메뉴 건너뛰기




Volumn 290, Issue 20, 2015, Pages 12497-12503

Acetylation stimulates the epithelial sodium channel by reducing its ubiquitination and degradation

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLATION; AMINO ACIDS; BLOOD PRESSURE; CELL MEMBRANES; DUCTS;

EID: 84929377394     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.635540     Document Type: Article
Times cited : (26)

References (45)
  • 1
    • 4644268448 scopus 로고    scopus 로고
    • The epithelial sodium channel: From molecule to disease
    • Schild, L. (2004) The epithelial sodium channel: from molecule to disease. Rev. Physiol. Biochem. Pharmacol. 151, 93-107
    • (2004) Rev. Physiol. Biochem. Pharmacol. , vol.151 , pp. 93-107
    • Schild, L.1
  • 2
    • 27844476338 scopus 로고    scopus 로고
    • Minireview: Regulation of epithelial Na+ channel trafficking
    • Snyder, P. M. (2005) Minireview: regulation of epithelial Na+ channel trafficking. Endocrinology 146, 5079-5085
    • (2005) Endocrinology , vol.146 , pp. 5079-5085
    • Snyder, P.M.1
  • 3
    • 0030068024 scopus 로고    scopus 로고
    • Molecular genetics of human blood pressure variation
    • Lifton, R. P. (1996) Molecular genetics of human blood pressure variation. Science 272, 676-680
    • (1996) Science , vol.272 , pp. 676-680
    • Lifton, R.P.1
  • 4
    • 0023789980 scopus 로고
    • Evidence for reduced Cl+ and increased Na+ permeability in cystic fibrosis human primary cell cultures
    • Boucher, R. C., Cotton, C. U., Gatzy, J. T., Knowles, M. R., and Yankaskas, J. R. (1988) Evidence for reduced Cl+ and increased Na+ permeability in cystic fibrosis human primary cell cultures. J. Physiol. 405, 77-103
    • (1988) J. Physiol. , vol.405 , pp. 77-103
    • Boucher, R.C.1    Cotton, C.U.2    Gatzy, J.T.3    Knowles, M.R.4    Yankaskas, J.R.5
  • 5
    • 0029591506 scopus 로고
    • Mechanism by which Liddle's syndrome mutations increase activity of a human epithelial Na+ channel
    • Snyder, P. M., Price, M. P., McDonald, F. J., Adams, C. M., Volk, K. A., Zeiher, B. G., Stokes, J. B., and Welsh, M. J. (1995) Mechanism by which Liddle's syndrome mutations increase activity of a human epithelial Na+ channel. Cell 83, 969-978
    • (1995) Cell , vol.83 , pp. 969-978
    • Snyder, P.M.1    Price, M.P.2    McDonald, F.J.3    Adams, C.M.4    Volk, K.A.5    Zeiher, B.G.6    Stokes, J.B.7    Welsh, M.J.8
  • 6
    • 0032491407 scopus 로고    scopus 로고
    • Inhibition of the epithelial Na+ channel by interaction of Nedd4 with a PY motif deleted in Liddle's syndrome
    • Goulet, C. C., Volk, K. A., Adams, C. M., Prince, L. S., Stokes, J. B., and Snyder, P. M. (1998) Inhibition of the epithelial Na+ channel by interaction of Nedd4 with a PY motif deleted in Liddle's syndrome. J. Biol. Chem. 273, 30012-30017
    • (1998) J. Biol. Chem. , vol.273 , pp. 30012-30017
    • Goulet, C.C.1    Volk, K.A.2    Adams, C.M.3    Prince, L.S.4    Stokes, J.B.5    Snyder, P.M.6
  • 7
    • 0029874436 scopus 로고    scopus 로고
    • WW domains of Nedd4 bind to the proline-rich PY motifs in the epithelial Na+ channel deleted in Liddle's syndrome
    • Staub, O., Dho, S., Henry, P., Correa, J., Ishikawa, T., McGlade, J., and Rotin, D. (1996) WW domains of Nedd4 bind to the proline-rich PY motifs in the epithelial Na+ channel deleted in Liddle's syndrome. EMBO J. 15, 2371-2380
    • (1996) EMBO J , vol.15 , pp. 2371-2380
    • Staub, O.1    Dho, S.2    Henry, P.3    Correa, J.4    Ishikawa, T.5    McGlade, J.6    Rotin, D.7
  • 8
    • 34547107368 scopus 로고    scopus 로고
    • Nedd4-2 catalyzes ubiquitination and degradation of cell surface ENaC
    • Zhou, R., Patel, S. V., and Snyder, P. M. (2007) Nedd4-2 catalyzes ubiquitination and degradation of cell surface ENaC. J. Biol. Chem. 282, 20207-20212
    • (2007) J. Biol. Chem. , vol.282 , pp. 20207-20212
    • Zhou, R.1    Patel, S.V.2    Snyder, P.M.3
  • 9
    • 44449161555 scopus 로고    scopus 로고
    • Nedd4-2 induces endocytosis and degradation of proteolytically cleaved epithelial Na+ channels
    • Kabra, R., Knight, K. K., Zhou, R., and Snyder, P. M. (2008) Nedd4-2 induces endocytosis and degradation of proteolytically cleaved epithelial Na+ channels. J. Biol. Chem. 283, 6033-6039
    • (2008) J. Biol. Chem. , vol.283 , pp. 6033-6039
    • Kabra, R.1    Knight, K.K.2    Zhou, R.3    Snyder, P.M.4
  • 10
    • 34547830212 scopus 로고    scopus 로고
    • The PY motif of ENaC, mutated in Liddle syndrome, regulates channel internalization, sorting and mobilization from subapical pool
    • Lu, C., Pribanic, S., Debonneville, A., Jiang, C., and Rotin, D. (2007) The PY motif of ENaC, mutated in Liddle syndrome, regulates channel internalization, sorting and mobilization from subapical pool. Traffic 8, 1246-1264
    • (2007) Traffic , vol.8 , pp. 1246-1264
    • Lu, C.1    Pribanic, S.2    Debonneville, A.3    Jiang, C.4    Rotin, D.5
  • 11
  • 12
    • 84874289201 scopus 로고    scopus 로고
    • Ubiquitin-specific peptidase 8 (USP8) regulates endosomal trafficking of the epithelial Na+ channel
    • Zhou, R., Tomkovicz, V. R., Butler, P. L., Ochoa, L. A., Peterson, Z. J., and Snyder, P. M. (2013) Ubiquitin-specific peptidase 8 (USP8) regulates endosomal trafficking of the epithelial Na+ channel. J. Biol. Chem. 288, 5389-5397
    • (2013) J. Biol. Chem. , vol.288 , pp. 5389-5397
    • Zhou, R.1    Tomkovicz, V.R.2    Butler, P.L.3    Ochoa, L.A.4    Peterson, Z.J.5    Snyder, P.M.6
  • 13
    • 77949461455 scopus 로고    scopus 로고
    • The endoplasmic reticulum-associated degradation of the epithelial sodium channel requires a unique complement of molecular chaperones
    • Buck, T. M., Kolb, A. R., Boyd, C. R., Kleyman, T. R., and Brodsky, J. L. (2010) The endoplasmic reticulum-associated degradation of the epithelial sodium channel requires a unique complement of molecular chaperones. Mol. Biol. Cell 21, 1047-1058
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1047-1058
    • Buck, T.M.1    Kolb, A.R.2    Boyd, C.R.3    Kleyman, T.R.4    Brodsky, J.L.5
  • 15
    • 0030731428 scopus 로고    scopus 로고
    • Regulation of stability and function of the epithelial Na+ channel (ENaC) by ubiquitination
    • Staub, O., Gautschi, I., Ishikawa, T., Breitschopf, K., Ciechanover, A., Schild, L., and Rotin, D. (1997) Regulation of stability and function of the epithelial Na+ channel (ENaC) by ubiquitination.EMBOJ. 16, 6325-6336
    • (1997) EMBO J , vol.16 , pp. 6325-6336
    • Staub, O.1    Gautschi, I.2    Ishikawa, T.3    Breitschopf, K.4    Ciechanover, A.5    Schild, L.6    Rotin, D.7
  • 16
    • 78951476724 scopus 로고    scopus 로고
    • Intracellular ubiquitylation of the epithelial Na+ channel controls extracellular proteolytic channel activation via conformational change
    • Ruffieux-Daidié, D., and Staub, O. (2011) Intracellular ubiquitylation of the epithelial Na+ channel controls extracellular proteolytic channel activation via conformational change. J. Biol. Chem. 286, 2416-2424
    • (2011) J. Biol. Chem. , vol.286 , pp. 2416-2424
    • Ruffieux-Daidié, D.1    Staub, O.2
  • 17
    • 0034654011 scopus 로고    scopus 로고
    • Acetylation: A regulatory modification to rival phosphorylation?
    • Kouzarides, T. (2000) Acetylation: a regulatory modification to rival phosphorylation? EMBO J. 19, 1176-1179
    • (2000) EMBO J , vol.19 , pp. 1176-1179
    • Kouzarides, T.1
  • 18
    • 38649092744 scopus 로고    scopus 로고
    • Regulation of protein turnover by acetyltransferases and deacetylases
    • Sadoul, K., Boyault, C., Pabion, M., and Khochbin, S. (2008) Regulation of protein turnover by acetyltransferases and deacetylases. Biochimie 90, 306-312
    • (2008) Biochimie , vol.90 , pp. 306-312
    • Sadoul, K.1    Boyault, C.2    Pabion, M.3    Khochbin, S.4
  • 19
    • 0037184969 scopus 로고    scopus 로고
    • Acetylation of p53 inhibits its ubiquitination by Mdm2
    • Li, M., Luo, J., Brooks, C. L., and Gu, W. (2002) Acetylation of p53 inhibits its ubiquitination by Mdm2. J. Biol. Chem. 277, 50607-50611
    • (2002) J. Biol. Chem. , vol.277 , pp. 50607-50611
    • Li, M.1    Luo, J.2    Brooks, C.L.3    Gu, W.4
  • 22
    • 0029005859 scopus 로고
    • Cloning and expression of the α- And β-subunits of the human epithelial sodium channel
    • McDonald, F. J., Price, M. P., Snyder, P. M., and Welsh, M. J. (1995) Cloning and expression of the α- and β-subunits of the human epithelial sodium channel. Am. J. Physiol. 268, C1157-C1163
    • (1995) Am. J. Physiol. , vol.268 , pp. C1157-C1163
    • McDonald, F.J.1    Price, M.P.2    Snyder, P.M.3    Welsh, M.J.4
  • 23
    • 0028278274 scopus 로고
    • Cloning, expression, and tissue distribution of a human amiloride-sensitive Na+ channel
    • McDonald, F. J., Snyder, P. M., McCray, P. B., Jr., and Welsh, M. J. (1994) Cloning, expression, and tissue distribution of a human amiloride-sensitive Na+ channel. Am. J. Physiol. 266, L728-L734
    • (1994) Am. J. Physiol. , vol.266 , pp. L728-L734
    • McDonald, F.J.1    Snyder, P.M.2    McCray, P.B.3    Welsh, M.J.4
  • 24
    • 0033964223 scopus 로고    scopus 로고
    • Isolation of a novel histone deacetylase reveals that class i and class II deacetylases promote SMRT-mediated repression
    • Kao, H. Y., Downes, M., Ordentlich, P., and Evans, R. M. (2000) Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression. Genes Dev. 14, 55-66
    • (2000) Genes Dev. , vol.14 , pp. 55-66
    • Kao, H.Y.1    Downes, M.2    Ordentlich, P.3    Evans, R.M.4
  • 26
    • 0028027308 scopus 로고
    • Ubiquitin-dependent c-Jun degradation in vivo is mediated by the δ domain
    • Treier, M., Staszewski, L. M., and Bohmann, D. (1994) Ubiquitin-dependent c-Jun degradation in vivo is mediated by the δ domain. Cell 78, 787-798
    • (1994) Cell , vol.78 , pp. 787-798
    • Treier, M.1    Staszewski, L.M.2    Bohmann, D.3
  • 31
    • 33644543413 scopus 로고    scopus 로고
    • Liddle's syndrome mutations increase Na+ transport through dual effects on epithelial Na+ channel surface expression and proteolytic cleavage
    • Knight, K. K., Olson, D. R., Zhou, R., and Snyder, P. M. (2006) Liddle's syndrome mutations increase Na+ transport through dual effects on epithelial Na+ channel surface expression and proteolytic cleavage. Proc. Natl. Acad. Sci. U.S.A. 103, 2805-2808
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 2805-2808
    • Knight, K.K.1    Olson, D.R.2    Zhou, R.3    Snyder, P.M.4
  • 32
    • 0027483065 scopus 로고
    • Epithelial sodium channel related to proteins involved in neurodegeneration
    • Canessa, C. M., Horisberger, J. D., and Rossier, B. C. (1993) Epithelial sodium channel related to proteins involved in neurodegeneration. Nature 361, 467-470
    • (1993) Nature , vol.361 , pp. 467-470
    • Canessa, C.M.1    Horisberger, J.D.2    Rossier, B.C.3
  • 33
    • 0033986427 scopus 로고    scopus 로고
    • Liddle's syndrome mutations disrupt cAMP-mediated translocation of the epithelial Na+ channel to the cell surface
    • Snyder, P. M. (2000) Liddle's syndrome mutations disrupt cAMP-mediated translocation of the epithelial Na+ channel to the cell surface. J. Clin. Invest. 105, 45-53
    • (2000) J. Clin. Invest. , vol.105 , pp. 45-53
    • Snyder, P.M.1
  • 34
    • 20844435326 scopus 로고    scopus 로고
    • Role of Nedd4-2 and polyubiquitination in epithelial sodium channel degradation in untransfected renal A6 cells expressing endogenous ENaC subunits
    • Malik, B., Yue, Q., Yue, G., Chen, X. J., Price, S. R., Mitch, W. E., and Eaton, D. C. (2005) Role of Nedd4-2 and polyubiquitination in epithelial sodium channel degradation in untransfected renal A6 cells expressing endogenous ENaC subunits. Am. J. Physiol. Renal Physiol. 289, F107-F116
    • (2005) Am. J. Physiol. Renal Physiol. , vol.289 , pp. F107-F116
    • Malik, B.1    Yue, Q.2    Yue, G.3    Chen, X.J.4    Price, S.R.5    Mitch, W.E.6    Eaton, D.C.7
  • 35
    • 0035161876 scopus 로고    scopus 로고
    • A novel mouse Nedd4 protein suppresses the activity of the epithelial Na+ channel
    • Kamynina, E., Debonneville, C., Bens, M., Vandewalle, A., and Staub, O. (2001) A novel mouse Nedd4 protein suppresses the activity of the epithelial Na+ channel. FASEB J. 15, 204-214
    • (2001) FASEB J , vol.15 , pp. 204-214
    • Kamynina, E.1    Debonneville, C.2    Bens, M.3    Vandewalle, A.4    Staub, O.5
  • 37
    • 77957266397 scopus 로고    scopus 로고
    • Hrs controls sorting of the epithelial Na+channel between endosomal degradation and recycling pathways
    • Zhou, R., Kabra, R., Olson, D. R., Piper, R. C., and Snyder, P. M. (2010) Hrs controls sorting of the epithelial Na+channel between endosomal degradation and recycling pathways. J. Biol. Chem. 285, 30523-30530
    • (2010) J. Biol. Chem. , vol.285 , pp. 30523-30530
    • Zhou, R.1    Kabra, R.2    Olson, D.R.3    Piper, R.C.4    Snyder, P.M.5
  • 38
    • 0033060575 scopus 로고    scopus 로고
    • Antisense oligonucleotides against the α-subunit of ENaC decrease lung epithelial cation-channel activity
    • Jain, L., Chen, X. J., Malik, B., Al-Khalili, O., and Eaton, D. C. (1999) Antisense oligonucleotides against the α-subunit of ENaC decrease lung epithelial cation-channel activity. Am. J. Physiol. 276, L1046-L1051
    • (1999) Am. J. Physiol. , vol.276 , pp. L1046-L1051
    • Jain, L.1    Chen, X.J.2    Malik, B.3    Al-Khalili, O.4    Eaton, D.C.5
  • 39
    • 0035009443 scopus 로고    scopus 로고
    • Expression of highly selective sodium channels in alveolar type II cells is determined by culture conditions
    • Jain, L., Chen, X. J., Ramosevac, S., Brown, L. A., and Eaton, D. C. (2001) Expression of highly selective sodium channels in alveolar type II cells is determined by culture conditions. Am. J. Physiol. Lung Cell. Mol. Physiol. 280, L646-L658
    • (2001) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.280 , pp. L646-L658
    • Jain, L.1    Chen, X.J.2    Ramosevac, S.3    Brown, L.A.4    Eaton, D.C.5
  • 40
    • 77955655256 scopus 로고    scopus 로고
    • Histone deacetylase 7 (HDAC7) regulates myocyte migration and differentiation
    • Gao, C., Liu, Y., Lam, M., and Kao, H. Y. (2010) Histone deacetylase 7 (HDAC7) regulates myocyte migration and differentiation. Biochim. Biophys. Acta 1803, 1186-1197
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 1186-1197
    • Gao, C.1    Liu, Y.2    Lam, M.3    Kao, H.Y.4
  • 42
    • 84873019253 scopus 로고    scopus 로고
    • HDAC7 inhibits osteoclastogenesis by reversing RANKL-triggered β-catenin switch
    • Jin, Z., Wei, W., Dechow, P. C., and Wan, Y. (2013) HDAC7 inhibits osteoclastogenesis by reversing RANKL-triggered β-catenin switch. Mol. Endocrinol. 27, 325-335
    • (2013) Mol. Endocrinol. , vol.27 , pp. 325-335
    • Jin, Z.1    Wei, W.2    Dechow, P.C.3    Wan, Y.4
  • 43
    • 79954993361 scopus 로고    scopus 로고
    • Histone deacetylase 7 regulates cell survival and TCR signaling in CD4/CD8 double-positive thymocytes
    • Kasler, H. G., Young, B. D., Mottet, D., Lim, H. W., Collins, A. M., Olson, E. N., and Verdin, E. (2011) Histone deacetylase 7 regulates cell survival and TCR signaling in CD4/CD8 double-positive thymocytes. J. Immunol. 186, 4782-4793
    • (2011) J. Immunol. , vol.186 , pp. 4782-4793
    • Kasler, H.G.1    Young, B.D.2    Mottet, D.3    Lim, H.W.4    Collins, A.M.5    Olson, E.N.6    Verdin, E.7
  • 45
    • 84868334619 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor (HDACi) suberoylanilide hydroxamic acid (SAHA)-mediated correction of α1-antitrypsin deficiency
    • Bouchecareilh, M., Hutt, D. M., Szajner, P., Flotte, T. R., and Balch, W. E. (2012) Histone deacetylase inhibitor (HDACi) suberoylanilide hydroxamic acid (SAHA)-mediated correction of α1-antitrypsin deficiency. J. Biol. Chem. 287, 38265-38278
    • (2012) J. Biol. Chem. , vol.287 , pp. 38265-38278
    • Bouchecareilh, M.1    Hutt, D.M.2    Szajner, P.3    Flotte, T.R.4    Balch, W.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.