메뉴 건너뛰기




Volumn 248, Issue 3, 1997, Pages 834-839

Characterization of gelsolin truncates that inhibit actin depolymerization by severing activity of gelsolin and cofilin

Author keywords

Cofilin; F actin; Gelsolin; Severing inhibitor

Indexed keywords

COFILIN; GELSOLIN; PROTEIN DERIVATIVE;

EID: 0030874557     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00834.x     Document Type: Article
Times cited : (15)

References (37)
  • 1
    • 0023424175 scopus 로고
    • Gelsolin: Calcium- and polyphosphoinositide-regulated actin-modulating protein
    • Yin, H. L. (1987) Gelsolin: calcium- and polyphosphoinositide-regulated actin-modulating protein, Bioessays 7, 176-179.
    • (1987) Bioessays , vol.7 , pp. 176-179
    • Yin, H.L.1
  • 2
    • 0028274104 scopus 로고
    • Phosphoinositides and calsium as regulators of cellular actin assembly and disassembly
    • Janmey, P. A. (1994) Phosphoinositides and calsium as regulators of cellular actin assembly and disassembly, Annu. Rev. Physiol. 56, 169-191.
    • (1994) Annu. Rev. Physiol. , vol.56 , pp. 169-191
    • Janmey, P.A.1
  • 3
    • 0025782925 scopus 로고
    • Enhanced motility in NIH 3T3 fibroblasts that overexpress gelsolin
    • Cunningham, C. C., Stossel, T. P. & Kwiatkowski, D. J. (1991) Enhanced motility in NIH 3T3 fibroblasts that overexpress gelsolin, Science 251, 1233-1236.
    • (1991) Science , vol.251 , pp. 1233-1236
    • Cunningham, C.C.1    Stossel, T.P.2    Kwiatkowski, D.J.3
  • 4
    • 0029787092 scopus 로고    scopus 로고
    • Dependence of fibroblast migration on actin severing activity of gelsolin
    • Arora, P. D. & McCulloch, C. A. G. (1996) Dependence of fibroblast migration on actin severing activity of gelsolin, J. Biol. Chem. 271, 20 516-20 523.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20516-20523
    • Arora, P.D.1    McCulloch, C.A.G.2
  • 5
    • 0028914814 scopus 로고
    • Hemostatic, inflammatory, and fibroblast responses are blunted in mice lacking gelsolin
    • Witke, W., Sharpe, A. H., Hartwig, J. H., Azuma, T., Stossel, T. P. & Kwiatkowski, D. J. (1995) Hemostatic, inflammatory, and fibroblast responses are blunted in mice lacking gelsolin, Cell 81, 41-51.
    • (1995) Cell , vol.81 , pp. 41-51
    • Witke, W.1    Sharpe, A.H.2    Hartwig, J.H.3    Azuma, T.4    Stossel, T.P.5    Kwiatkowski, D.J.6
  • 6
    • 0028773922 scopus 로고
    • The machinery of blood cell movements
    • Stossel, T. P. (1994) The machinery of blood cell movements, Blood 84, 367-379.
    • (1994) Blood , vol.84 , pp. 367-379
    • Stossel, T.P.1
  • 7
    • 0022381477 scopus 로고
    • Isolation and properties of two actin-binding domains in gelsolin
    • Kwiatkowski, D. J., Janmey, P. A., Mole, J. E. & Yin, H. L. (1985) Isolation and properties of two actin-binding domains in gelsolin, J. Biol. Chem. 260, 15232-15238.
    • (1985) J. Biol. Chem. , vol.260 , pp. 15232-15238
    • Kwiatkowski, D.J.1    Janmey, P.A.2    Mole, J.E.3    Yin, H.L.4
  • 8
    • 0023008203 scopus 로고
    • The actin-filament-severing domain of plasma gelsolin
    • Chaponnier, C., Janmey, P. A. & Yin, H. L. (1986) The actin-filament-severing domain of plasma gelsolin, J. Cell. Biol. 103, 1473-1481.
    • (1986) J. Cell. Biol. , vol.103 , pp. 1473-1481
    • Chaponnier, C.1    Janmey, P.A.2    Yin, H.L.3
  • 9
    • 0023894120 scopus 로고
    • Gelsolin has three actin-binding sites
    • Bryan, J. (1988) Gelsolin has three actin-binding sites, J. Cell. Biol. 106, 1553-1562.
    • (1988) J. Cell. Biol. , vol.106 , pp. 1553-1562
    • Bryan, J.1
  • 10
    • 0024566030 scopus 로고
    • Identification of critical functional and regulatory domains in gelsolin
    • Kwiatkowski, D. J., Janmey, P. A. & Yin, H. L. (1989) Identification of critical functional and regulatory domains in gelsolin, J. Cell. Biol. 108, 1717-1726.
    • (1989) J. Cell. Biol. , vol.108 , pp. 1717-1726
    • Kwiatkowski, D.J.1    Janmey, P.A.2    Yin, H.L.3
  • 11
    • 0024318706 scopus 로고
    • Expression of human plasma gelsolin in Escherichia coli and dissection of actin binding sites by segmental deletion mutagenesis
    • Way, M., Gooch, J., Pope, B. & Weeds, A. G. (1989) Expression of human plasma gelsolin in Escherichia coli and dissection of actin binding sites by segmental deletion mutagenesis, J. Cell. Biol. 109, 593-605.
    • (1989) J. Cell. Biol. , vol.109 , pp. 593-605
    • Way, M.1    Gooch, J.2    Pope, B.3    Weeds, A.G.4
  • 12
    • 0026495427 scopus 로고
    • Evidence for functional homology in the F-actin binding domains of gelsolin and alpha-actinin: Implications for the requirements of severing and capping
    • Way, M., Pope, B. & Weeds, A. G. (1992) Evidence for functional homology in the F-actin binding domains of gelsolin and alpha-actinin: implications for the requirements of severing and capping, J. Cell. Biol. 119, 835-842.
    • (1992) J. Cell. Biol. , vol.119 , pp. 835-842
    • Way, M.1    Pope, B.2    Weeds, A.G.3
  • 13
    • 0028235759 scopus 로고
    • The actin side-binding domain of gelsolin also caps actin filaments. Implications for actin filament severing
    • Sun, H. Q., Wooten, D. C., Janmey, P. A. & Yin, H. L. (1994) The actin side-binding domain of gelsolin also caps actin filaments. Implications for actin filament severing, J. Biol. Chem. 269, 9473-9479.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9473-9479
    • Sun, H.Q.1    Wooten, D.C.2    Janmey, P.A.3    Yin, H.L.4
  • 14
    • 0023849688 scopus 로고
    • Identification of a polyphosphoinositide-modulated domain in gelsolin which binds to the sides of actin filaments
    • Yin, H. L., Iida, K. & Janmey, P. A. (1988) Identification of a polyphosphoinositide-modulated domain in gelsolin which binds to the sides of actin filaments, J. Cell. Biol. 106, 805-812.
    • (1988) J. Cell. Biol. , vol.106 , pp. 805-812
    • Yin, H.L.1    Iida, K.2    Janmey, P.A.3
  • 15
    • 0028839660 scopus 로고
    • The ADF/cofilin proteins: Stimulus-responsive modulators of actin dynamics
    • Moon, A. & Drubin, D. G. (1995) The ADF/cofilin proteins: stimulus-responsive modulators of actin dynamics, Mol. Biol. Cell. 6, 1423-1431.
    • (1995) Mol. Biol. Cell. , vol.6 , pp. 1423-1431
    • Moon, A.1    Drubin, D.G.2
  • 16
    • 0030843484 scopus 로고    scopus 로고
    • Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: Implication in actin-based motility
    • Carlier, M. K. Laurent, V., Santolini, J., Melki, R., Didry, D., Xia, G. X., Hong, Y., Chua, N. H. & Pantaloni, D. (1997) Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility, J. Cell. Biol. 136, 1307-1322.
    • (1997) J. Cell. Biol. , vol.136 , pp. 1307-1322
    • Carlier, M.K.1    Laurent, V.2    Santolini, J.3    Melki, R.4    Didry, D.5    Xia, G.X.6    Hong, Y.7    Chua, N.H.8    Pantaloni, D.9
  • 17
    • 0022403777 scopus 로고
    • pH control of actin polymerization by cofilin
    • Yonezawa, N., Nishida, E. & Sakai, H. (1985) pH control of actin polymerization by cofilin. J. Biol. Chem. 260, 14410-14412.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14410-14412
    • Yonezawa, N.1    Nishida, E.2    Sakai, H.3
  • 18
    • 0030604703 scopus 로고    scopus 로고
    • Tertiary structure of destrin and structural similarity between two actin-regulating protein families
    • Hatanaka, H., Ogura, K., Moriyama, K., Ichikawa, S., Yahara, I. & Inagaki, F. (1996) Tertiary structure of destrin and structural similarity between two actin-regulating protein families, Cell 85, 1047-1055.
    • (1996) Cell , vol.85 , pp. 1047-1055
    • Hatanaka, H.1    Ogura, K.2    Moriyama, K.3    Ichikawa, S.4    Yahara, I.5    Inagaki, F.6
  • 19
    • 0023239517 scopus 로고
    • Functional inactivation of genes by dominant negative mutations
    • Herskowitz, I. (1987) Functional inactivation of genes by dominant negative mutations, Nature 329, 219-222.
    • (1987) Nature , vol.329 , pp. 219-222
    • Herskowitz, I.1
  • 20
    • 0027240628 scopus 로고
    • Tumor-suppressive function of mutated gelsolin in ras-transformed cells
    • Müllauer, L., Fujita, H., Ishizaki, A. & Kuzumaki, N. (1993) Tumor-suppressive function of mutated gelsolin in ras-transformed cells, Oncogene 8, 2531-2536.
    • (1993) Oncogene , vol.8 , pp. 2531-2536
    • Müllauer, L.1    Fujita, H.2    Ishizaki, A.3    Kuzumaki, N.4
  • 22
    • 0019427215 scopus 로고
    • Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin
    • Kouyama, T. & Mihashi, K. (1981) Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin, Eur. J. Biochem. 114, 33-38.
    • (1981) Eur. J. Biochem. , vol.114 , pp. 33-38
    • Kouyama, T.1    Mihashi, K.2
  • 23
    • 0028603483 scopus 로고
    • 2+ affect the rate at which gelsolin severs F-actin
    • 2+ affect the rate at which gelsolin severs F-actin. J. Biol. Chem. 269, 32916-32923.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32916-32923
    • Allen, P.G.1    Janmey, P.A.2
  • 24
    • 0029866597 scopus 로고    scopus 로고
    • Binding of phosphate, aluminum fluoride, or beryllium fluoride to F-actin inhibits severing by gelsolin
    • Allen, P. G., Laham, L. E., Way, M. & Janmey, P. A. (1996) Binding of phosphate, aluminum fluoride, or beryllium fluoride to F-actin inhibits severing by gelsolin, J. Biol. Chem. 271, 4665-4670.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4665-4670
    • Allen, P.G.1    Laham, L.E.2    Way, M.3    Janmey, P.A.4
  • 25
    • 0021801388 scopus 로고
    • Interactions of gelsolin and gelsolin-actin complexes with actin. Effects of calcium on actin nucleation, filament severing, and end blocking
    • Janmey, P. A., Chaponnier, C., Lind, S. E., Zaner, K. S., Stossel, T. P. & Yin, H. L. (1985) Interactions of gelsolin and gelsolin-actin complexes with actin. Effects of calcium on actin nucleation, filament severing, and end blocking, Biochemistry 24, 3714-3723.
    • (1985) Biochemistry , vol.24 , pp. 3714-3723
    • Janmey, P.A.1    Chaponnier, C.2    Lind, S.E.3    Zaner, K.S.4    Stossel, T.P.5    Yin, H.L.6
  • 26
    • 0020600552 scopus 로고
    • Isolation and some structural and functional properties of macrophage tropomyosin
    • Fattoum, A., Hartwig, J. H. & Stossel, T. P. (1983) Isolation and some structural and functional properties of macrophage tropomyosin, Biochemistry 22, 1187-1193.
    • (1983) Biochemistry , vol.22 , pp. 1187-1193
    • Fattoum, A.1    Hartwig, J.H.2    Stossel, T.P.3
  • 27
    • 0024565757 scopus 로고
    • Differential modulation of actin-severing activity of gelsolin by multiple isoforms of cultured rat cell tropomyosin. Potentiation of protective ability of tropomyosins by 83-kDa nonmuscle caldesmon
    • Ishikawa, R., Yamashiro, S. & Matsumura, F. (1989) Differential modulation of actin-severing activity of gelsolin by multiple isoforms of cultured rat cell tropomyosin. Potentiation of protective ability of tropomyosins by 83-kDa nonmuscle caldesmon. J. Biol. Chem. 264, 7490-7497.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7490-7497
    • Ishikawa, R.1    Yamashiro, S.2    Matsumura, F.3
  • 28
    • 0028246755 scopus 로고
    • Purification of tropomyosin from bovine adrenal medulla and its inhibitory effect on the actin severing activity of adseverin (adrenal medulla 74 kDa actin severing protein)
    • Maekawa, S. & Toriyama, M. (1994) Purification of tropomyosin from bovine adrenal medulla and its inhibitory effect on the actin severing activity of adseverin (adrenal medulla 74 kDa actin severing protein), Biochem. Mol. Biol. Int. 33, 661-668.
    • (1994) Biochem. Mol. Biol. Int. , vol.33 , pp. 661-668
    • Maekawa, S.1    Toriyama, M.2
  • 29
    • 0025982039 scopus 로고
    • The role of actin polymerization in cell motility
    • Cooper, J. A. (1991) The role of actin polymerization in cell motility, Annu. Rev. Physiol. 53, 585-605.
    • (1991) Annu. Rev. Physiol. , vol.53 , pp. 585-605
    • Cooper, J.A.1
  • 30
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: A physically integrated molecular process
    • Lauffenburger, D. A. & Horwitz, A. F. (1996) Cell migration: A physically integrated molecular process, Cell 84, 359-369.
    • (1996) Cell , vol.84 , pp. 359-369
    • Lauffenburger, D.A.1    Horwitz, A.F.2
  • 31
    • 0030049170 scopus 로고    scopus 로고
    • Actin-based cell motility and cell locomotion
    • Mitchison, T. J. & Cramer, L. P. (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
  • 32
    • 0024404994 scopus 로고
    • Microfilament-based motility in non-muscle cells
    • Small, J. V. (1989) Microfilament-based motility in non-muscle cells. Curr. Opin. Cell Biol. 1, 75-79.
    • (1989) Curr. Opin. Cell Biol. , vol.1 , pp. 75-79
    • Small, J.V.1
  • 33
    • 0027299745 scopus 로고
    • On the crawling of animal cells
    • Stossel, T. P. (1993) On the crawling of animal cells, Science 260, 1086-1094.
    • (1993) Science , vol.260 , pp. 1086-1094
    • Stossel, T.P.1
  • 34
    • 0025363536 scopus 로고
    • Cancer cell structure: Actin changes in tumour cells - Possible mechanisms for malignant tumour formation
    • Holme, T. C. (1990) Cancer cell structure: actin changes in tumour cells - possible mechanisms for malignant tumour formation, Eur. J. Surg. Oncol. 16, 161-169.
    • (1990) Eur. J. Surg. Oncol. , vol.16 , pp. 161-169
    • Holme, T.C.1
  • 35
    • 0026520267 scopus 로고
    • Role of the cytoskeleton in genome regulation and cancer
    • Puck, T. T. & Krystosek, A. (1992) Role of the cytoskeleton in genome regulation and cancer, Int. rev. Cytol. 132, 75-108.
    • (1992) Int. Rev. Cytol. , vol.132 , pp. 75-108
    • Puck, T.T.1    Krystosek, A.2
  • 36
    • 0025720781 scopus 로고
    • Actin cytoskeletal network in aging and cancer
    • Rao, K. M. & Cohen, H. J. (1991) Actin cytoskeletal network in aging and cancer, Mutat. Res. 256, 139-148.
    • (1991) Mutat. Res. , vol.256 , pp. 139-148
    • Rao, K.M.1    Cohen, H.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.