메뉴 건너뛰기




Volumn 250, Issue 2, 1997, Pages 447-450

Examining F-actin interaction with intact talin and talin head and tail fragment using static and dynamic light scattering

Author keywords

Actin; Dynamic light scattering; Stopped flow kinetics; Talin

Indexed keywords

ACTIN; F ACTIN; TALIN;

EID: 0031436950     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.0447a.x     Document Type: Article
Times cited : (14)

References (28)
  • 1
    • 0000295888 scopus 로고    scopus 로고
    • New concepts for signal perception and transduction by the actin cytoskeleton at cell boundaries
    • Isenberg, G. (1996) New concepts for signal perception and transduction by the actin cytoskeleton at cell boundaries, Sem. Cell Dev. Biol. 7, 707-715.
    • (1996) Sem. Cell Dev. Biol. , vol.7 , pp. 707-715
    • Isenberg, G.1
  • 2
    • 0020506943 scopus 로고
    • 125I-vinculin gel overlay technique
    • 125I-vinculin gel overlay technique, J. Cell Biol. 97, 1283-1287.
    • (1983) J. Cell Biol. , vol.97 , pp. 1283-1287
    • Otto, J.J.1
  • 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
  • 4
    • 0025313592 scopus 로고
    • Functional studies of the domains of talin
    • Nuckolls, G. H., Turner, C. E. & Burridge, K. (1990) Functional studies of the domains of talin, J. Cell Biol. 110, 1635-1644.
    • (1990) J. Cell Biol. , vol.110 , pp. 1635-1644
    • Nuckolls, G.H.1    Turner, C.E.2    Burridge, K.3
  • 5
    • 0026700187 scopus 로고
    • Augmentation of α-actinin-induced gelation of actin by talin
    • Muguruma, M., Matsumura, S. & Fukuzawa, T. (1992) Augmentation of α-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    Fukuzawa, T.3
  • 11
    • 0026803329 scopus 로고
    • Probing actin and liposome interaction of falin 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 falin 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
  • 12
    • 0026483847 scopus 로고
    • Talin anchors and nucleates actin filaments at lipid membranes: A direct demonstration
    • Kaufmann, S., Kaes, J., Goldmann, W. H., Sackmann, E. & Isenberg, G. (1992) Talin anchors and nucleates actin filaments at lipid membranes: a direct demonstration, FEBS Lett. 314, 203-205.
    • (1992) FEBS Lett. , vol.314 , pp. 203-205
    • Kaufmann, S.1    Kaes, J.2    Goldmann, W.H.3    Sackmann, E.4    Isenberg, G.5
  • 13
    • 0028146835 scopus 로고
    • Identification of functional domains in the cytoskeletal protein talin
    • Niggli, V., Kaufmann, S., Goldmann, W. H., Weber, T. & Isenherg, 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    Isenherg, G.5
  • 14
    • 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., Isenherg, 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    Isenherg, G.3    Sackmann, E.4
  • 15
    • 0024990759 scopus 로고
    • Sequence and domain structure of talin
    • Rees, D. J. G., Ades, S. E., Singer, S. J. & Hynes, R. 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, R.O.4
  • 16
    • 0028067413 scopus 로고
    • Native talin is a dumbbell-shaped homodimer when it interacts with actin
    • Goldmann, W. H., Bremer, A., Haener, M., Aebi, U. & 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    Haener, M.3    Aebi, U.4    Isenberg, G.5
  • 17
    • 0031033956 scopus 로고    scopus 로고
    • Energy-filtered electron microscopy reveals that talin is a highly flexible protein composed of a series of globular domains
    • Winkler, J., Luensdorf, H. & Jockusch, B. M. (1997) Energy-filtered electron microscopy reveals that talin is a highly flexible protein composed of a series of globular domains, Eur. J. Biochem. 243, 430-436.
    • (1997) Eur. J. Biochem. , vol.243 , pp. 430-436
    • Winkler, J.1    Luensdorf, H.2    Jockusch, B.M.3
  • 19
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. 1. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich, J. A. & Watt, S. (1971) The regulation of rabbit skeletal muscle contraction. 1. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin, J. Biol. Chem. 246, 4866-4871.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 20
    • 0020266005 scopus 로고
    • 1 protein which restricts the length of actin filaments
    • 1 protein which restricts the length of actin filaments, FEBS Lett. 143, 205-210.
    • (1982) FEBS Lett. , vol.143 , pp. 205-210
    • Collier, N.C.1    Wang, K.2
  • 21
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation 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
  • 22
    • 0029050645 scopus 로고
    • Organization of the functional domains in membrane cytoskeletal prolein talin
    • Muguruma, M., Nishimuta, S., Tomisaka, Y., Ito, T. & Matsumura, S. (1995) Organization of the functional domains in membrane cytoskeletal prolein talin, J. Biochem. (Tokyo) 117, 1036-1042.
    • (1995) J. Biochem. (Tokyo) , vol.117 , pp. 1036-1042
    • Muguruma, M.1    Nishimuta, S.2    Tomisaka, Y.3    Ito, T.4    Matsumura, S.5
  • 23
    • 4243085908 scopus 로고
    • Dynamic light scattering from semidilute actin solutions: A study of hydrodynamic screening, filament bending stiffness, and the effect of tropomyosin/troponin-binding
    • Goetter, R., Kroy, K., Frey, E., Baermann, M. & Sackmann, E. (1995) 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.
    • (1995) Macromolecules , vol.29 , pp. 30-36
    • Goetter, R.1    Kroy, K.2    Frey, E.3    Baermann, M.4    Sackmann, E.5
  • 24
    • 0030908297 scopus 로고    scopus 로고
    • The 1/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 1/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
  • 25
    • 0027376824 scopus 로고
    • The viscoelasticity of entangled networks, the influence of defects and the modulation by talin and vinculin
    • Ruddies, R., Goldmann, W. H., Isenberg, G. & Sackmann, E. (1993) The viscoelasticity of entangled networks, the influence of defects and the 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
  • 26
    • 0028274229 scopus 로고
    • Talin decreases the bending elasticity of actin filaments
    • Goldmann, W. H., Kaes, J. & Isenberg, G. (1993) Talin decreases the bending elasticity of actin filaments, Biocheim. Soc. Trans. 22, 46S.
    • (1993) Biocheim. Soc. Trans. , vol.22
    • Goldmann, W.H.1    Kaes, J.2    Isenberg, G.3
  • 27
    • 15144338521 scopus 로고    scopus 로고
    • Differences in viscoleasticity of vinculin-deficient F9 cells measured by magnetometry and atomic force microscopy
    • Galneder, R., Ludwig, M., Goldmann, W. H., Wang, N., Gaub, H. E. & Ezzell, R. M. (1996) Differences in viscoleasticity of vinculin-deficient F9 cells measured by magnetometry and atomic force microscopy, Mol. Biol. Cell 7, 385a.
    • (1996) Mol. Biol. Cell , vol.7
    • Galneder, R.1    Ludwig, M.2    Goldmann, W.H.3    Wang, N.4    Gaub, H.E.5    Ezzell, R.M.6
  • 28
    • 0000411158 scopus 로고    scopus 로고
    • Dynamic scattering from solutions of semiflexible polymers
    • Kvoy, K. & Frey, F. (1997) Dynamic scattering from solutions of semiflexible polymers, Physical Review E 55, 3092-3101.
    • (1997) Physical Review E , vol.55 , pp. 3092-3101
    • Kvoy, K.1    Frey, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.