메뉴 건너뛰기




Volumn 288, Issue 28, 2013, Pages 20427-20434

A connexin50 mutant, CX50fs, that causes cataracts is unstable, but is rescued by a proteasomal inhibitor

Author keywords

[No Author keywords available]

Indexed keywords

ACCELERATED DEGRADATION; CONGENITAL CATARACT; FUNCTIONAL BEHAVIORS; GAP JUNCTION PLAQUES; INTERCELLULAR COMMUNICATIONS; PROTEASE INHIBITION; PROTEIN DEGRADATION; WILD-TYPE PROTEINS;

EID: 84880059878     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.452847     Document Type: Article
Times cited : (20)

References (51)
  • 1
    • 17344390158 scopus 로고    scopus 로고
    • Plasma membrane channels formed by connexins: Their regulation and functions
    • Sáez, J. C., Berthoud, V. M., Braňes, M. C., Martínez, A. D., and Beyer, E. C. (2003) Plasma membrane channels formed by connexins: their regulation and functions. Physiol. Rev. 83, 1359-1400 (Pubitemid 37222275)
    • (2003) Physiological Reviews , vol.83 , Issue.4 , pp. 1359-1400
    • Saez, J.C.1    Berthoud, V.M.2    Branes, M.C.3    Martinez, A.D.4    Beyer, E.C.5
  • 3
    • 33645002735 scopus 로고    scopus 로고
    • Life cycle of connexins in health and disease
    • Laird, D. W. (2006) Life cycle of connexins in health and disease. Biochem. J. 394, 527-543
    • (2006) Biochem. J. , vol.394 , pp. 527-543
    • Laird, D.W.1
  • 4
    • 39149086399 scopus 로고    scopus 로고
    • Congenital cataracts and their molecular genetics
    • Hejtmancik, J. F. (2008) Congenital cataracts and their molecular genetics. Semin. Cell Dev. Biol. 19, 134-149
    • (2008) Semin. Cell Dev. Biol. , vol.19 , pp. 134-149
    • Hejtmancik, J.F.1
  • 6
    • 77954954398 scopus 로고    scopus 로고
    • Paradigm of genetic mosaicism and lone atrial fibrillation: Physiological characterization of a connexin 43-deletion mutant identified from atrial tissue
    • Thibodeau, I. L., Xu, J., Li, Q., Liu, G., Lam, K., Veinot, J. P., Birnie, D. H., Jones, D. L., Krahn, A. D., Lemery, R., Nicholson, B. J., and Gollob, M. H. (2010) Paradigm of genetic mosaicism and lone atrial fibrillation: physiological characterization of a connexin 43-deletion mutant identified from atrial tissue. Circulation 122, 236-244
    • (2010) Circulation , vol.122 , pp. 236-244
    • Thibodeau, I.L.1    Xu, J.2    Li, Q.3    Liu, G.4    Lam, K.5    Veinot, J.P.6    Birnie, D.H.7    Jones, D.L.8    Krahn, A.D.9    Lemery, R.10    Nicholson, B.J.11    Gollob, M.H.12
  • 7
    • 84861625594 scopus 로고    scopus 로고
    • Gap junctions in inherited human disorders of the central nervous system
    • Abrams, C. K., and Scherer, S. S. (2012) Gap junctions in inherited human disorders of the central nervous system. Biochim. Biophys. Acta 1818, 2030-2047
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 2030-2047
    • Abrams, C.K.1    Scherer, S.S.2
  • 9
    • 80051677021 scopus 로고    scopus 로고
    • Key functions for gap junctions in skin and hearing
    • Scott, C. A., and Kelsell, D. P. (2011) Key functions for gap junctions in skin and hearing. Biochem. J. 438, 245-254
    • (2011) Biochem. J. , vol.438 , pp. 245-254
    • Scott, C.A.1    Kelsell, D.P.2
  • 13
    • 28844450617 scopus 로고    scopus 로고
    • An aberrant sequence in a connexin46 mutant underlies congenital cataracts
    • DOI 10.1074/jbc.M504765200
    • Minogue, P. J., Liu, X., Ebihara, L., Beyer, E. C., and Berthoud, V. M. (2005) An aberrant sequence in a connexin46 mutant underlies congenital cataracts. J. Biol. Chem. 280, 40788-40795 (Pubitemid 41780570)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.49 , pp. 40788-40795
    • Minogue, P.J.1    Liu, X.2    Ebihara, L.3    Beyer, E.C.4    Berthoud, V.M.5
  • 14
    • 38349054558 scopus 로고    scopus 로고
    • The cataract-inducing S50P mutation in Cx50 dominantly alters the channel gating of wild-type lens connexins
    • DeRosa, A. M., Xia, C. H., Gong, X., and White, T. W. (2007) The cataract-inducing S50P mutation in Cx50 dominantly alters the channel gating of wild-type lens connexins. J. Cell Sci. 120, 4107-4116
    • (2007) J. Cell Sci. , vol.120 , pp. 4107-4116
    • DeRosa, A.M.1    Xia, C.H.2    Gong, X.3    White, T.W.4
  • 15
    • 61549139397 scopus 로고    scopus 로고
    • The cytoplasmic accumulations of the cataract-associated mutant, Connexin50P88S, are long-lived and form in the endoplasmic reticulum
    • Lichtenstein, A., Gaietta, G. M., Deerinck, T. J., Crum, J., Sosinsky, G. E., Beyer, E. C., and Berthoud, V. M. (2009) The cytoplasmic accumulations of the cataract-associated mutant, Connexin50P88S, are long-lived and form in the endoplasmic reticulum. Exp. Eye Res. 88, 600-609
    • (2009) Exp. Eye Res. , vol.88 , pp. 600-609
    • Lichtenstein, A.1    Gaietta, G.M.2    Deerinck, T.J.3    Crum, J.4    Sosinsky, G.E.5    Beyer, E.C.6    Berthoud, V.M.7
  • 17
    • 79955557177 scopus 로고    scopus 로고
    • Different consequences of cataract-associated mutations at adjacent positions in the first extracellular boundary of connexin50
    • Tong, J. J., Minogue, P. J., Guo, W., Chen, T. L., Beyer, E. C., Berthoud, V. M., and Ebihara, L. (2011) Different consequences of cataract-associated mutations at adjacent positions in the first extracellular boundary of connexin50. Am. J. Physiol. Cell Physiol. 300, C1055-C1064
    • (2011) Am. J. Physiol. Cell Physiol. , vol.300
    • Tong, J.J.1    Minogue, P.J.2    Guo, W.3    Chen, T.L.4    Beyer, E.C.5    Berthoud, V.M.6    Ebihara, L.7
  • 18
    • 43949140835 scopus 로고    scopus 로고
    • A novel GJA8 mutation causing a recessive triangular cataract
    • Schmidt, W., Klopp, N., Illig, T., and Graw, J. (2008) A novel GJA8 mutation causing recessive triangular cataract. Mol. Vis. 14, 851-856 (Pubitemid 351699496)
    • (2008) Molecular Vision , vol.14 , pp. 851-856
    • Schmidt, W.1    Klopp, N.2    Illig, T.3    Graw, J.4
  • 19
    • 43149099696 scopus 로고    scopus 로고
    • Inhibition of p97-dependent protein degradation by eeyarestatin I
    • Wang, Q., Li, L., and Ye, Y. (2008) Inhibition of p97-dependent protein degradation by eeyarestatin I. J. Biol. Chem. 283, 7445-7454
    • (2008) J. Biol. Chem. , vol.283 , pp. 7445-7454
    • Wang, Q.1    Li, L.2    Ye, Y.3
  • 20
    • 84856474838 scopus 로고    scopus 로고
    • Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system
    • Meyer, H., Bug, M., and Bremer, S. (2012) Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system. Nat. Cell Biol. 14, 117-123
    • (2012) Nat. Cell Biol. , vol.14 , pp. 117-123
    • Meyer, H.1    Bug, M.2    Bremer, S.3
  • 22
    • 82655189989 scopus 로고    scopus 로고
    • Cx50 requires an intact PDZ-binding motif and ZO-1 for the formation of functional intercellular channels
    • Chai, Z., Goodenough, D. A., and Paul, D. L. (2011) Cx50 requires an intact PDZ-binding motif and ZO-1 for the formation of functional intercellular channels. Mol. Biol. Cell 22, 4503-4512
    • (2011) Mol. Biol. Cell , vol.22 , pp. 4503-4512
    • Chai, Z.1    Goodenough, D.A.2    Paul, D.L.3
  • 24
    • 0036126655 scopus 로고    scopus 로고
    • pH gating of lens fibre connexins
    • Eckert R. (2002) pH gating of lens fibre connexins. Pflügers Archiv. 443, 843-851
    • (2002) Pflügers Archiv. , vol.443 , pp. 843-851
    • Eckert, R.1
  • 25
    • 0037087452 scopus 로고    scopus 로고
    • Functional role of the carboxyl terminal domain of human connexin 50 in gap junctional channels
    • DOI 10.1007/s00232-001-0139-5
    • Xu, X., Berthoud, V. M., Beyer, E. C., and Ebihara, L. (2002) Functional role of the carboxyl terminal domain of human connexin 50 in gap junctional channels. J. Membr. Biol. 186, 101-112 (Pubitemid 34252646)
    • (2002) Journal of Membrane Biology , vol.186 , Issue.2 , pp. 101-112
    • Xu, X.1    Berthoud, V.M.2    Beyer, E.C.3    Ebihara, L.4
  • 26
    • 0031664396 scopus 로고    scopus 로고
    • Spatial differences in gap junction gating in the lens are a consequence of connexin cleavage
    • Lin, J. S., Eckert, R., Kistler, J., and Donaldson, P. (1998) Spatial differences in gap junction gating in the lens are a consequence of connexin cleavage. Eur. J. Cell Biol. 76, 246-250 (Pubitemid 28431572)
    • (1998) European Journal of Cell Biology , vol.76 , Issue.4 , pp. 246-250
    • Lin, J.S.1    Eckert, R.2    Kistler, J.3    Donaldson, P.4
  • 27
    • 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 (Pubitemid 30408055)
    • (2000) Molecular Biology of the Cell , vol.11 , Issue.6 , pp. 1933-1946
    • VanSlyke, J.K.1    Deschenes, S.M.2    Musil, L.S.3
  • 28
    • 84858146420 scopus 로고    scopus 로고
    • Non-canonical ubiq-uitin- based signals for proteasomal degradation
    • Kravtsova-Ivantsiv, Y., and Ciechanover, A. (2012) Non-canonical ubiq-uitin- based signals for proteasomal degradation. J. Cell Sci. 125, 539-548
    • (2012) J. Cell Sci. , vol.125 , pp. 539-548
    • Kravtsova-Ivantsiv, Y.1    Ciechanover, A.2
  • 29
    • 48449100846 scopus 로고    scopus 로고
    • Lens fiber connexin turnover and caspase-3-mediated cleavage are regulated alternately by phosphorylation
    • Yin, X., Liu, J., and Jiang, J. X. (2008) Lens fiber connexin turnover and caspase-3-mediated cleavage are regulated alternately by phosphorylation. Cell Commun. Adhes. 15, 1-11
    • (2008) Cell Commun. Adhes. , vol.15 , pp. 1-11
    • Yin, X.1    Liu, J.2    Jiang, J.X.3
  • 30
    • 79952792541 scopus 로고    scopus 로고
    • Autophagy: A pathway that contributes to connexin degradation
    • Lichtenstein, A., Minogue, P. J., Beyer, E. C., and Berthoud, V. M. (2011) Autophagy: a pathway that contributes to connexin degradation. J. Cell Sci. 124, 910-920
    • (2011) J. Cell Sci. , vol.124 , pp. 910-920
    • Lichtenstein, A.1    Minogue, P.J.2    Beyer, E.C.3    Berthoud, V.M.4
  • 31
    • 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
  • 32
    • 0037473023 scopus 로고    scopus 로고
    • Phosphorylation of connexin 43 acts as a stimuli for proteasome-dependent degradation of the protein in lens epithelial cells
    • Girǎo, H., and Pereira, P. (2003) Phosphorylation of connexin 43 acts as a stimulus for proteasome-dependent degradation of the protein in lens epithelial cells. Mol. Vis. 9, 24-30 (Pubitemid 38097563)
    • (2003) Molecular Vision , vol.9 , pp. 24-30
    • Girao, H.1    Pereira, P.2
  • 33
    • 0037672616 scopus 로고    scopus 로고
    • A tyrosine-based sorting signal is involved in connexin43 stability and gap junction turnover
    • DOI 10.1242/jcs.00440
    • Thomas, M. A., Zosso, N., Scerri, I., Demaurex, N., Chanson, M., and Staub, O. (2003) A tyrosine-based sorting signal is involved in connexin43 stability and gap junction turnover. J. Cell Sci. 116, 2213-2222 (Pubitemid 36722368)
    • (2003) Journal of Cell Science , vol.116 , Issue.11 , pp. 2213-2222
    • Thomas, M.A.1    Zosso, N.2    Scerri, I.3    Demaurex, N.4    Chanson, M.5    Staub, O.6
  • 34
    • 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
    • DOI 10.1074/jbc.M300614200
    • 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 (Pubitemid 36962390)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.32 , pp. 30005-30014
    • Qin, H.1    Shao, Q.2    Igdoura, S.A.3    Alaoui-Jamali, M.A.4    Laird, D.W.5
  • 35
    • 84856067520 scopus 로고    scopus 로고
    • Activation of Akt, not connexin 43 protein ubiquitination, regulates gap junction stability
    • Dunn, C. A., Su, V., Lau, A. F., and Lampe, P. D. (2012) Activation of Akt, not connexin 43 protein ubiquitination, regulates gap junction stability. J. Biol. Chem. 287, 2600-2607
    • (2012) J. Biol. Chem. , vol.287 , pp. 2600-2607
    • Dunn, C.A.1    Su, V.2    Lau, A.F.3    Lampe, P.D.4
  • 36
    • 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
  • 37
    • 0031281674 scopus 로고    scopus 로고
    • Degradation of connexin43 gap junctions involves both the proteasome and the lysosome
    • DOI 10.1006/excr.1997.3747
    • 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 (Pubitemid 27505601)
    • (1997) Experimental Cell Research , vol.236 , Issue.2 , pp. 482-492
    • Laing, J.G.1    Tadros, P.N.2    Westphale, E.M.3    Beyer, E.C.4
  • 39
    • 0032103769 scopus 로고    scopus 로고
    • Proteolysis of connexin43-containing gap junctions in normal and heat-stressed cardiac myocytes
    • Laing, J. G., Tadros, P. N., Green, K., Saffitz, J. E., and Beyer, E. C. (1998) Proteolysis of connexin43-containing gap junctions in normal and heat-stressed cardiac myocytes. Cardiovasc. Res. 38, 711-718
    • (1998) Cardiovasc. Res. , vol.38 , pp. 711-718
    • Laing, J.G.1    Tadros, P.N.2    Green, K.3    Saffitz, J.E.4    Beyer, E.C.5
  • 40
    • 0030881029 scopus 로고    scopus 로고
    • Activity of ubiquitin-dependent pathway in response to oxidative stress: Ubiquitin-activating enzyme is transiently up-regulated
    • DOI 10.1074/jbc.272.37.23086
    • Shang, F., Gong, X., and Taylor, A. (1997) Activity of ubiquitin-dependent pathway in response to oxidative stress: ubiquitin-activating enzyme is transiently up-regulated. J. Biol. Chem. 272, 23086-23093 (Pubitemid 27392436)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.37 , pp. 23086-23093
    • Shang, F.1    Gong, X.2    Taylor, A.3
  • 41
    • 0037402905 scopus 로고    scopus 로고
    • Lens fibers have a fully functional ubiquitin-proteasome pathway
    • DOI 10.1016/S0014-4835(03)00020-4
    • Pereira, P., Shang, F., Hobbs, M., Girão, H., and Taylor, A. (2003) Lens fibers have a fully functional ubiquitin-proteasome pathway. Exp. Eye Res. 76, 623-631 (Pubitemid 36411937)
    • (2003) Experimental Eye Research , vol.76 , Issue.5 , pp. 623-631
    • Pereira, P.1    Shang, F.2    Hobbs, M.3    Girao, H.4    Taylor, A.5
  • 42
    • 0032476578 scopus 로고    scopus 로고
    • Targeted ablation of connexin50 in mice results in microphthalmia and zonular pulverulent cataracts
    • DOI 10.1083/jcb.143.3.815
    • White, T. W., Goodenough, D. A., and Paul D. L. (1998) Targeted ablation of connexin50 in mice results in microphthalmia and zonular pulverulent cataracts. J. Cell Biol. 143, 815-825 (Pubitemid 28512573)
    • (1998) Journal of Cell Biology , vol.143 , Issue.3 , pp. 815-825
    • White, T.W.1    Goodenough, D.A.2    Paul, D.L.3
  • 43
    • 0036023359 scopus 로고    scopus 로고
    • Disruption of Gja8 (α8 connexin) in mice leads to microphthalmia associated with retardation of lens growth and lens fiber maturation
    • Rong, P., Wang, X., Niesman, I., Wu, Y., Benedetti, L. E., Dunia, I., Levy, E., and Gong, X. (2002) Disruption of Gja8 (α8 connexin) in mice leads to microphthalmia associated with retardation of lens growth and lens fiber maturation. Development 129, 167-174 (Pubitemid 34863785)
    • (2002) Development , vol.129 , Issue.1 , pp. 167-174
    • Pong, P.1    Wang, X.2    Niesman, I.3    Wu, Y.4    Benedetti, L.E.5    Dunia, I.6    Levy, E.7    Gong, X.8
  • 45
  • 48
    • 84871352589 scopus 로고    scopus 로고
    • Rescue of murine F508del CFTR activity in native intestine by low temperature and proteasome inhibitors
    • Wilke, M., Bot, A., Jorna, H., Scholte, B. J., and de Jonge, H. R. (2012) Rescue of murine F508del CFTR activity in native intestine by low temperature and proteasome inhibitors. PLoS One 7, e52070
    • (2012) PLoS One , vol.7
    • Wilke, M.1    Bot, A.2    Jorna, H.3    Scholte, B.J.4    De Jonge, H.R.5
  • 49
    • 79960208716 scopus 로고    scopus 로고
    • Novel proteasome inhibitors to overcome bortezomib resistance
    • Ruschak, A. M., Slassi, M., Kay, L. E., and Schimmer, A. D. (2011) Novel proteasome inhibitors to overcome bortezomib resistance. J. Natl. Cancer Inst. 103, 1007-1017
    • (2011) J. Natl. Cancer Inst. , vol.103 , pp. 1007-1017
    • Ruschak, A.M.1    Slassi, M.2    Kay, L.E.3    Schimmer, A.D.4
  • 50
    • 84885422353 scopus 로고    scopus 로고
    • Non-covalent proteasome inhibitors
    • Kaffy, J., Bernadat, G., and Ongeri, S. (2013) Non-covalent proteasome inhibitors. Curr. Pharm. Des. 19, 4115-4130
    • (2013) Curr. Pharm. Des. , vol.19 , pp. 4115-4130
    • Kaffy, J.1    Bernadat, G.2    Ongeri, S.3
  • 51
    • 0035800832 scopus 로고    scopus 로고
    • Defining a link between gap junction communication, proteolysis, and cataract formation
    • Baruch, A., Greenbaum, D., Levy, E. T., Nielsen, P. A., Gilula, N. B., Kumar, N. M., and Bogyo, M. (2001) Defining a link between gap junction communication, proteolysis, and cataract formation. J. Biol. Chem. 276, 28999-29006
    • (2001) J. Biol. Chem. , vol.276 , pp. 28999-29006
    • Baruch, A.1    Greenbaum, D.2    Levy, E.T.3    Nielsen, P.A.4    Gilula, N.B.5    Kumar, N.M.6    Bogyo, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.