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Volumn 260, Issue 2, 1999, Pages 439-445

The effect of intact talin and talin tail fragment on actin filament dynamics and structure depends on pH and ionic strength

Author keywords

Actin filament cross linking; Focal adhesion complex; Talin; Tension

Indexed keywords

ACTIN; TALIN;

EID: 0033106139     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00177.x     Document Type: Article
Times cited : (15)

References (32)
  • 1
    • 0031850240 scopus 로고    scopus 로고
    • The cytoskeleton and cell signaling: Component localization and mechanical coupling
    • Janmey, P.A. (1998) The cytoskeleton and cell signaling: component localization and mechanical coupling. Physiol. Rev. 78, 763-781.
    • (1998) Physiol. Rev. , vol.78 , pp. 763-781
    • Janmey, P.A.1
  • 2
    • 0022534722 scopus 로고
    • Interaction of plasma membrane fibronectin receptor with talin - A transmembrane linkage
    • Horwitz, A., Duggan, K., Buck, C., Beckerle, M. & Burridge, K. (1986) Interaction of plasma membrane fibronectin receptor with talin - a transmembrane linkage. Nature 320, 531-533.
    • (1986) Nature , vol.320 , pp. 531-533
    • Horwitz, A.1    Duggan, K.2    Buck, C.3    Beckerle, M.4    Burridge, K.5
  • 3
    • 0021214312 scopus 로고
    • An interaction between vinculin and talin
    • Burridge, K. & 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
  • 5
    • 0026803329 scopus 로고
    • Probing actin and liposome interaction of talin and talin-vinculin complexes: A kinetic, thermodynamic and lipid labeling study
    • Goldmann, W.H., Niggli, V., Kaufmann, S. & Isenberg, G. (1992) Probing actin and liposome interaction of talin and talin-vinculin complexes: a kinetic, thermodynamic and lipid labeling study. Biochemistry 31, 7665-7671.
    • (1992) Biochemistry , vol.31 , pp. 7665-7671
    • Goldmann, W.H.1    Niggli, V.2    Kaufmann, S.3    Isenberg, G.4
  • 6
    • 0024990759 scopus 로고
    • Sequence and domain structure of talin
    • Rees, D.J.G., Ades, S.E., Singer, S.J. & Hynes, O. (1990) Sequence and domain structure of talin. Nature 347, 685-689.
    • (1990) Nature , vol.347 , pp. 685-689
    • Rees, D.J.G.1    Ades, S.E.2    Singer, S.J.3    Hynes, O.4
  • 7
    • 0028146835 scopus 로고
    • Identification of functional domains in the cytoskeletal protein talin
    • Niggli, V., Kaufmann, S., Goldmann, W.H., Weber, T. & Isenberg, G. (1994) Identification of functional domains in the cytoskeletal protein talin. Eur. J. Biochem. 224, 951-957.
    • (1994) Eur. J. Biochem. , vol.224 , pp. 951-957
    • Niggli, V.1    Kaufmann, S.2    Goldmann, W.H.3    Weber, T.4    Isenberg, G.5
  • 10
    • 0026700187 scopus 로고
    • Augmentation of alpha-actinin-induced gelation of actin by talin
    • Muguruma, M., Matsumura, S. & Fukazawa, T. (1992) Augmentation of alpha-actinin-induced gelation of actin by talin. J. Biol. Chem. 267, 5621-5624.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5621-5624
    • Muguruma, M.1    Matsumura, S.2    Fukazawa, T.3
  • 12
    • 0027376824 scopus 로고
    • The viscoelasticity of entangled actin networks: The influence of defects and modulation by talin and vinculin
    • Ruddies, R., Goldmann, W.H., Isenberg, G. & Sackmann, E. (1993) The viscoelasticity of entangled actin networks: the influence of defects and modulation by talin and vinculin. Eur. Biophys. J. 22, 309-321.
    • (1993) Eur. Biophys. J. , vol.22 , pp. 309-321
    • Ruddies, R.1    Goldmann, W.H.2    Isenberg, G.3    Sackmann, E.4
  • 13
    • 0031436950 scopus 로고    scopus 로고
    • Examining F-actin interaction with intact talin and talin head and tail fragment using static and dynamic light scattering
    • and (1998) 254, 207
    • Goldmann, W.H., Guttenberg, Z., Kaufmann, S., Hess, D., Ezzell, P.M. & Isenberg, G. (1997) Examining F-actin interaction with intact talin and talin head and tail fragment using static and dynamic light scattering. Eur. J. Biochem. 250, 447-450, and (1998) 254, 207.
    • (1997) Eur. J. Biochem. , vol.250 , pp. 447-450
    • Goldmann, W.H.1    Guttenberg, Z.2    Kaufmann, S.3    Hess, D.4    Ezzell, P.M.5    Isenberg, G.6
  • 14
    • 0031817205 scopus 로고    scopus 로고
    • Differences in elasticity of vinculin-deficient F9 cells measured by magnetometry and atomic force microscopy
    • Goldmann, W.H., Galneder, R., Ludwig, M., Xu, W., Adamson, E.D., Wang, N. & Ezzell, R.M. (1998) Differences in elasticity of vinculin-deficient F9 cells measured by magnetometry and atomic force microscopy. Exp. Cell Res. 239, 235-242.
    • (1998) Exp. Cell Res. , vol.239 , pp. 235-242
    • Goldmann, W.H.1    Galneder, R.2    Ludwig, M.3    Xu, W.4    Adamson, E.D.5    Wang, N.6    Ezzell, R.M.7
  • 15
    • 0031836593 scopus 로고    scopus 로고
    • Rescue of mutant phenotype by reexpression of full-Mength vinculin in null F9 cells: Effects on cell locomotion by domain deleted vinculin
    • Xu, W., Coll, J.L. & Adamson, E.D. (1998) Rescue of mutant phenotype by reexpression of full-Mength vinculin in null F9 cells: effects on cell locomotion by domain deleted vinculin. J. Cell Sci. 111, 1535-1544.
    • (1998) J. Cell Sci. , vol.111 , pp. 1535-1544
    • Xu, W.1    Coll, J.L.2    Adamson, E.D.3
  • 16
    • 0039728833 scopus 로고    scopus 로고
    • Talin-null cells of Dictyostelium are strongly defective in adhesion to particle and substrate surfaces and slightly impaired in cytokinesis
    • Niewöhner, J., Weber, I., Maniak, M., Müller-Taubenberger, A. & Gerisch, G. (1997) Talin-null cells of Dictyostelium are strongly defective in adhesion to particle and substrate surfaces and slightly impaired in cytokinesis. J. Cell Biol. 138, 349-361.
    • (1997) J. Cell Biol. , vol.138 , pp. 349-361
    • Niewöhner, J.1    Weber, I.2    Maniak, M.3    Müller-Taubenberger, A.4    Gerisch, G.5
  • 17
    • 0032563558 scopus 로고    scopus 로고
    • Disruption of the talin gene compromises focal adhesion assembly in undifferentiated but not differentiated embryonic stem cells
    • Priddle, H., Hemmings, L., Monkley, S., Woods, A., Patel, B., Sutton, D., Dunn, G.A., Zicha, D. & Critchley, D.R. (1998) Disruption of the talin gene compromises focal adhesion assembly in undifferentiated but not differentiated embryonic stem cells. J. Cell Biol. 142, 1121-1133.
    • (1998) J. Cell Biol. , vol.142 , pp. 1121-1133
    • Priddle, H.1    Hemmings, L.2    Monkley, S.3    Woods, A.4    Patel, B.5    Sutton, D.6    Dunn, G.A.7    Zicha, D.8    Critchley, D.R.9
  • 18
    • 0030899760 scopus 로고    scopus 로고
    • Tensegrity: The architectural basis of cellular mechanotransduction
    • Ingber, D.E. (1997) Tensegrity: The architectural basis of cellular mechanotransduction. Ann. Rev. Physiol. 59, 575-599.
    • (1997) Ann. Rev. Physiol. , vol.59 , pp. 575-599
    • Ingber, D.E.1
  • 19
    • 0020021878 scopus 로고
    • Purification of muscle actin
    • Pardee, J.D. & Spudich, J.A. (1982) Purification of muscle actin. Meth Enzymol. 85 (B), 164-181.
    • (1982) Meth Enzymol. , vol.85 , Issue.B , pp. 164-181
    • Pardee, J.D.1    Spudich, J.A.2
  • 20
    • 0019135186 scopus 로고
    • Identification of a factor in conventional muscle actin preparations which inhibits actin filament self-association
    • MacLean-Fletcher, S.D. & Pollard, T.D. (1980) Identification of a factor in conventional muscle actin preparations which inhibits actin filament self-association. Biochem. Biophys. Res. Commun. 96, 18-27.
    • (1980) Biochem. Biophys. Res. Commun. , vol.96 , pp. 18-27
    • MacLean-Fletcher, S.D.1    Pollard, T.D.2
  • 21
    • 0020490735 scopus 로고
    • Purification and properties of human platelets p235
    • Collier, N. & Wang, K. (1982) Purification and properties of human platelets p235. J. Biol. Chem. 257, 6937-6943.
    • (1982) J. Biol. Chem. , vol.257 , pp. 6937-6943
    • Collier, N.1    Wang, K.2
  • 23
    • 0026955828 scopus 로고
    • Quasi-elastic light scattering study of thermal excitations of F-actin solutions and of growth kinetics of actin filaments
    • Pieckenbrock, T.H. & Sackmann, E. (1992) Quasi-elastic light scattering study of thermal excitations of F-actin solutions and of growth kinetics of actin filaments. Biopolymers 32, 1471-1489.
    • (1992) Biopolymers , vol.32 , pp. 1471-1489
    • Pieckenbrock, T.H.1    Sackmann, E.2
  • 25
    • 0001660186 scopus 로고
    • Measurement of the persistence length of polymerized actin using fluorescence microscopy
    • Ott, A., Magnasco, M., Simon, A. & Libchaber, A. (1993) Measurement of the persistence length of polymerized actin using fluorescence microscopy. Phys. Rev. Lett. E48, R1642-R1645.
    • (1993) Phys. Rev. Lett. , vol.E48
    • Ott, A.1    Magnasco, M.2    Simon, A.3    Libchaber, A.4
  • 26
    • 4243085908 scopus 로고    scopus 로고
    • Dynamic light scattering from semidilute actin solutions: A study of hydrodynamic screening, filament bending stiffness, and the effect of tropomyosin/troponin binding
    • Götter, R., Kroy, K., Frey, E., Bärmann, M. & Sackmann, E. (1996) Dynamic light scattering from semidilute actin solutions: a study of hydrodynamic screening, filament bending stiffness, and the effect of tropomyosin/troponin binding. Macromolecules 29, 30-36.
    • (1996) Macromolecules , vol.29 , pp. 30-36
    • Götter, R.1    Kroy, K.2    Frey, E.3    Bärmann, M.4    Sackmann, E.5
  • 27
    • 0000411158 scopus 로고    scopus 로고
    • Dynamic scattering from solutions of semiflexible polymers
    • Kroy, K. & Frey, E. (1997) Dynamic scattering from solutions of semiflexible polymers. Phys. Rev. Lett., E55, 3092-3101.
    • (1997) Phys. Rev. Lett. , vol.E55 , pp. 3092-3101
    • Kroy, K.1    Frey, E.2
  • 28
    • 0030908297 scopus 로고    scopus 로고
    • The I/LWEQ module: A conserved sequence that signifies F-actin binding in functionally diverse proteins from yeast to mammals
    • McCann, R.O. & Craig, S.W. (1997) The I/LWEQ module: a conserved sequence that signifies F-actin binding in functionally diverse proteins from yeast to mammals. Proc Natl Acad. Sci. USA 94, 5679-5684.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5679-5684
    • McCann, R.O.1    Craig, S.W.2
  • 30
    • 0029062869 scopus 로고
    • Interaction of the 47-kDa talin fragment and the 32-kDa vinculin fragment with acidic phospholipids: A computer analysis
    • Tempel, M., Goldmann, W.H., Isenberg, G. & Sackmann, E. (1995) Interaction of the 47-kDa talin fragment and the 32-kDa vinculin fragment with acidic phospholipids: a computer analysis. Biophys. J. 69, 228-241.
    • (1995) Biophys. J. , vol.69 , pp. 228-241
    • Tempel, M.1    Goldmann, W.H.2    Isenberg, G.3    Sackmann, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.