley, D.R.4
  • 26
    • 0027956825 scopus 로고
    • Characterization of an F-actinbinding domain in the cytoskeletal protein vinculin
    • Menkel, A. R., Kroemker, M., Bubeck, P., Ronsiek, M., Nikolai, G., and Jockusch, B. M. (1994) Characterization of an F-actinbinding domain in the cytoskeletal protein vinculin, J. Cell Biol. 126, 1231-1240.
    • (1994) J. Cell Biol. , vol.126 , pp. 1231-1240
    • Menkel, A.R.1    Kroemker, M.2    Bubeck, P.3    Ronsiek, M.4    Nikolai, G.5    Jockusch, B.M.6
  • 27
    • 0022419401 scopus 로고
    • Electron microscopy of rotary shadowed vinculin and vinculin complexes
    • Milam, L. M. (1985) Electron microscopy of rotary shadowed vinculin and vinculin complexes, J. Mol. Biol. 184, 543-545.
    • (1985) J. Mol. Biol. , vol.184 , pp. 543-545
    • Milam, L.M.1
  • 28
    • 0022004694 scopus 로고
    • Molecular shape and self-association of vinculin and metavinculin
    • Molony, L., and Burridge, K. (1985) Molecular shape and self-association of vinculin and metavinculin, J. Cell. Biochem. 29, 31-36.
    • (1985) J. Cell. Biochem. , vol.29 , pp. 31-36
    • Molony, L.1    Burridge, K.2
  • 29
    • 0020506943 scopus 로고
    • 125 I-vinculin gel overlay technique
    • 125 I-vinculin gel overlay technique, J. Cell Biol. 97, 1283-1287.
    • (1983) J. Cell Biol. , vol.97 , pp. 1283-1287
    • Otto, J.J.1
  • 33
    • 0027311930 scopus 로고
    • Expression of chicken vinculin complements the adhesion-defective phenotype of a mutant mouse F9 embryonal carcinoma cell
    • Samuels, M., Ezzell, R. M., Cardozo, T. J., Critchley, D. R., Coll, J.-L., and Adamson, E. D. (1993) Expression of chicken vinculin complements the adhesion-defective phenotype of a mutant mouse F9 embryonal carcinoma cell, J. Cell Biol. 121, 909-921.
    • (1993) J. Cell Biol. , vol.121 , pp. 909-921
    • Samuels, M.1    Ezzell, R.M.2    Cardozo, T.J.3    Critchley, D.R.4    Coll, J.-L.5    Adamson, E.D.6
  • 34
    • 0025008074 scopus 로고
    • Paxillin: A new vinculin-binding protein present in focal contacts
    • Turner, C. E., Glenney, Jr., J. R., and Burridge, K. (1990) Paxillin: A new vinculin-binding protein present in focal contacts, J. Cell Biol. 111, 1059-1068.
    • (1990) J. Cell Biol. , vol.111 , pp. 1059-1068
    • Turner, C.E.1    Glenney J.R., Jr.2    Burridge, K.3
  • 35
    • 0014301425 scopus 로고
    • Regulation of glutamine synthetase. XII. Electron microscopy of the enzyme from Escherichia coli
    • Valentine, R. C., Shapiro, B. M., and Stadtman, E. R. (1968) Regulation of glutamine synthetase. XII. Electron microscopy of the enzyme from Escherichia coli., Biochemistry 7, 2143-2152.
    • (1968) Biochemistry , vol.7 , pp. 2143-2152
    • Valentine, R.C.1    Shapiro, B.M.2    Stadtman, E.R.3
  • 37
    • 0028324634 scopus 로고
    • Characterisation of the paxillin-binding site and the c-terminal focal adhesion targeting sequence in vinculin
    • Wood, C. K., Turner, C. E., Jackson, P., and Critchley, D. R. (1994) Characterisation of the paxillin-binding site and the c-terminal focal adhesion targeting sequence in vinculin, J. Cell Sci. 107, 709-717.
    • (1994) J. Cell Sci. , vol.107 , pp. 709-717
    • Wood, C.K.1    Turner, C.E.2    Jackson, P.3    Critchley, D.R.4


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