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Volumn 14, Issue 8, 2004, Pages 650-658

Drebrin is a novel connexin-43 binding partner that links gap junctions to the submembrane cytoskeleton

Author keywords

[No Author keywords available]

Indexed keywords

CONNEXIN 43; DREBRINS; NEUROPEPTIDE; PRIMER DNA; SMALL INTERFERING RNA;

EID: 1942445036     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2004.03.063     Document Type: Article
Times cited : (166)

References (31)
  • 1
    • 0030028301 scopus 로고    scopus 로고
    • The gap junction communication channel
    • Kumar N.M., Gilula N.B. The gap junction communication channel. Cell. 84:1996;381-388.
    • (1996) Cell , vol.84 , pp. 381-388
    • Kumar, N.M.1    Gilula, N.B.2
  • 2
    • 0033224243 scopus 로고    scopus 로고
    • Selective transfer of endogenous metabolites through gap junctions composed of different connexins
    • Goldberg G.S., Lampe P.D., Nicholson B.J. Selective transfer of endogenous metabolites through gap junctions composed of different connexins. Nat. Cell Biol. 1:1999;457-459.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 457-459
    • Goldberg, G.S.1    Lampe, P.D.2    Nicholson, B.J.3
  • 5
    • 0032557460 scopus 로고    scopus 로고
    • Direct association of the gap junction protein connexin-43 with ZO-1 in cardiac myocytes
    • Toyofuku T., Yabuki M., Otsu K., Kuzuya T., Hori M., Tada M. Direct association of the gap junction protein connexin-43 with ZO-1 in cardiac myocytes. J. Biol. Chem. 273:1998;12725-12731.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12725-12731
    • Toyofuku, T.1    Yabuki, M.2    Otsu, K.3    Kuzuya, T.4    Hori, M.5    Tada, M.6
  • 6
    • 13144252170 scopus 로고    scopus 로고
    • The gap junction protein connexin-43 interacts with the second PDZ domain of the zona occludens-1 protein
    • Giepmans B.N., Moolenaar W.H. The gap junction protein connexin-43 interacts with the second PDZ domain of the zona occludens-1 protein. Curr. Biol. 8:1998;931-934.
    • (1998) Curr. Biol. , vol.8 , pp. 931-934
    • Giepmans, B.N.1    Moolenaar, W.H.2
  • 8
    • 0035896527 scopus 로고    scopus 로고
    • Interaction of c-Src with gap junction protein connexin-43. Role in the regulation of cell-cell communication
    • Giepmans B.N., Hengeveld T., Postma F.R., Moolenaar W.H. Interaction of c-Src with gap junction protein connexin-43. Role in the regulation of cell-cell communication. J. Biol. Chem. 276:2001;8544-8549.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8544-8549
    • Giepmans, B.N.1    Hengeveld, T.2    Postma, F.R.3    Moolenaar, W.H.4
  • 9
    • 0028238878 scopus 로고
    • Actin-binding protein, drebrin, accumulates in submembranous regions in parallel with neuronal differentiation
    • Asada H., Uyemura K., Shirao T. Actin-binding protein, drebrin, accumulates in submembranous regions in parallel with neuronal differentiation. J. Neurosci. Res. 38:1994;149-159.
    • (1994) J. Neurosci. Res. , vol.38 , pp. 149-159
    • Asada, H.1    Uyemura, K.2    Shirao, T.3
  • 10
    • 0037166050 scopus 로고    scopus 로고
    • Drebrin, a dendritic spine protein, is manifold decreased in brains of patients with Alzheimer's disease and Down syndrome
    • Shim K.S., Lubec G. Drebrin, a dendritic spine protein, is manifold decreased in brains of patients with Alzheimer's disease and Down syndrome. Neurosci. Lett. 324:2002;209-212.
    • (2002) Neurosci. Lett. , vol.324 , pp. 209-212
    • Shim, K.S.1    Lubec, G.2
  • 11
    • 0029898287 scopus 로고    scopus 로고
    • Transport of an external Lys-Asp-Glu-Leu (KDEL) protein from the plasma membrane to the endoplasmic reticulum: Studies with cholera toxin in Vero cells
    • Majoul I.V., Bastiaens P.I., Soling H.D. Transport of an external Lys-Asp-Glu-Leu (KDEL) protein from the plasma membrane to the endoplasmic reticulum. studies with cholera toxin in Vero cells J. Cell Biol. 133:1996;777-789.
    • (1996) J. Cell Biol. , vol.133 , pp. 777-789
    • Majoul, I.V.1    Bastiaens, P.I.2    Soling, H.D.3
  • 12
    • 0035407522 scopus 로고    scopus 로고
    • KDEL-cargo regulates interactions between proteins involved in COPI vesicle traffic: Measurements in living cells using FRET
    • Majoul I., Straub M., Hell S.W., Duden R., Soling H.D. KDEL-cargo regulates interactions between proteins involved in COPI vesicle traffic. measurements in living cells using FRET Dev. Cell. 1:2001;139-153.
    • (2001) Dev. Cell , vol.1 , pp. 139-153
    • Majoul, I.1    Straub, M.2    Hell, S.W.3    Duden, R.4    Soling, H.D.5
  • 13
    • 0036183614 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer analysis of protein-protein interactions in single living cells by multifocal multiphoton microscopy
    • Majoul I., Straub M., Duden R., Hell S.W., Soling H.D. Fluorescence resonance energy transfer analysis of protein-protein interactions in single living cells by multifocal multiphoton microscopy. J. Biotechnol. 82:2002;267-277.
    • (2002) J. Biotechnol. , vol.82 , pp. 267-277
    • Majoul, I.1    Straub, M.2    Duden, R.3    Hell, S.W.4    Soling, H.D.5
  • 14
    • 0036351317 scopus 로고    scopus 로고
    • Analysis of gene function in somatic mammalian cells using small interfering RNAs
    • Elbashir S.M., Harborth J., Weber K., Tuschl T. Analysis of gene function in somatic mammalian cells using small interfering RNAs. Methods. 26:2002;199-213.
    • (2002) Methods , vol.26 , pp. 199-213
    • Elbashir, S.M.1    Harborth, J.2    Weber, K.3    Tuschl, T.4
  • 15
    • 0035921428 scopus 로고    scopus 로고
    • V-Src phosphorylation of connexin 43 on Tyr247 and Tyr265 disrupts gap junctional communication
    • Lin R., Warn-Cramer B.J., Kurata W.E., Lau A.F. v-Src phosphorylation of connexin 43 on Tyr247 and Tyr265 disrupts gap junctional communication. J. Cell Biol. 154:2001;815-827.
    • (2001) J. Cell Biol. , vol.154 , pp. 815-827
    • Lin, R.1    Warn-Cramer, B.J.2    Kurata, W.E.3    Lau, A.F.4
  • 17
    • 0742289962 scopus 로고    scopus 로고
    • Gap junction communication between cells aggregated on a cellulose-coated polystyrene: Influence of connexin 43 phosphorylation
    • Faucheux N., Zahm J.M., Bonnet N., Legeay G., Nagel M.D. Gap junction communication between cells aggregated on a cellulose-coated polystyrene. influence of connexin 43 phosphorylation Biomaterials. 25:2004;2501-2506.
    • (2004) Biomaterials , vol.25 , pp. 2501-2506
    • Faucheux, N.1    Zahm, J.M.2    Bonnet, N.3    Legeay, G.4    Nagel, M.D.5
  • 18
    • 0028139040 scopus 로고
    • Drebrin, a development-associated brain protein from rat embryo, causes the dissociation of tropomyosin from actin filaments
    • Ishikawa R., Hayashi K., Shirao T., Xue Y., Takagi T., Sasaki Y., Kohama K. Drebrin, a development-associated brain protein from rat embryo, causes the dissociation of tropomyosin from actin filaments. J. Biol. Chem. 269:1994;29928-29933.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29928-29933
    • Ishikawa, R.1    Hayashi, K.2    Shirao, T.3    Xue, Y.4    Takagi, T.5    Sasaki, Y.6    Kohama, K.7
  • 19
    • 0035058882 scopus 로고    scopus 로고
    • Clustering and anchoring mechanisms of molecular constituents of postsynaptic scaffolds in dendritic spines
    • Shirao T., Sekino Y. Clustering and anchoring mechanisms of molecular constituents of postsynaptic scaffolds in dendritic spines. Neurosci. Res. 40:2001;1-7.
    • (2001) Neurosci. Res. , vol.40 , pp. 1-7
    • Shirao, T.1    Sekino, Y.2
  • 20
    • 0041342023 scopus 로고    scopus 로고
    • Drebrin-dependent actin clustering in dendritic filopodia governs synaptic targeting of postsynaptic density-95 and dendritic spine morphogenesis
    • Takahashi H., Sekino Y., Tanaka S., Mizui T., Kishi S., Shirao T. Drebrin-dependent actin clustering in dendritic filopodia governs synaptic targeting of postsynaptic density-95 and dendritic spine morphogenesis. J. Neurosci. 23:2003;6586-6595.
    • (2003) J. Neurosci. , vol.23 , pp. 6586-6595
    • Takahashi, H.1    Sekino, Y.2    Tanaka, S.3    Mizui, T.4    Kishi, S.5    Shirao, T.6
  • 21
    • 0036228744 scopus 로고    scopus 로고
    • Intercellular adhesion, signalling and the cytoskeleton
    • Jamora C., Fuchs E. Intercellular adhesion, signalling and the cytoskeleton. Nat. Cell Biol. 4:2002;E101-E108.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 101-E108
    • Jamora, C.1    Fuchs, E.2
  • 22
    • 0028821093 scopus 로고
    • Cell-to-cell adherens junction formation and actin filament organization: Similarities and differences between non-polarized fibroblasts and polarized epithelial cells
    • Yonemura S., Itoh M., Nagafuchi A., Tsukita S. Cell-to-cell adherens junction formation and actin filament organization. similarities and differences between non-polarized fibroblasts and polarized epithelial cells J. Cell Sci. 108:1995;127-142.
    • (1995) J. Cell Sci. , vol.108 , pp. 127-142
    • Yonemura, S.1    Itoh, M.2    Nagafuchi, A.3    Tsukita, S.4
  • 23
    • 0030748548 scopus 로고    scopus 로고
    • Involvement of ZO-1 in cadherin-based cell adhesion through its direct binding to alpha catenin and actin filaments
    • Itoh M., Nagafuchi A., Moroi S., Tsukita S. Involvement of ZO-1 in cadherin-based cell adhesion through its direct binding to alpha catenin and actin filaments. J. Cell Biol. 138:1997;181-192.
    • (1997) J. Cell Biol. , vol.138 , pp. 181-192
    • Itoh, M.1    Nagafuchi, A.2    Moroi, S.3    Tsukita, S.4
  • 24
    • 0030039226 scopus 로고    scopus 로고
    • Catenins and zonula occludens-1 form a complex during early stages in the assembly of tight junctions
    • Rajasekaran A.K., Hojo M., Huima T., Rodriguez Boulan E. Catenins and zonula occludens-1 form a complex during early stages in the assembly of tight junctions. J. Cell Biol. 132:1996;451-463.
    • (1996) J. Cell Biol. , vol.132 , pp. 451-463
    • Rajasekaran, A.K.1    Hojo, M.2    Huima, T.3    Rodriguez Boulan, E.4
  • 25
    • 0030025216 scopus 로고    scopus 로고
    • Disappearance of actin-binding protein, drebrin, from hippocampal synapses in Alzheimer's disease
    • Harigaya Y., Shoji M., Shirao T., Hirai S. Disappearance of actin-binding protein, drebrin, from hippocampal synapses in Alzheimer's disease. J. Neurosci. Res. 43:1996;87-92.
    • (1996) J. Neurosci. Res. , vol.43 , pp. 87-92
    • Harigaya, Y.1    Shoji, M.2    Shirao, T.3    Hirai, S.4
  • 26
    • 0029879282 scopus 로고    scopus 로고
    • Elevated connexin-43 immunoreactivity at sites of amyloid plaques in Alzheimer's disease
    • Nagy J.I., Li W., Hertzberg E.L., Marotta C.A. Elevated connexin-43 immunoreactivity at sites of amyloid plaques in Alzheimer's disease. Brain Res. 717:1996;173-178.
    • (1996) Brain Res. , vol.717 , pp. 173-178
    • Nagy, J.I.1    Li, W.2    Hertzberg, E.L.3    Marotta, C.A.4
  • 28
    • 0028077475 scopus 로고
    • Membrane insertion of gap junction connexins: Polytopic channel forming membrane proteins
    • Falk M.M., Kumar N.M., Gilula N.B. Membrane insertion of gap junction connexins. polytopic channel forming membrane proteins J. Cell Biol. 127:1994;343-354.
    • (1994) J. Cell Biol. , vol.127 , pp. 343-354
    • Falk, M.M.1    Kumar, N.M.2    Gilula, N.B.3
  • 30
    • 0018148591 scopus 로고
    • A study of positive staining of ultrathin frozen sections
    • Tokuyasu K.T. A study of positive staining of ultrathin frozen sections. J. Ultrastruct. Res. 63:1978;287-307.
    • (1978) J. Ultrastruct. Res. , vol.63 , pp. 287-307
    • Tokuyasu, K.T.1
  • 31
    • 0034659732 scopus 로고    scopus 로고
    • Postsynaptic scaffolds of excitatory and inhibitory synapses in hippocampal neurons: Maintenance of core components independent of actin filaments and microtubules
    • Allison D.W., Chervin A.S., Gelfand V.I., Craig A.M. Postsynaptic scaffolds of excitatory and inhibitory synapses in hippocampal neurons. maintenance of core components independent of actin filaments and microtubules J. Neurosci. 20:2000;4545-4554.
    • (2000) J. Neurosci. , vol.20 , pp. 4545-4554
    • Allison, D.W.1    Chervin, A.S.2    Gelfand, V.I.3    Craig, A.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.