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Volumn 132, Issue 3, 2009, Pages 263-280

Limiting transport steps and novel interactions of Connexin-43 along the secretory pathway

Author keywords

Arf; Connexins; COP; FRET; Gap junction

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR 6; CONNEXIN 43; DYNEIN ADENOSINE TRIPHOSPHATASE; GLATIRAMER; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; PROTEIN 14 3 3; PROTEIN P50;

EID: 69249229462     PISSN: 09486143     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00418-009-0617-x     Document Type: Article
Times cited : (25)

References (61)
  • 1
    • 0028971172 scopus 로고
    • Sequential coupling between COPII and COPI vesicle coats in endoplasmic reticulum to Golgi transport
    • M Aridor SI Bannykh T Rowe WE Balch 1995 Sequential coupling between COPII and COPI vesicle coats in endoplasmic reticulum to Golgi transport J Cell Biol 131 875 893
    • (1995) J Cell Biol , vol.131 , pp. 875-893
    • Aridor, M.1    Bannykh, S.I.2    Rowe, T.3    Balch, W.E.4
  • 2
    • 0037127035 scopus 로고    scopus 로고
    • Immunolocalisation of 14-3-3 isoforms in normal and scrapie-infected murine brain
    • HC Baxter WL Liu JL Forster A Aitken JR Fraser 2002 Immunolocalisation of 14-3-3 isoforms in normal and scrapie-infected murine brain Neuroscience 109 5 14
    • (2002) Neuroscience , vol.109 , pp. 5-14
    • Baxter, H.C.1    Liu, W.L.2    Forster, J.L.3    Aitken, A.4    Fraser, J.R.5
  • 3
    • 0842324801 scopus 로고    scopus 로고
    • The mechanisms of vesicle budding and fusion
    • JS Bonifacino BS Glick 2004 The mechanisms of vesicle budding and fusion Cell 116 153 166
    • (2004) Cell , vol.116 , pp. 153-166
    • Bonifacino, J.S.1    Glick, B.S.2
  • 4
    • 0016108076 scopus 로고
    • Measurement of electrical coupling between cells of axolotl embryos during cleavage divisions
    • VP Bozhkova IS Kvavilashvili NN Rott LM Chailakhyan 1974 Measurement of electrical coupling between cells of axolotl embryos during cleavage divisions Sov J Dev Biol 4 480 482
    • (1974) Sov J Dev Biol , vol.4 , pp. 480-482
    • Bozhkova, V.P.1    Kvavilashvili, I.S.2    Rott, N.N.3    Chailakhyan, L.M.4
  • 5
    • 0030727535 scopus 로고    scopus 로고
    • Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution
    • JK Burkhardt CJ Echeverri T Nilsson RB Vallee 1997 Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution J Cell Biol 139 469 484
    • (1997) J Cell Biol , vol.139 , pp. 469-484
    • Burkhardt, J.K.1    Echeverri, C.J.2    Nilsson, T.3    Vallee, R.B.4
  • 6
    • 69249226310 scopus 로고    scopus 로고
    • PhD thesis
    • Butkevich E (2004) PhD thesis. http://webdoc.sub.gwdg.de/diss/2004/ butkevich/butkevich.pdf
    • (2004)
    • Butkevich, E.1
  • 7
    • 1942445036 scopus 로고    scopus 로고
    • Drebrin is a novel connexin-43 binding partner that links gap junctions to the submembrane cytoskeleton
    • E Butkevich S Hulsmann D Wenzel T Shirao R Duden I Majoul 2004 Drebrin is a novel connexin-43 binding partner that links gap junctions to the submembrane cytoskeleton Curr Biol 14 650 658
    • (2004) Curr Biol , vol.14 , pp. 650-658
    • Butkevich, E.1    Hulsmann, S.2    Wenzel, D.3    Shirao, T.4    Duden, R.5    Majoul, I.6
  • 8
    • 69249234672 scopus 로고
    • Contact membranes in cell cultures and embryonic tissues
    • LM Chailakhyan 1976 Contact membranes in cell cultures and embryonic tissues Stud Biophys (Berlin) 56 23 24
    • (1976) Stud Biophys (Berlin) , vol.56 , pp. 23-24
    • Chailakhyan, L.M.1
  • 9
    • 0025184208 scopus 로고
    • Ligand-receptor and junction-mediated cell-cell interactions: Comparison of the two principles
    • LM Chailakhyan 1990 Ligand-receptor and junction-mediated cell-cell interactions: comparison of the two principles Differentiation 45 1 6
    • (1990) Differentiation , vol.45 , pp. 1-6
    • Chailakhyan, L.M.1
  • 12
  • 13
    • 0030017422 scopus 로고    scopus 로고
    • Functional and structural assessment of intercellular communication. Increased conduction velocity and enhanced connexin expression in dibutyryl cAMP-treated cultured cardiac myocytes
    • BJ Darrow VG Fast AG Kléber EC Beyer JE Saffitz 1996 Functional and structural assessment of intercellular communication. Increased conduction velocity and enhanced connexin expression in dibutyryl cAMP-treated cultured cardiac myocytes Circ Res 79 174 183
    • (1996) Circ Res , vol.79 , pp. 174-183
    • Darrow, B.J.1    Fast, V.G.2    Kléber, A.G.3    Beyer, E.C.4    Saffitz, J.E.5
  • 14
    • 0027953550 scopus 로고
    • Dominant inhibitory mutants of ARF1 block endoplasmic reticulum to Golgi transport and trigger disassembly of the Golgi apparatus
    • C Dascher WE Balch 1994 Dominant inhibitory mutants of ARF1 block endoplasmic reticulum to Golgi transport and trigger disassembly of the Golgi apparatus J Biol Chem 269 1437 1448
    • (1994) J Biol Chem , vol.269 , pp. 1437-1448
    • Dascher, C.1    Balch, W.E.2
  • 15
    • 0038726917 scopus 로고    scopus 로고
    • ER-to-Golgi transport: COP i and COP II function (Review)
    • R Duden 2003 ER-to-Golgi transport: COP I and COP II function (Review) Mol Membr Biol 20 197 207
    • (2003) Mol Membr Biol , vol.20 , pp. 197-207
    • Duden, R.1
  • 16
    • 42749085966 scopus 로고    scopus 로고
    • Gap junctions: Multifaceted regulators of embryonic cortical development
    • LA Elias AR Kriegstein 2008 Gap junctions: multifaceted regulators of embryonic cortical development Trends Neurosci 31 243 250
    • (2008) Trends Neurosci , vol.31 , pp. 243-250
    • Elias, L.A.1    Kriegstein, A.R.2
  • 17
    • 35348885467 scopus 로고    scopus 로고
    • Two human ARFGAPs associated with COP-I-coated vesicles
    • G Frigerio N Grimsey M Dale I Majoul R Duden 2007 Two human ARFGAPs associated with COP-I-coated vesicles Traffic 8 1644 1655
    • (2007) Traffic , vol.8 , pp. 1644-1655
    • Frigerio, G.1    Grimsey, N.2    Dale, M.3    Majoul, I.4    Duden, R.5
  • 20
    • 0033224243 scopus 로고    scopus 로고
    • Selective transfer of endogenous metabolites through gap junctions composed of different connexins
    • GS Goldberg PD Lampe BJ Nicholson 1999 Selective transfer of endogenous metabolites through gap junctions composed of different connexins Nat Cell Biol 1 457 459
    • (1999) Nat Cell Biol , vol.1 , pp. 457-459
    • Goldberg, G.S.1    Lampe, P.D.2    Nicholson, B.J.3
  • 22
    • 0037093237 scopus 로고    scopus 로고
    • Connexin 43 suppresses human glioblastoma cell growth by down-regulation of monocyte chemotactic protein 1, as discovered using protein array technology
    • R Huang Y Lin CC Wang J Gano B Lin Q Shi A Boynton J Burke RP Huang 2002 Connexin 43 suppresses human glioblastoma cell growth by down-regulation of monocyte chemotactic protein 1, as discovered using protein array technology Cancer Res 62 2806 2812
    • (2002) Cancer Res , vol.62 , pp. 2806-2812
    • Huang, R.1    Lin, Y.2    Wang, C.C.3    Gano, J.4    Lin, B.5    Shi, Q.6    Boynton, A.7    Burke, J.8    Huang, R.P.9
  • 23
    • 30044435325 scopus 로고    scopus 로고
    • An effector domain mutant of Arf6 implicates phospholipase D in endosomal membrane recycling
    • OF Jovanovic D Brown JG Donaldson 2006 An effector domain mutant of Arf6 implicates phospholipase D in endosomal membrane recycling Mol Biol Cell 17 327 335
    • (2006) Mol Biol Cell , vol.17 , pp. 327-335
    • Jovanovic, O.F.1    Brown, D.2    Donaldson, J.G.3
  • 25
    • 0037013148 scopus 로고    scopus 로고
    • Role of phosphatidylinositol (4,5) bisphosphate organization in membrane transport by the Unc104 kinesin motor
    • DR Klopfenstein M Tomishige N Stuurman RD Vale 2002 Role of phosphatidylinositol (4,5) bisphosphate organization in membrane transport by the Unc104 kinesin motor Cell 109 347 358
    • (2002) Cell , vol.109 , pp. 347-358
    • Klopfenstein, D.R.1    Tomishige, M.2    Stuurman, N.3    Vale, R.D.4
  • 26
    • 0036375021 scopus 로고    scopus 로고
    • Implication of direct host-tumor intercellular interactions in non-immune host resistance to neoplastic growth
    • V Krutovskikh 2002 Implication of direct host-tumor intercellular interactions in non-immune host resistance to neoplastic growth Sem Cancer Biol 12 267 276
    • (2002) Sem Cancer Biol , vol.12 , pp. 267-276
    • Krutovskikh, V.1
  • 28
    • 0030028301 scopus 로고    scopus 로고
    • The gap junction communication channel
    • NM Kumar NB Gilula 1996 The gap junction communication channel Cell 84 381 388
    • (1996) Cell , vol.84 , pp. 381-388
    • Kumar, N.M.1    Gilula, N.B.2
  • 29
    • 41949131052 scopus 로고    scopus 로고
    • A novel connexin43-interacting protein, CIP75, which belongs to the UbL-UBA protein family, regulates the turnover of connexin43
    • X Li V Su WE Kurata C Jin AF Lau 2008 A novel connexin43-interacting protein, CIP75, which belongs to the UbL-UBA protein family, regulates the turnover of connexin43 J Biol Chem 283 5748 5759
    • (2008) J Biol Chem , vol.283 , pp. 5748-5759
    • Li, X.1    Su, V.2    Kurata, W.E.3    Jin, C.4    Lau, A.F.5
  • 30
    • 0019624299 scopus 로고
    • Junctional intercellular communication: The cell-to-cell membrane channel
    • WR Loewenstein 1981 Junctional intercellular communication: the cell-to-cell membrane channel Physiol Rev 61 829 913
    • (1981) Physiol Rev , vol.61 , pp. 829-913
    • Loewenstein, W.R.1
  • 31
    • 0029844218 scopus 로고    scopus 로고
    • In vivo assembly of coatomer, the COP-I coat precursor
    • M Lowe TE Kreis 1996 In vivo assembly of coatomer, the COP-I coat precursor J Biol Chem 271 30725 30730
    • (1996) J Biol Chem , vol.271 , pp. 30725-30730
    • Lowe, M.1    Kreis, T.E.2
  • 32
    • 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
    • IV Majoul PI Bastiaens HD Soling 1996 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 133 777 789
    • (1996) J Cell Biol , vol.133 , pp. 777-789
    • Majoul, I.V.1    Bastiaens, P.I.2    Soling, H.D.3
  • 34
    • 0036382829 scopus 로고    scopus 로고
    • Assembly-dependent assays in the detection of receptor-receptor interactions
    • M Margeta-Mitrovic 2002 Assembly-dependent assays in the detection of receptor-receptor interactions Methods 4 311 317
    • (2002) Methods , vol.4 , pp. 311-317
    • Margeta-Mitrovic, M.1
  • 35
    • 0033667466 scopus 로고    scopus 로고
    • A trafficking checkpoint controls GABA(B) receptor heterodimerization
    • M Margeta-Mitrovic YN Jan LY Jan 2000 A trafficking checkpoint controls GABA(B) receptor heterodimerization Neuron 27 97 106
    • (2000) Neuron , vol.27 , pp. 97-106
    • Margeta-Mitrovic, M.1    Jan, Y.N.2    Jan, L.Y.3
  • 36
    • 20444387943 scopus 로고    scopus 로고
    • Defining a minimal motif required to prevent connexin oligomerization in the endoplasmic reticulum
    • J Maza J Das Sarma M Koval 2005 Defining a minimal motif required to prevent connexin oligomerization in the endoplasmic reticulum J Biol Chem 280 21115 21121
    • (2005) J Biol Chem , vol.280 , pp. 21115-21121
    • Maza, J.1    Das Sarma, J.2    Koval, M.3
  • 37
    • 0036873006 scopus 로고    scopus 로고
    • Connexins and cancer
    • M Mesnil 2002 Connexins and cancer Biol Cell 94 493 500
    • (2002) Biol Cell , vol.94 , pp. 493-500
    • Mesnil, M.1
  • 39
    • 0034581516 scopus 로고    scopus 로고
    • Monitoring protein conformations and interactions by fluorescence resonance energy transfer between mutants of green fluorescent protein
    • A Miyawaki RY Tsien 2000 Monitoring protein conformations and interactions by fluorescence resonance energy transfer between mutants of green fluorescent protein Methods Enzymol 327 472 500
    • (2000) Methods Enzymol , vol.327 , pp. 472-500
    • Miyawaki, A.1    Tsien, R.Y.2
  • 40
    • 0025083620 scopus 로고
    • Gap junctional intercellular communication and the regulation of connexin expression and function
    • LS Musil DA Goodenough 1990 Gap junctional intercellular communication and the regulation of connexin expression and function Curr Opin Cell Biol 2 875 880
    • (1990) Curr Opin Cell Biol , vol.2 , pp. 875-880
    • Musil, L.S.1    Goodenough, D.A.2
  • 41
    • 3342977736 scopus 로고    scopus 로고
    • Characterization of a nonclathrin endocytic pathway: Membrane cargo and lipid requirements
    • N Naslavsky R Weigert JG Donaldson 2004 Characterization of a nonclathrin endocytic pathway: membrane cargo and lipid requirements Mol Biol Cell 15 3542 3552
    • (2004) Mol Biol Cell , vol.15 , pp. 3542-3552
    • Naslavsky, N.1    Weigert, R.2    Donaldson, J.G.3
  • 42
    • 0037112329 scopus 로고    scopus 로고
    • Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals
    • I O'Kelly MH Butler N Zilberberg SA Goldstein 2002 Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals Cell 111 577 588
    • (2002) Cell , vol.111 , pp. 577-588
    • O'Kelly, I.1    Butler, M.H.2    Zilberberg, N.3    Goldstein, S.A.4
  • 43
    • 25444505690 scopus 로고    scopus 로고
    • Contribution of gap junctional communication between tumor cells and astroglia to the invasion of the brain parenchyma by human glioblastomas
    • DOI 10.1186/1471-2121-6-7
    • R Oliveira C Christov JS Guillamo S de Boüard S Palfi L Venance M Tardy M Peschanski 2005 Contribution of gap junctional communication between tumor cells and astroglia to the invasion of the brain parenchyma by human glioblastomas BMC Cell Biol 6 7 10.1186/1471-2121-6-7 (Pubitemid 41357629)
    • (2005) BMC Cell Biology , vol.6 , pp. 7
    • Oliveira, R.1    Christov, C.2    Guillamo, J.S.3    De Bouard, S.4    Palfi, S.5    Venance, L.6    Tardy, M.7    Peschanski, M.8
  • 45
    • 33749368927 scopus 로고    scopus 로고
    • Molecular dynamics and in vitro analysis of Connexin43: A new 14-3-3 mode-1 interacting protein
    • DJ Park TA Freitas CJ Wallick CV Guyette BJ Warn-Cramer 2006 Molecular dynamics and in vitro analysis of Connexin43: a new 14-3-3 mode-1 interacting protein Protein Sci 15 2344 2355
    • (2006) Protein Sci , vol.15 , pp. 2344-2355
    • Park, D.J.1    Freitas, T.A.2    Wallick, C.J.3    Guyette, C.V.4    Warn-Cramer, B.J.5
  • 47
    • 0035341508 scopus 로고    scopus 로고
    • An NMDA receptor ER retention signal regulated by phosphorylation and alternative splicing
    • DB Scott TA Blanpied GT Swanson C Zhang MD Ehlers 2001 An NMDA receptor ER retention signal regulated by phosphorylation and alternative splicing J Neurosci 21 3063 3072
    • (2001) J Neurosci , vol.21 , pp. 3063-3072
    • Scott, D.B.1    Blanpied, T.A.2    Swanson, G.T.3    Zhang, C.4    Ehlers, M.D.5
  • 48
    • 1642340298 scopus 로고    scopus 로고
    • New insights into the expression and function of neural connexins with transgenic mouse mutants
    • DOI 10.1016/j.brainresrev.2004.05.006, PII S0165017304000712, Chemical and Electrical Synapses
    • G Sohl B Odermatt S Maxeiner J Degen K Willecke 2004 New insights into the expression and function of neural connexins with transgenic mouse mutants Brain Res Rev 47 245 259 (Pubitemid 39574323)
    • (2004) Brain Research Reviews , vol.47 , Issue.1-3 , pp. 245-259
    • Sohl, G.1    Odermatt, B.2    Maxeiner, S.3    Degen, J.4    Willecke, K.5
  • 49
    • 0034520590 scopus 로고    scopus 로고
    • PDZ domain suppression of an ER retention signal in NMDA receptor NR1 splice variants
    • S Standley KW Roche J McCallum N Sans RJ Wenthold 2000 PDZ domain suppression of an ER retention signal in NMDA receptor NR1 splice variants Neuron 28 887 898
    • (2000) Neuron , vol.28 , pp. 887-898
    • Standley, S.1    Roche, K.W.2    McCallum, J.3    Sans, N.4    Wenthold, R.J.5
  • 50
    • 27644547807 scopus 로고    scopus 로고
    • Mechanisms of Cx43 and Cx26 transport to the plasma membrane and gap junction regeneration
    • T Thomas K Jordan J Simek Q Shao C Jedeszko P Walton DW Laird 2005 Mechanisms of Cx43 and Cx26 transport to the plasma membrane and gap junction regeneration J Cell Sci 118 4451 4462
    • (2005) J Cell Sci , vol.118 , pp. 4451-4462
    • Thomas, T.1    Jordan, K.2    Simek, J.3    Shao, Q.4    Jedeszko, C.5    Walton, P.6    Laird, D.W.7
  • 51
    • 0018148591 scopus 로고
    • A study of positive staining of ultrathin frozen sections
    • KT Tokuyasu 1978 A study of positive staining of ultrathin frozen sections J Ultrastruct Res 63 287 307
    • (1978) J Ultrastruct Res , vol.63 , pp. 287-307
    • Tokuyasu, K.T.1
  • 53
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • RY Tsien 1998 The green fluorescent protein Annu Rev Biochem 67 509 544
    • (1998) Annu Rev Biochem , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 54
    • 0033582686 scopus 로고    scopus 로고
    • Three-dimensional structure of a recombinant gap junction membrane channel
    • VM Unger NM Kumar NB Gilula M Yeager 1999 Three-dimensional structure of a recombinant gap junction membrane channel Science 283 1176 1180
    • (1999) Science , vol.283 , pp. 1176-1180
    • Unger, V.M.1    Kumar, N.M.2    Gilula, N.B.3    Yeager, M.4
  • 56
    • 65649098623 scopus 로고    scopus 로고
    • Conformational maturation and post-ER multisubunit assembly of gap junction proteins
    • JK VanSlyke CC Naus LS Musil 2009 Conformational maturation and post-ER multisubunit assembly of gap junction proteins Mol Biol Cell 20 2451 2463
    • (2009) Mol Biol Cell , vol.20 , pp. 2451-2463
    • Vanslyke, J.K.1    Naus, C.C.2    Musil, L.S.3
  • 58
    • 0034788270 scopus 로고    scopus 로고
    • An ER retention signal explains differences in surface expression of NMDA and AMPA receptor subunits
    • H Xia ZD Hornby RC Malenka 2001 An ER retention signal explains differences in surface expression of NMDA and AMPA receptor subunits Neuropharmacology 41 714 723
    • (2001) Neuropharmacology , vol.41 , pp. 714-723
    • Xia, H.1    Hornby, Z.D.2    Malenka, R.C.3
  • 59
    • 0029780351 scopus 로고    scopus 로고
    • The molecular structure of green fluorescent protein
    • Yang F, Moss LG, Phillips GN Jr (1996) The molecular structure of green fluorescent protein. Nat Biotech 14:1246-1251
    • (1996) Nat Biotech , vol.14 , pp. 1246-1251
    • Yang, F.1    Moss, L.G.2    Jr P.Gn3
  • 60
    • 0037447231 scopus 로고    scopus 로고
    • 14-3-3 dimers probe the assembly status of multimeric membrane proteins
    • H Yuan K Michelsen B Schwappach 2003 14-3-3 dimers probe the assembly status of multimeric membrane proteins Curr Biol 13 638 646
    • (2003) Curr Biol , vol.13 , pp. 638-646
    • Yuan, H.1    Michelsen, K.2    Schwappach, B.3
  • 61
    • 0033103174 scopus 로고    scopus 로고
    • A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane K(ATP) channels
    • N Zerangue B Schwappach YN Jan LY Jan 1999 A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane K(ATP) channels Neuron 22 537 548
    • (1999) Neuron , vol.22 , pp. 537-548
    • Zerangue, N.1    Schwappach, B.2    Jan, Y.N.3    Jan, L.Y.4


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