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Volumn 16, Issue 11, 2005, Pages 5247-5257

Cytosolic stress reduces degradation of connexin43 internalized from the cell surface and enhances gap junction formation and function

Author keywords

[No Author keywords available]

Indexed keywords

CONNEXIN 43; PROTEASOME INHIBITOR;

EID: 27644455648     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E05-05-0415     Document Type: Article
Times cited : (74)

References (41)
  • 1
    • 0242442576 scopus 로고    scopus 로고
    • Expression of CONNEXIN43 is highly sensitive to ionizing radiation and other environmental stresses
    • Azzam, E. I., de Toledo, S. M., and Little, J. B. (2003). Expression of CONNEXIN43 is highly sensitive to ionizing radiation and other environmental stresses. Cancer Res. 63, 7128-7135.
    • (2003) Cancer Res. , vol.63 , pp. 7128-7135
    • Azzam, E.I.1    De Toledo, S.M.2    Little, J.B.3
  • 2
    • 0032555956 scopus 로고    scopus 로고
    • Rapid turnover of connexin43 in the adult rat heart
    • Beardslee, M. A., Laing, J. G., Beyer, E. C., and Saffitz, J. E. (1998). Rapid turnover of connexin43 in the adult rat heart. Circ. Res. 83, 629-635.
    • (1998) Circ. Res. , vol.83 , pp. 629-635
    • Beardslee, M.A.1    Laing, J.G.2    Beyer, E.C.3    Saffitz, J.E.4
  • 3
    • 0026623463 scopus 로고
    • Examining the function and regulation of hsp 70 in cells subjected to metabolic stress
    • Beckmann, R. P., Lovett, M., and Welch, W. J. (1992). Examining the function and regulation of hsp 70 in cells subjected to metabolic stress. J. Cell Biol. 117, 1137-1150.
    • (1992) J. Cell Biol. , vol.117 , pp. 1137-1150
    • Beckmann, R.P.1    Lovett, M.2    Welch, W.J.3
  • 6
    • 0031785364 scopus 로고    scopus 로고
    • Effect of chloroquine and leupeptin on intracellular accumulation of amyloid-β(Aβ) 1-42 peptide in a murine N9 microglial cell line
    • Chu, T., Tran, T., Yang, F., Beech, W., Cole, G. M., and Frautschy, S. A. (1998). Effect of chloroquine and leupeptin on intracellular accumulation of amyloid-β(Aβ) 1-42 peptide in a murine N9 microglial cell line. FEBS Lett. 436, 439-444.
    • (1998) FEBS Lett. , vol.436 , pp. 439-444
    • Chu, T.1    Tran, T.2    Yang, F.3    Beech, W.4    Cole, G.M.5    Frautschy, S.A.6
  • 7
    • 9144274481 scopus 로고    scopus 로고
    • Ganglioside GD3 traffics from the trans-Golgi network to plasma membrane by a Rab11-independent and brefeldin A-insensitive exocytic pathway
    • Crespo, P. M., Iglesias-Bartolome, R., and Daniotti, J. L. (2004). Ganglioside GD3 traffics from the trans-Golgi network to plasma membrane by a Rab11-independent and brefeldin A-insensitive exocytic pathway. J. Biol. Chem. 279, 47610-47618.
    • (2004) J. Biol. Chem. , vol.279 , pp. 47610-47618
    • Crespo, P.M.1    Iglesias-Bartolome, R.2    Daniotti, J.L.3
  • 8
    • 0019603292 scopus 로고
    • Five-hour half-life of mouse liver gap-junction protein
    • Fallon, R. F., and Goodenough, D. A. (1981). Five-hour half-life of mouse liver gap-junction protein. J. Cell Biol. 90, 521-526.
    • (1981) J. Cell Biol. , vol.90 , pp. 521-526
    • Fallon, R.F.1    Goodenough, D.A.2
  • 10
    • 0344466781 scopus 로고    scopus 로고
    • Characterization and dynamics of aggresome formation by a cytosolic GFP-chimera
    • Garcia-Mata, R., Bebok, Z., Sorscher, E. J., and Sztul, E. S. (1999). Characterization and dynamics of aggresome formation by a cytosolic GFP-chimera. J. Cell Biol. 146, 1239-1254.
    • (1999) J. Cell Biol. , vol.146 , pp. 1239-1254
    • Garcia-Mata, R.1    Bebok, Z.2    Sorscher, E.J.3    Sztul, E.S.4
  • 11
    • 0037023764 scopus 로고    scopus 로고
    • A principal role for the proteasome in endoplasmic reticulum-associated degradation of misfolded intracellular cystic fibrosis transmembrane conductance regulator
    • Gelman, M. S., Kannegaard, E. S., and Kopito, R. R. (2002). A principal role for the proteasome in endoplasmic reticulum-associated degradation of misfolded intracellular cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 277, 11709-11714.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11709-11714
    • Gelman, M.S.1    Kannegaard, E.S.2    Kopito, R.R.3
  • 12
    • 0037382614 scopus 로고    scopus 로고
    • Beyond the gap: Functions of unpaired connexon channels
    • Goodenough, D. A., and Paul, D. L. (2003). Beyond the gap: functions of unpaired connexon channels. Nat. Rev. Mol. Cell. Biol. 4, 285-294.
    • (2003) Nat. Rev. Mol. Cell. Biol. , vol.4 , pp. 285-294
    • Goodenough, D.A.1    Paul, D.L.2
  • 13
    • 0022528457 scopus 로고
    • Alterations in hepatocyte plasma membrane in carbon tetrachloride poisoning. Freeze-fracture analysis of gap junction and electron spin resonance analysis of lipid fluidity
    • James, J. L., Friend, D. S., MacDonald, J. R., and Smuckler, E. A. (1986). Alterations in hepatocyte plasma membrane in carbon tetrachloride poisoning. Freeze-fracture analysis of gap junction and electron spin resonance analysis of lipid fluidity. Lab. Investig. 54, 268-274.
    • (1986) Lab. Investig. , vol.54 , pp. 268-274
    • James, J.L.1    Friend, D.S.2    MacDonald, J.R.3    Smuckler, E.A.4
  • 14
    • 0035085580 scopus 로고    scopus 로고
    • The origin of annular junctions: A mechanism of gap junction internalization
    • Jordan, K., Chodock, R., Hand, A. R., and Laird, D. W. (2001). The origin of annular junctions: a mechanism of gap junction internalization. J. Cell Sci. 114, 763-773.
    • (2001) J. Cell Sci. , vol.114 , pp. 763-773
    • Jordan, K.1    Chodock, R.2    Hand, A.R.3    Laird, D.W.4
  • 15
    • 0026561901 scopus 로고
    • Brefeldin A: Insights into the control of membrane traffic and organelle structure
    • Klausner, R. D., Donaldson, J. G., and Lippincott-Schwartz, J. (1992). Brefeldin A: insights into the control of membrane traffic and organelle structure. J. Cell Biol. 116, 1071-1080.
    • (1992) J. Cell Biol. , vol.116 , pp. 1071-1080
    • Klausner, R.D.1    Donaldson, J.G.2    Lippincott-Schwartz, J.3
  • 16
    • 0028817813 scopus 로고
    • The gap junction protein connexin43 is degraded via the ubiquitin proteasome pathway
    • Laing, J. G., and Beyer, E. C. (1995). The gap junction protein connexin43 is degraded via the ubiquitin proteasome pathway. J. Biol. Chem. 270, 26399-26403.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26399-26403
    • Laing, J.G.1    Beyer, E.C.2
  • 17
    • 0031281674 scopus 로고    scopus 로고
    • Degradation of connexin43 gap junctions involves both the proteasome and the lysosome
    • Laing, J. G., Tadros, P. N., Westphale, E. M., and Beyer, E. C. (1997). Degradation of connexin43 gap junctions involves both the proteasome and the lysosome. Exp. Cell Res. 236, 482-492.
    • (1997) Exp. Cell Res. , vol.236 , pp. 482-492
    • Laing, J.G.1    Tadros, P.N.2    Westphale, E.M.3    Beyer, E.C.4
  • 18
    • 0029176855 scopus 로고
    • Gap junction turnover, intracellular trafficking, and phosphorylation of connexin43 in brefeldin A-treated rat mammary tumor cells
    • Laird, D. W., Castillo, M., and Kasprzak, L. (1995). Gap junction turnover, intracellular trafficking, and phosphorylation of connexin43 in brefeldin A-treated rat mammary tumor cells. J. Cell Biol. 131, 1193-1203.
    • (1995) J. Cell Biol. , vol.131 , pp. 1193-1203
    • Laird, D.W.1    Castillo, M.2    Kasprzak, L.3
  • 19
    • 0025254368 scopus 로고
    • Increased thermostability of thermotolerant CHL V79 cells as determined by differential scanning calorimetry
    • Lepock, J. R., Frey, H. E., Heynen, M. P., Nishio, J., Waters, B., Ritchie, K. P., and Kruuv, J. (1990). Increased thermostability of thermotolerant CHL V79 cells as determined by differential scanning calorimetry. J. Cell. Physiol. 142, 628-634.
    • (1990) J. Cell. Physiol. , vol.142 , pp. 628-634
    • Lepock, J.R.1    Frey, H.E.2    Heynen, M.P.3    Nishio, J.4    Waters, B.5    Ritchie, K.P.6    Kruuv, J.7
  • 20
    • 0027199872 scopus 로고
    • Protein denaturation in intact hepatocytes and isolated cellular organelles during heat shock
    • Lepock, J. R., Frey, H. E., and Ritchie, K. P. (1993). Protein denaturation in intact hepatocytes and isolated cellular organelles during heat shock. J. Cell Biol. 122, 1267-1276.
    • (1993) J. Cell Biol. , vol.122 , pp. 1267-1276
    • Lepock, J.R.1    Frey, H.E.2    Ritchie, K.P.3
  • 21
    • 0037018146 scopus 로고    scopus 로고
    • Ubiquitination and proteasomal activity is required for transport of the EGF receptor to inner membranes of multivesicular bodies
    • Longva, K. E., Blystad, F. D., Stang, E., Larsen, A. M., Johannessen, L. E., and Madshus, I. H. (2002). Ubiquitination and proteasomal activity is required for transport of the EGF receptor to inner membranes of multivesicular bodies. J. Cell Biol. 156, 843-854.
    • (2002) J. Cell Biol. , vol.156 , pp. 843-854
    • Longva, K.E.1    Blystad, F.D.2    Stang, E.3    Larsen, A.M.4    Johannessen, L.E.5    Madshus, I.H.6
  • 22
    • 9444236763 scopus 로고    scopus 로고
    • Ubiquitin-dependent lysosomal degradation of the HNE-modified proteins in lens epithelial cells
    • Marques, C., Pereira, P., Taylor, A., Liang, J. N., Reddy, V. N., Szweda, L. I., and Shang, F. (2004). Ubiquitin-dependent lysosomal degradation of the HNE-modified proteins in lens epithelial cells. FASEB J. 18, 1424-1426.
    • (2004) FASEB J. , vol.18 , pp. 1424-1426
    • Marques, C.1    Pereira, P.2    Taylor, A.3    Liang, J.N.4    Reddy, V.N.5    Szweda, L.I.6    Shang, F.7
  • 23
    • 0022555867 scopus 로고
    • Acidification of the endocytic and exocytic pathways
    • Mellman, I., Fuchs, R., and Helenius, A. (1986). Acidification of the endocytic and exocytic pathways. Annu. Rev. Biochem. 55, 663-700.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 663-700
    • Mellman, I.1    Fuchs, R.2    Helenius, A.3
  • 24
    • 0026776711 scopus 로고
    • Post-Golgi membrane traffic: Brefeldin a inhibits export from distal Golgi compartments to the cell surface but not recycling
    • Miller, S. G., Carnell, L., and Moore, H. H. (1992). Post-Golgi membrane traffic: brefeldin A inhibits export from distal Golgi compartments to the cell surface but not recycling. J. Cell Biol. 118, 267-283.
    • (1992) J. Cell Biol. , vol.118 , pp. 267-283
    • Miller, S.G.1    Carnell, L.2    Moore, H.H.3
  • 25
    • 0023924166 scopus 로고
    • Characterization of the thermotolerant cell. I. Effects on protein synthesis activity and the regulation of heat-shock protein 70 expression
    • Mizzen, L. A., and Welch, W. J. (1988). Characterization of the thermotolerant cell. I. Effects on protein synthesis activity and the regulation of heat-shock protein 70 expression. J. Cell Biol. 106, 1105-1116.
    • (1988) J. Cell Biol. , vol.106 , pp. 1105-1116
    • Mizzen, L.A.1    Welch, W.J.2
  • 26
    • 0025155347 scopus 로고
    • Differential phosphorylation of the gap junction protein connexin43 in junctional communication-competent and -deficient cell lines
    • Musil, L. S., Cunningham, B. A., Edelman, G. M., and Goodenough, D. A. (1990). Differential phosphorylation of the gap junction protein connexin43 in junctional communication-competent and -deficient cell lines. J. Cell Biol. 111, 2077-2088.
    • (1990) J. Cell Biol. , vol.111 , pp. 2077-2088
    • Musil, L.S.1    Cunningham, B.A.2    Edelman, G.M.3    Goodenough, D.A.4
  • 27
    • 0025789648 scopus 로고
    • Biochemical analysis of connexin43 intracellular transport, phosphorylation, and assembly into gap junctional plaques
    • Musil, L. S., and Goodenough, D. A. (1991). Biochemical analysis of connexin43 intracellular transport, phosphorylation, and assembly into gap junctional plaques. J. Cell Biol. 115, 1357-1374.
    • (1991) J. Cell Biol. , vol.115 , pp. 1357-1374
    • Musil, L.S.1    Goodenough, D.A.2
  • 28
    • 0027364529 scopus 로고
    • Multisubunit assembly of an integral plasma membrane channel protein, gap junction connexin43, occurs after exit from the ER
    • Musil, L. S., and Goodenough, D. A. (1993). Multisubunit assembly of an integral plasma membrane channel protein, gap junction connexin43, occurs after exit from the ER. Cell 74, 1065-1077.
    • (1993) Cell , vol.74 , pp. 1065-1077
    • Musil, L.S.1    Goodenough, D.A.2
  • 29
    • 0034682799 scopus 로고    scopus 로고
    • Regulation of connexin degradation as a mechanism to increase gap junction assembly and function
    • Musil, L. S., Le, A. C., VanSlyke, J. K., and Roberts, L. M. (2000). Regulation of connexin degradation as a mechanism to increase gap junction assembly and function. J. Biol. Chem. 275, 25207-25215.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25207-25215
    • Musil, L.S.1    Le, A.C.2    VanSlyke, J.K.3    Roberts, L.M.4
  • 30
    • 0031563776 scopus 로고    scopus 로고
    • Selective monoclonal antibody recognition and cellular localization of an unphosphorylated form of connexin43
    • Nagy, J. I., Li, W. E., Roy, C., Doble, B. W., Gilchrist, J. S., Kardami, E., and Hertzberg, E. L. (1997). Selective monoclonal antibody recognition and cellular localization of an unphosphorylated form of connexin43. Exp. Cell Res. 236, 127-136.
    • (1997) Exp. Cell Res. , vol.236 , pp. 127-136
    • Nagy, J.I.1    Li, W.E.2    Roy, C.3    Doble, B.W.4    Gilchrist, J.S.5    Kardami, E.6    Hertzberg, E.L.7
  • 31
    • 0028218169 scopus 로고
    • Metabolic coupling of glutathione between mouse and quail cardiac myocytes and its protective role against oxidative stress
    • Nakamura, T. Y., Yamamoto, I., Kanno, Y., Shiba, Y., and Goshima, K. (1994). Metabolic coupling of glutathione between mouse and quail cardiac myocytes and its protective role against oxidative stress. Circ. Res. 74, 806-816.
    • (1994) Circ. Res. , vol.74 , pp. 806-816
    • Nakamura, T.Y.1    Yamamoto, I.2    Kanno, Y.3    Shiba, Y.4    Goshima, K.5
  • 32
    • 0042030808 scopus 로고    scopus 로고
    • Lysosomal and proteasomal degradation play distinct roles in the life cycle of Cx43 in gap junctional intercellular communication-deficient and -competent breast tumor cells
    • Qin, H., Shao, Q., Igdoura, S. A., Alaoui-Jamali, M. A., and Laird, D. W. (2003). Lysosomal and proteasomal degradation play distinct roles in the life cycle of Cx43 in gap junctional intercellular communication-deficient and -competent breast tumor cells. J. Biol. Chem. 278, 30005-30014.
    • (2003) J. Biol. Chem. , vol.278 , pp. 30005-30014
    • Qin, H.1    Shao, Q.2    Igdoura, S.A.3    Alaoui-Jamali, M.A.4    Laird, D.W.5
  • 33
    • 0028330487 scopus 로고
    • Astrocytes as rapid sensors of peripheral axotomy in the facial nucleus of rats
    • Rohlmann, A., Laskawi, R., Hofer, A., Dermietzel, R., and Wolff, J. R. (1994). Astrocytes as rapid sensors of peripheral axotomy in the facial nucleus of rats. Neuroreport 5, 409-412.
    • (1994) Neuroreport , vol.5 , pp. 409-412
    • Rohlmann, A.1    Laskawi, R.2    Hofer, A.3    Dermietzel, R.4    Wolff, J.R.5
  • 34
    • 0034131086 scopus 로고    scopus 로고
    • Increased connexin43 gap junction protein in hamster cardiomyocytes during cold acclimatization and hibernation
    • Saitongdee, P., Milner, P., Becker, D. L., Knight, G. E., and Burnstock, G. (2000). Increased connexin43 gap junction protein in hamster cardiomyocytes during cold acclimatization and hibernation. Cardiovasc. Res. 47, 108-115.
    • (2000) Cardiovasc. Res. , vol.47 , pp. 108-115
    • Saitongdee, P.1    Milner, P.2    Becker, D.L.3    Knight, G.E.4    Burnstock, G.5
  • 35
    • 0030936274 scopus 로고    scopus 로고
    • Synaptic-like microvesicles of neuroendocrine cells originate from a novel compartment that is continuous with the plasma membrane and devoid of transfetrin receptor
    • Schmidt, A., Hannah, M. J., and Huttner, W. B. (1997). Synaptic-like microvesicles of neuroendocrine cells originate from a novel compartment that is continuous with the plasma membrane and devoid of transfetrin receptor. J. Cell Biol. 137, 445-458.
    • (1997) J. Cell Biol. , vol.137 , pp. 445-458
    • Schmidt, A.1    Hannah, M.J.2    Huttner, W.B.3
  • 36
    • 1642407845 scopus 로고    scopus 로고
    • Regulation of connexin biosynthesis, assembly, gap junction formation, and removal
    • Segretain, D., and Falk, M. M. (2004). Regulation of connexin biosynthesis, assembly, gap junction formation, and removal. Biochim. Biophys. Acta 1662, 3-21.
    • (2004) Biochim. Biophys. Acta , vol.1662 , pp. 3-21
    • Segretain, D.1    Falk, M.M.2
  • 37
    • 0028306459 scopus 로고
    • Expression of achaete-scute homolog 3 in Xenopus embryos converts ectodermal cells to a neural fate
    • Turner, D. L., and Weintraub, H. (1994). Expression of achaete-scute homolog 3 in Xenopus embryos converts ectodermal cells to a neural fate. Genes Dev. 8, 1434-1447.
    • (1994) Genes Dev. , vol.8 , pp. 1434-1447
    • Turner, D.L.1    Weintraub, H.2
  • 38
    • 0030888343 scopus 로고    scopus 로고
    • Conductances and selective permeability of connexin43 gap junction channels examined in neonatal rat heart cells
    • Valiunas, V., Bukauskas, F. F., and Weingart, R. (1997). Conductances and selective permeability of connexin43 gap junction channels examined in neonatal rat heart cells. Circ. Res. 80, 708-719.
    • (1997) Circ. Res. , vol.80 , pp. 708-719
    • Valiunas, V.1    Bukauskas, F.F.2    Weingart, R.3
  • 39
    • 0034047183 scopus 로고    scopus 로고
    • Intracellular transport, assembly, and degradation of wild-type and disease-linked mutant gap junction proteins
    • VanSlyke, J. K., Deschenes, S. M., and Musil, L. S. (2000). Intracellular transport, assembly, and degradation of wild-type and disease-linked mutant gap junction proteins. Mol. Biol. Cell 11, 1933-1946.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1933-1946
    • VanSlyke, J.K.1    Deschenes, S.M.2    Musil, L.S.3
  • 40
    • 0034106939 scopus 로고    scopus 로고
    • Analysis of connexin intracellular transport and assembly
    • VanSlyke, J. K., and Musil, L. S. (2000). Analysis of connexin intracellular transport and assembly. Methods 20, 156-164.
    • (2000) Methods , vol.20 , pp. 156-164
    • VanSlyke, J.K.1    Musil, L.S.2
  • 41
    • 0037193468 scopus 로고    scopus 로고
    • Dislocation and degradation from the ER are regulated by cytosolic stress
    • VanSlyke, J. K., and Musil, L. S. (2002). Dislocation and degradation from the ER are regulated by cytosolic stress. J. Cell Biol. 157, 381-394.
    • (2002) J. Cell Biol. , vol.157 , pp. 381-394
    • VanSlyke, J.K.1    Musil, L.S.2


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