메뉴 건너뛰기




Volumn 250, Issue 1, 1999, Pages 142-154

Characterization of NF-L and βIIΣ1-spectrin interaction in live cells

Author keywords

Actin; Cytoskeleton; Intermediate filaments; Protein protein interaction; Spectrin

Indexed keywords

ACTIN; F ACTIN; FODRIN; SPECTRIN;

EID: 0033542735     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.1999.4479     Document Type: Article
Times cited : (15)

References (49)
  • 1
    • 0023951297 scopus 로고
    • Molecular and cellular biology of intermediate filaments
    • Steinert P. M., Roop D. R. Molecular and cellular biology of intermediate filaments. Annu. Rev. Biochem. 57:1988;593-625.
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 593-625
    • Steinert, P.M.1    Roop, D.R.2
  • 2
    • 0026334107 scopus 로고
    • Cellular and molecular biology of neuronal intermediate filaments
    • Fliegner K. H., Liem R. K. H. Cellular and molecular biology of neuronal intermediate filaments. Int. Rev. Cytol. 131:1991;109-167.
    • (1991) Int. Rev. Cytol. , vol.131 , pp. 109-167
    • Fliegner, K.H.1    Liem, R.K.H.2
  • 3
    • 0000994037 scopus 로고
    • Neurofilament proteins
    • R. D. Burgoyne. New York: A. R. Liss
    • Shaw G. Neurofilament proteins. Burgoyne R. D. The Neuronal Cytoskeleton. 1991;185-214 A. R. Liss, New York.
    • (1991) The Neuronal Cytoskeleton , pp. 185-214
    • Shaw, G.1
  • 4
    • 0019888431 scopus 로고
    • In vitro self-assembly of the 68,000 molecular weight component of the mammalian neurofilament triplet proteins into intermediate-size filaments
    • Geisler N., Weber K. In vitro self-assembly of the 68,000 molecular weight component of the mammalian neurofilament triplet proteins into intermediate-size filaments. J. Mol. Biol. 151:1981;565-571.
    • (1981) J. Mol. Biol. , vol.151 , pp. 565-571
    • Geisler, N.1    Weber, K.2
  • 5
    • 0020488844 scopus 로고
    • Purification of individual components of the neurofilament triplet: Filament assembly from the 70 000 dalton subunit
    • Liem R. K. H., Hutchison S. B. Purification of individual components of the neurofilament triplet: Filament assembly from the 70 000 dalton subunit. Biochemistry. 21:1982;3221-3226.
    • (1982) Biochemistry , vol.21 , pp. 3221-3226
    • Liem, R.K.H.1    Hutchison, S.B.2
  • 6
    • 0021359297 scopus 로고
    • Formation of 10 nm filaments from the 150-k-dalton neurofilament protein in vitro
    • Gardner E. E., Dahal D., Bignami A. Formation of 10 nm filaments from the 150-k-dalton neurofilament protein in vitro. J. Neurosci. Res. 11:1984;145-155.
    • (1984) J. Neurosci. Res. , vol.11 , pp. 145-155
    • Gardner, E.E.1    Dahal, D.2    Bignami, A.3
  • 7
    • 0027220073 scopus 로고
    • Assembly of type IV neuronal intermediate filaments in nonneural cells in the absence of preexisting cytoplasmic intermediate filaments
    • Ching G. Y., Liem R. K. H. Assembly of type IV neuronal intermediate filaments in nonneural cells in the absence of preexisting cytoplasmic intermediate filaments. J. Cell Biol. 122:1993;1323-1335.
    • (1993) J. Cell Biol. , vol.122 , pp. 1323-1335
    • Ching, G.Y.1    Liem, R.K.H.2
  • 8
    • 0027293898 scopus 로고
    • Neurofilaments are obligate heteropolymers in vivo
    • Lee M. K., Xu Z., Wong P. C., Cleveland D. W. Neurofilaments are obligate heteropolymers in vivo. J. Cell Biol. 122:1993;1336-1350.
    • (1993) J. Cell Biol. , vol.122 , pp. 1336-1350
    • Lee, M.K.1    Xu, Z.2    Wong, P.C.3    Cleveland, D.W.4
  • 9
    • 0024787034 scopus 로고
    • Expression of rat neurofilament proteins NF-L and NF-M in transfected non-neuronal cells
    • Chin S. S. M., Liem R. K. H. Expression of rat neurofilament proteins NF-L and NF-M in transfected non-neuronal cells. Eur. J. Cell Biol. 50:1989;475-490.
    • (1989) Eur. J. Cell Biol. , vol.50 , pp. 475-490
    • Chin, S.S.M.1    Liem, R.K.H.2
  • 10
    • 0025514319 scopus 로고
    • Transfected rat high-molecular-weight neurofilament NF-H coassembles with vimentin in a predominantly nonphosphorylated form
    • Chin S. S. M., Liem R. K. H. Transfected rat high-molecular-weight neurofilament NF-H coassembles with vimentin in a predominantly nonphosphorylated form. J. Neurosci. 10:1990;3714-3726.
    • (1990) J. Neurosci. , vol.10 , pp. 3714-3726
    • Chin, S.S.M.1    Liem, R.K.H.2
  • 11
    • 0024578553 scopus 로고
    • Expression of NF-L and NF-M in fibroblasts reveals coassembly of neurofilaments and vimentin subunits
    • Monteiro M. J., Cleveland D. W. Expression of NF-L and NF-M in fibroblasts reveals coassembly of neurofilaments and vimentin subunits. J. Cell Biol. 108:1989;579-593.
    • (1989) J. Cell Biol. , vol.108 , pp. 579-593
    • Monteiro, M.J.1    Cleveland, D.W.2
  • 12
    • 0025828675 scopus 로고
    • Effects of truncated neurofilament proteins on the endogenous intermediate filaments in transfected fibroblasts
    • Chin S. S. M., Macioce P., Liem R. K. H. Effects of truncated neurofilament proteins on the endogenous intermediate filaments in transfected fibroblasts. J. Cell Sci. 99:1991;335-350.
    • (1991) J. Cell Sci. , vol.99 , pp. 335-350
    • Chin, S.S.M.1    Macioce, P.2    Liem, R.K.H.3
  • 13
    • 0025107358 scopus 로고
    • Assembly properties of dominant and recessive mutations in the small mouse neurofilament (NF-L) subunit
    • Gill S. R., Wong P. C., Monteiro M. J., Cleveland D. W. Assembly properties of dominant and recessive mutations in the small mouse neurofilament (NF-L) subunit. J. Cell Biol. 111:1990;2005-2020.
    • (1990) J. Cell Biol. , vol.111 , pp. 2005-2020
    • Gill, S.R.1    Wong, P.C.2    Monteiro, M.J.3    Cleveland, D.W.4
  • 14
    • 0025013886 scopus 로고
    • Characterization of dominant and recessive assembly defective mutations in mouse neurofilament NF-M
    • Wong P. C., Cleveland D. W. Characterization of dominant and recessive assembly defective mutations in mouse neurofilament NF-M. J. Cell Biol. 90:1990;1987-2003.
    • (1990) J. Cell Biol. , vol.90 , pp. 1987-2003
    • Wong, P.C.1    Cleveland, D.W.2
  • 15
    • 0027530064 scopus 로고
    • Neurofilament deficiency in quail caused by nonsense mutation in neurofilament-L gene
    • Ohara O., Gahara Y., Miyake T., Teraoka H., Kitamura T. Neurofilament deficiency in quail caused by nonsense mutation in neurofilament-L gene. J. Cell Biol. 121:1993;387-395.
    • (1993) J. Cell Biol. , vol.121 , pp. 387-395
    • Ohara, O.1    Gahara, Y.2    Miyake, T.3    Teraoka, H.4    Kitamura, T.5
  • 16
    • 0028261670 scopus 로고
    • Neurofilament-deficient axons and perikaryal aggregates in viable transgenic mice expressing a neurofilament-β-galactosidase fusion protein
    • Eyer J., Peterson A. Neurofilament-deficient axons and perikaryal aggregates in viable transgenic mice expressing a neurofilament-β-galactosidase fusion protein. Neuron. 12:1994;389-405.
    • (1994) Neuron , vol.12 , pp. 389-405
    • Eyer, J.1    Peterson, A.2
  • 18
    • 0027333413 scopus 로고
    • The spectrin-based membrane skeleton and micron-scale organization of the plasma membrane
    • Bennett V. B., Gilligan D. M. The spectrin-based membrane skeleton and micron-scale organization of the plasma membrane. Annu. Rev. Cell Biol. 9:1993;27-66.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 27-66
    • Bennett, V.B.1    Gilligan, D.M.2
  • 19
    • 0027301038 scopus 로고
    • Erythroid and nonerythroid spectrins
    • Winkelmann J. C., Forget B. G. Erythroid and nonerythroid spectrins. Blood. 81:1993;3173-3185.
    • (1993) Blood , vol.81 , pp. 3173-3185
    • Winkelmann, J.C.1    Forget, B.G.2
  • 20
    • 0021187624 scopus 로고
    • Immunoprecipitation of nonerythrocyte spectrin within live cells following microinjection of specific antibodies: Relation to cytoskeletal structures
    • Mangeat P. H., Burridge K. Immunoprecipitation of nonerythrocyte spectrin within live cells following microinjection of specific antibodies: relation to cytoskeletal structures. J. Cell Biol. 98:1984;1363-1377.
    • (1984) J. Cell Biol. , vol.98 , pp. 1363-1377
    • Mangeat, P.H.1    Burridge, K.2
  • 21
    • 0023127448 scopus 로고
    • Cytoskeletal polarity in mammalian lymphocytes in situ
    • Lee J. K., Repasky E. A. Cytoskeletal polarity in mammalian lymphocytes in situ. Cell Tissue Res. 247:1987;195-202.
    • (1987) Cell Tissue Res. , vol.247 , pp. 195-202
    • Lee, J.K.1    Repasky, E.A.2
  • 22
    • 0023497802 scopus 로고
    • Cell type-specific association between two types of spectrin and two types of intermediate filaments
    • Langley R. C., Cohen C. M. Cell type-specific association between two types of spectrin and two types of intermediate filaments. Cell Motil. Cytoskel. 8:1987;165-173.
    • (1987) Cell Motil. Cytoskel. , vol.8 , pp. 165-173
    • Langley, R.C.1    Cohen, C.M.2
  • 23
    • 0023657022 scopus 로고
    • Binding of brain spectrin to the 70-kDa neurofilament subunit protein
    • Frappier T., Regnouf F., Pradel L. A. Binding of brain spectrin to the 70-kDa neurofilament subunit protein. Eur. J. Biochem. 169:1987;651-657.
    • (1987) Eur. J. Biochem. , vol.169 , pp. 651-657
    • Frappier, T.1    Regnouf, F.2    Pradel, L.A.3
  • 24
    • 0025754337 scopus 로고
    • Interaction domains of neurofilament light chain and brain spectrin
    • Frappier T., Stetzkowski-Marden F., Pradel L.-A. Interaction domains of neurofilament light chain and brain spectrin. Biochem. J. 275:1991;521-527.
    • (1991) Biochem. J. , vol.275 , pp. 521-527
    • Frappier, T.1    Stetzkowski-Marden, F.2    Pradel, L.-A.3
  • 25
    • 0026524937 scopus 로고
    • Actin and neurofilament binding domain of brain spectrin β subunit
    • Frappier T., Derancourt J., Pradel L.-A. Actin and neurofilament binding domain of brain spectrin β subunit. Eur. J. Biochem. 205:1992;85-91.
    • (1992) Eur. J. Biochem. , vol.205 , pp. 85-91
    • Frappier, T.1    Derancourt, J.2    Pradel, L.-A.3
  • 26
    • 0027397194 scopus 로고
    • Reorganization of brain spectrin (fodrin) during differentiation of PC12 cells
    • Takemura R., Okabe S., Kobayashi N., Hirokawa N. Reorganization of brain spectrin (fodrin) during differentiation of PC12 cells. Neuroscience. 52:1993;381-391.
    • (1993) Neuroscience , vol.52 , pp. 381-391
    • Takemura, R.1    Okabe, S.2    Kobayashi, N.3    Hirokawa, N.4
  • 27
    • 0025339874 scopus 로고
    • Regulated expression of vimentin cDNA in cells in the presence and absence of a preexisting vimentin filament network
    • Sarria A. J., Nordeen S. K., Evans R. M. Regulated expression of vimentin cDNA in cells in the presence and absence of a preexisting vimentin filament network. J. Cell Biol. 111:1990;553-565.
    • (1990) J. Cell Biol. , vol.111 , pp. 553-565
    • Sarria, A.J.1    Nordeen, S.K.2    Evans, R.M.3
  • 28
    • 0018763470 scopus 로고
    • Regulation of simian virus 40 transcription: Sensitive analysis of the RNA species present early in infections by virus or viral DNA
    • Parker G. A., Stark G. R. Regulation of simian virus 40 transcription: Sensitive analysis of the RNA species present early in infections by virus or viral DNA. Virology. 31:1979;360-369.
    • (1979) Virology , vol.31 , pp. 360-369
    • Parker, G.A.1    Stark, G.R.2
  • 29
    • 0015847039 scopus 로고
    • A new technique for the assay of infectivity of human adenovirus 5 DNA
    • Graham F. L., van der Eb A. J. A new technique for the assay of infectivity of human adenovirus 5 DNA. Virology. 52:1973;456-467.
    • (1973) Virology , vol.52 , pp. 456-467
    • Graham, F.L.1    Van Der Eb, A.J.2
  • 31
    • 0025995618 scopus 로고
    • Ankyrin binds to the 15th repetitive unit of erythroid and non-erythroid β-spectrin
    • Kennedy S. P., Warren S. L., Forget B. G., Morrow J. S. Ankyrin binds to the 15th repetitive unit of erythroid and non-erythroid β-spectrin. J. Cell Biol. 115:1991;267-277.
    • (1991) J. Cell Biol. , vol.115 , pp. 267-277
    • Kennedy, S.P.1    Warren, S.L.2    Forget, B.G.3    Morrow, J.S.4
  • 32
    • 0026030612 scopus 로고
    • Neuronal fodrin proteolysis occurs independently of excitatory amino acid-induced neurotoxicity
    • Di Stasi A. M. M., Gallo V., Ceccarini M., Petrucci T. C. Neuronal fodrin proteolysis occurs independently of excitatory amino acid-induced neurotoxicity. Neuron. 6:1991;445-454.
    • (1991) Neuron , vol.6 , pp. 445-454
    • Di Stasi, A.M.M.1    Gallo, V.2    Ceccarini, M.3    Petrucci, T.C.4
  • 33
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrilamide gels to nitrocellulose sheets: Procedures and some applications
    • Towbin M., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrilamide gels to nitrocellulose sheets: Procedures and some applications. Proc. Natl. Acad. Sci. USA. 76:1979;4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, M.1    Staehelin, T.2    Gordon, J.3
  • 34
    • 0027525225 scopus 로고
    • The 270 kDa splice variant of erythrocyte β-spectrin (β1Σ2) segregates in vivo and in vitro to specific domains of cerebellar neurons
    • Malchiodi-Albedi F., Ceccarini M., Winkelmann J. C., Morrow J. S., Petrucci T. C. The 270 kDa splice variant of erythrocyte β-spectrin (β1Σ2) segregates in vivo and in vitro to specific domains of cerebellar neurons. J. Cell Sci. 106:1993;67-78.
    • (1993) J. Cell Sci. , vol.106 , pp. 67-78
    • Malchiodi-Albedi, F.1    Ceccarini, M.2    Winkelmann, J.C.3    Morrow, J.S.4    Petrucci, T.C.5
  • 35
    • 0030598838 scopus 로고    scopus 로고
    • An essential cytoskeletal linker protein connecting actin microfilaments to intermediate filaments
    • Yang Y., Dowling J., Yu Q.-C., Kouklis P., Cleveland D. W., Fuchs E. An essential cytoskeletal linker protein connecting actin microfilaments to intermediate filaments. Cell. 86:1996;655-665.
    • (1996) Cell , vol.86 , pp. 655-665
    • Yang, Y.1    Dowling, J.2    Yu, Q.-C.3    Kouklis, P.4    Cleveland, D.W.5    Fuchs, E.6
  • 36
    • 0018700703 scopus 로고
    • Fluorographic detection of radioactivity in polyacrylamide gels with the water-soluble fluor, sodium salicylate
    • Chamberlain J. P. Fluorographic detection of radioactivity in polyacrylamide gels with the water-soluble fluor, sodium salicylate. Anal. Biochem. 98:1979;132-135.
    • (1979) Anal. Biochem. , vol.98 , pp. 132-135
    • Chamberlain, J.P.1
  • 37
    • 17544371921 scopus 로고    scopus 로고
    • Characterization of interactions between the neurofilament triplet proteins by the yeast two-hybrid system
    • Leung C. L., Liem R. K. H. Characterization of interactions between the neurofilament triplet proteins by the yeast two-hybrid system. J. Biol. Chem. 271:1996;14041-14044.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14041-14044
    • Leung, C.L.1    Liem, R.K.H.2
  • 38
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields S., Song O. A novel genetic system to detect protein-protein interactions. Nature. 340:1989;245-247.
    • (1989) Nature , vol.340 , pp. 245-247
    • Fields, S.1    Song, O.2
  • 40
    • 0030001020 scopus 로고    scopus 로고
    • Identification of the spectrin subunit and domains required for formation of spectrin/adducin/actin complexes
    • Li X., Bennett V. Identification of the spectrin subunit and domains required for formation of spectrin/adducin/actin complexes. J. Biol. Chem. 271:1996;15695-15702.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15695-15702
    • Li, X.1    Bennett, V.2
  • 42
    • 0027174586 scopus 로고
    • Use of the two-hybrid system to identify the domain of p53 involved in oligomerization
    • Iwabuchi K., Li B., Bartel P., Fields S. Use of the two-hybrid system to identify the domain of p53 involved in oligomerization. Oncogene. 8:1993;1693-1696.
    • (1993) Oncogene , vol.8 , pp. 1693-1696
    • Iwabuchi, K.1    Li, B.2    Bartel, P.3    Fields, S.4
  • 43
    • 0027163762 scopus 로고
    • Identification of mutations in p53 that affect its binding to SV40 T antigen by using the yeast two-hybrid system
    • Li B., Fields S. Identification of mutations in p53 that affect its binding to SV40 T antigen by using the yeast two-hybrid system. FASEB J. 7:1993;957-963.
    • (1993) FASEB J. , vol.7 , pp. 957-963
    • Li, B.1    Fields, S.2
  • 45
    • 0028124463 scopus 로고
    • The two-hybrid system: An assay for protein-protein interactions
    • Fields S., Sternglanz R. The two-hybrid system: An assay for protein-protein interactions. Trends Genet. 10:1994;286-292.
    • (1994) Trends Genet. , vol.10 , pp. 286-292
    • Fields, S.1    Sternglanz, R.2
  • 46
    • 0030856050 scopus 로고    scopus 로고
    • Two-hybrid analysis reveals fundamental differences in direct interactions between desmoplakin and cell type-specific intermediate filaments
    • Meng J.-J., Bornslaeger E. A., Green K. J., Steinert P. M., Ip W. Two-hybrid analysis reveals fundamental differences in direct interactions between desmoplakin and cell type-specific intermediate filaments. J. Biol. Chem. 272:1997;21495-21503.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21495-21503
    • Meng, J.-J.1    Bornslaeger, E.A.2    Green, K.J.3    Steinert, P.M.4    Ip, W.5
  • 47
    • 0025903440 scopus 로고
    • Intermediate filaments-associated proteins
    • Foisner R., Wiche G. Intermediate filaments-associated proteins. Curr. Opin. Cell Biol. 3:1991;75-81.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 75-81
    • Foisner, R.1    Wiche, G.2
  • 48
    • 0030976095 scopus 로고    scopus 로고
    • Definition of a sequence unique in βiI spectrin required for its axon-specific interaction with fodaxin (A60)
    • Hayes N. V. L., Phillips G. W., Carden M. J., Baines A. J. Definition of a sequence unique in βII spectrin required for its axon-specific interaction with fodaxin (A60). J. Neurochem. 68:1997;1686-1695.
    • (1997) J. Neurochem. , vol.68 , pp. 1686-1695
    • Hayes, N.V.L.1    Phillips, G.W.2    Carden, M.J.3    Baines, A.J.4
  • 49
    • 0024387820 scopus 로고
    • A novel component of the axonal cortical cytoskeleton, A60, defined by a monoclonal antibody
    • Rainer D. A., Baines A. J. A novel component of the axonal cortical cytoskeleton, A60, defined by a monoclonal antibody. J. Cell Sci. 94:1989;489-500.
    • (1989) J. Cell Sci. , vol.94 , pp. 489-500
    • Rainer, D.A.1    Baines, A.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.