메뉴 건너뛰기




Volumn 287, Issue 13, 2012, Pages 10482-10493

Role of Derlin-1 protein in proteostasis regulation of ATP-sensitive potassium channels

Author keywords

[No Author keywords available]

Indexed keywords

CHANNEL PROTEINS; CYTOSOLIC; ENDOPLASMIC RETICULUM; EXPRESSION LEVELS; GLUCOSE METABOLISM; GLUCOSE-STIMULATED INSULIN SECRETIONS; IN-CHANNELS; INSULIN SECRETION; MEMBRANE POTENTIALS; OVER-EXPRESSION; PATHOLOGICAL CHANGES; POTASSIUM CHANNELS; PROTEASOMES; RETROTRANSLOCATION; RNA INTERFERENCE; SULFONYLUREA RECEPTORS; SURFACE CHANNEL; SURFACE EXPRESSION;

EID: 84858979919     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.312223     Document Type: Article
Times cited : (21)

References (53)
  • 1
    • 0032788372 scopus 로고    scopus 로고
    • Molecular biology of adenosine triphosphate-sensitive potassium channels
    • Aguilar-Bryan, L., and Bryan, J. (1999) Molecular biology of adenosine triphosphate-sensitive potassium channels. Endocr. Rev. 20, 101-135
    • (1999) Endocr. Rev. , vol.20 , pp. 101-135
    • Aguilar-Bryan, L.1    Bryan, J.2
  • 2
    • 23644442552 scopus 로고    scopus 로고
    • ATP-sensitive potassium channelopathies. Focus on insulin secretion
    • Ashcroft, F. M. (2005) ATP-sensitive potassium channelopathies. Focus on insulin secretion. J. Clin. Invest. 115, 2047-2058
    • (2005) J. Clin. Invest. , vol.115 , pp. 2047-2058
    • Ashcroft, F.M.1
  • 3
    • 33645322386 scopus 로고    scopus 로고
    • ATP channels as molecular sensors of cellular metabolism
    • ATP channels as molecular sensors of cellular metabolism. Nature 440, 470-476
    • (2006) Nature , vol.440 , pp. 470-476
    • Nichols, C.G.1
  • 4
    • 0035956875 scopus 로고    scopus 로고
    • ATP channels caused by a sulfonylurea receptor 1 mutation associated with persistent hyperinsulinemic hypoglycemia of infancy
    • ATP channels caused by a sulfonylurea receptor 1 mutation associated with persistent hyperinsulinemic hypoglycemia of infancy. Proc. Natl. Acad. Sci. U.S.A. 98, 2882-2887
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 2882-2887
    • Cartier, E.A.1    Conti, L.R.2    Vandenberg, C.A.3    Shyng, S.L.4
  • 6
    • 1642565240 scopus 로고    scopus 로고
    • Sulfonylureas correct trafficking defects of ATP-sensitive potassium channels caused by mutations in the sulfonylurea receptor
    • Yan, F., Lin, C. W., Weisiger, E., Cartier, E. A., Taschenberger, G., and Shyng, S. L. (2004) Sulfonylureas correct trafficking defects of ATP-sensitive potassium channels caused by mutations in the sulfonylurea receptor. J. Biol. Chem. 279, 11096-11105
    • (2004) J. Biol. Chem. , vol.279 , pp. 11096-11105
    • Yan, F.1    Lin, C.W.2    Weisiger, E.3    Cartier, E.A.4    Taschenberger, G.5    Shyng, S.L.6
  • 7
    • 34548384002 scopus 로고    scopus 로고
    • Congenital hyperinsulinism associated ABCC8 mutations that cause defective trafficking of ATP-sensitive K+ channels. Identification and rescue
    • Yan, F. F., Lin, Y. W., MacMullen, C., Ganguly, A., Stanley, C. A., and Shyng, S. L. (2007) Congenital hyperinsulinism associated ABCC8 mutations that cause defective trafficking of ATP-sensitive K+ channels. Identification and rescue. Diabetes 56, 2339-2348
    • (2007) Diabetes , vol.56 , pp. 2339-2348
    • Yan, F.F.1    Lin, Y.W.2    MacMullen, C.3    Ganguly, A.4    Stanley, C.A.5    Shyng, S.L.6
  • 8
    • 0036833473 scopus 로고    scopus 로고
    • Advances in diagnosis and treatment of hyperinsulinism in infants and children
    • Stanley, C. A. (2002) Advances in diagnosis and treatment of hyperinsulinism in infants and children. J. Clin. Endocrinol. Metab. 87, 4857-4859
    • (2002) J. Clin. Endocrinol. Metab. , vol.87 , pp. 4857-4859
    • Stanley, C.A.1
  • 16
    • 0036702298 scopus 로고    scopus 로고
    • ER-associated degradation in protein quality control and cellular regulation
    • Hampton, R. Y. (2002) ER-associated degradation in protein quality control and cellular regulation. Curr. Opin Cell Biol. 14, 476-482
    • (2002) Curr. Opin Cell Biol. , vol.14 , pp. 476-482
    • Hampton, R.Y.1
  • 18
    • 21044431965 scopus 로고    scopus 로고
    • Roles of molecular chaperones in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD)
    • Nishikawa, S., Brodsky, J. L., and Nakatsukasa, K. (2005) Roles of molecular chaperones in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD). J. Biochem. 137, 551-555
    • (2005) J. Biochem. , vol.137 , pp. 551-555
    • Nishikawa, S.1    Brodsky, J.L.2    Nakatsukasa, K.3
  • 19
    • 33746228127 scopus 로고    scopus 로고
    • Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins
    • Carvalho, P., Goder, V., and Rapoport, T. A. (2006) Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins. Cell 126, 361-373
    • (2006) Cell , vol.126 , pp. 361-373
    • Carvalho, P.1    Goder, V.2    Rapoport, T.A.3
  • 20
    • 75649114551 scopus 로고    scopus 로고
    • Mechanism and components of endoplasmic reticulum-associated degradation
    • Hoseki, J., Ushioda, R., and Nagata, K. (2010) Mechanism and components of endoplasmic reticulum-associated degradation. J. Biochem. 147, 19-25
    • (2010) J. Biochem. , vol.147 , pp. 19-25
    • Hoseki, J.1    Ushioda, R.2    Nagata, K.3
  • 21
    • 37649025515 scopus 로고    scopus 로고
    • Dissecting the ER-associated degradation of a misfolded polytopic membrane protein
    • Nakatsukasa, K., Huyer, G., Michaelis, S., and Brodsky, J. L. (2008) Dissecting the ER-associated degradation of a misfolded polytopic membrane protein. Cell 132, 101-112
    • (2008) Cell , vol.132 , pp. 101-112
    • Nakatsukasa, K.1    Huyer, G.2    Michaelis, S.3    Brodsky, J.L.4
  • 22
    • 3042677637 scopus 로고    scopus 로고
    • A membrane protein complex mediates retrotranslocation from the ER lumen into the cytosol
    • Ye, Y., Shibata, Y., Yun, C., Ron, D., and Rapoport, T. A. (2004) A membrane protein complex mediates retrotranslocation from the ER lumen into the cytosol. Nature 429, 841-847
    • (2004) Nature , vol.429 , pp. 841-847
    • Ye, Y.1    Shibata, Y.2    Yun, C.3    Ron, D.4    Rapoport, T.A.5
  • 23
    • 3042616595 scopus 로고    scopus 로고
    • A membrane protein required for dislocation of misfolded proteins from the ER
    • Lilley, B. N., and Ploegh, H. L. (2004) A membrane protein required for dislocation of misfolded proteins from the ER. Nature 429, 834-840
    • (2004) Nature , vol.429 , pp. 834-840
    • Lilley, B.N.1    Ploegh, H.L.2
  • 24
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • Ye, Y., Meyer, H. H., and Rapoport, T. A. (2001) The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature 414, 652-656
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 25
    • 44049091178 scopus 로고    scopus 로고
    • Role of S3 and S4 transmembrane domain charged amino acids in channel biogenesis and gating of KCa2.3 and KCa3.1
    • Gao, Y., Chotoo, C. K., Balut, C. M., Sun, F., Bailey, M. A., and Devor, D. C. (2008) Role of S3 and S4 transmembrane domain charged amino acids in channel biogenesis and gating of KCa2.3 and KCa3.1. J. Biol. Chem. 283, 9049-9059
    • (2008) J. Biol. Chem. , vol.283 , pp. 9049-9059
    • Gao, Y.1    Chotoo, C.K.2    Balut, C.M.3    Sun, F.4    Bailey, M.A.5    Devor, D.C.6
  • 26
    • 33846008398 scopus 로고    scopus 로고
    • Derlin-1 promotes the efficient degradation of the cystic fibrosis transmembrane conductance regulator (CFTR) and CFTR folding mutants
    • Sun, F., Zhang, R., Gong, X., Geng, X., Drain, P. F., and Frizzell, R. A. (2006) Derlin-1 promotes the efficient degradation of the cystic fibrosis transmembrane conductance regulator (CFTR) and CFTR folding mutants. J. Biol. Chem. 281, 36856-36863
    • (2006) J. Biol. Chem. , vol.281 , pp. 36856-36863
    • Sun, F.1    Zhang, R.2    Gong, X.3    Geng, X.4    Drain, P.F.5    Frizzell, R.A.6
  • 27
    • 33746675669 scopus 로고    scopus 로고
    • Sequential quality control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator
    • Younger, J. M., Chen, L., Ren, H. Y., Rosser, M. F., Turnbull, E. L., Fan, C. Y., Patterson, C., and Cyr, D. M. (2006) Sequential quality control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator. Cell 126, 571-582
    • (2006) Cell , vol.126 , pp. 571-582
    • Younger, J.M.1    Chen, L.2    Ren, H.Y.3    Rosser, M.F.4    Turnbull, E.L.5    Fan, C.Y.6    Patterson, C.7    Cyr, D.M.8
  • 29
    • 64149122748 scopus 로고    scopus 로고
    • LQT1-associated mutations increase KCNQ1 proteasomal degradation independently of Derlin-1
    • Peroz, D., Dahimène, S., Baró, I., Loussouarn, G., and Mérot, J. (2009) LQT1-associated mutations increase KCNQ1 proteasomal degradation independently of Derlin-1. J. Biol. Chem. 284, 5250-5256
    • (2009) J. Biol. Chem. , vol.284 , pp. 5250-5256
    • Peroz, D.1    Dahimène, S.2    Baró, I.3    Loussouarn, G.4    Mérot, J.5
  • 30
    • 26844459794 scopus 로고    scopus 로고
    • Role of ubiquitin-proteasome degradation pathway in biogenesis efficiency of β-cell ATP-sensitive potassium channels
    • Yan, F. F., Lin, C. W., Cartier, E. A., and Shyng, S. L. (2005) Role of ubiquitin-proteasome degradation pathway in biogenesis efficiency of β-cell ATP-sensitive potassium channels. Am. J. Physiol. 289, C1351-C1359
    • (2005) Am. J. Physiol. , vol.289
    • Yan, F.F.1    Lin, C.W.2    Cartier, E.A.3    Shyng, S.L.4
  • 32
    • 33847672778 scopus 로고    scopus 로고
    • Optimized expression vector for ion channel studies in Xenopus oocytes and mammalian cells using alfalfa mosaic virus
    • Venkatachalan, S. P., Bushman, J. D., Mercado, J. L., Sancar, F., Christopherson, K. R., and Boileau, A. J. (2007) Optimized expression vector for ion channel studies in Xenopus oocytes and mammalian cells using alfalfa mosaic virus. Pflugers Arch. 454, 155-163
    • (2007) Pflugers Arch. , vol.454 , pp. 155-163
    • Venkatachalan, S.P.1    Bushman, J.D.2    Mercado, J.L.3    Sancar, F.4    Christopherson, K.R.5    Boileau, A.J.6
  • 33
    • 25844434827 scopus 로고    scopus 로고
    • Membrane phosphoinositides control insulin secretion through their effects on ATP-sensitive K+ channel activity
    • Lin, C. W., Yan, F., Shimamura, S., Barg, S., and Shyng, S. L. (2005) Membrane phosphoinositides control insulin secretion through their effects on ATP-sensitive K+ channel activity. Diabetes 54, 2852-2858
    • (2005) Diabetes , vol.54 , pp. 2852-2858
    • Lin, C.W.1    Yan, F.2    Shimamura, S.3    Barg, S.4    Shyng, S.L.5
  • 34
    • 77953507086 scopus 로고    scopus 로고
    • Role of Hsp90 in biogenesis of the β-cell ATP-sensitive potassium channel complex
    • Yan, F. F., Pratt, E. B., Chen, P. C., Wang, F., Skach, W. R., David, L. L., and Shyng, S. L. (2010) Role of Hsp90 in biogenesis of the β-cell ATP-sensitive potassium channel complex. Mol. Biol. Cell 21, 1945-1954
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1945-1954
    • Yan, F.F.1    Pratt, E.B.2    Chen, P.C.3    Wang, F.4    Skach, W.R.5    David, L.L.6    Shyng, S.L.7
  • 35
    • 79952129862 scopus 로고    scopus 로고
    • Syntaxin 1A regulates surface expression of beta-cell ATP-sensitive potassium channels
    • Chen, P. C., Bruederle, C. E., Gaisano, H. Y., and Shyng, S. L. (2011) Syntaxin 1A regulates surface expression of beta-cell ATP-sensitive potassium channels. Am. J. Physiol. 300, C506-C516
    • (2011) Am. J. Physiol. , vol.300
    • Chen, P.C.1    Bruederle, C.E.2    Gaisano, H.Y.3    Shyng, S.L.4
  • 37
    • 0038487228 scopus 로고    scopus 로고
    • Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol. Dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains
    • Ye, Y., Meyer, H. H., and Rapoport, T. A. (2003) Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol. Dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. J. Cell Biol. 162, 71-84
    • (2003) J. Cell Biol. , vol.162 , pp. 71-84
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 38
    • 36249022750 scopus 로고    scopus 로고
    • Characterization of an ERAD pathway for nonglycosylated BiP substrates, which require Herp
    • Okuda-Shimizu, Y., and Hendershot, L. M. (2007) Characterization of an ERAD pathway for nonglycosylated BiP substrates, which require Herp. Mol. Cell 28, 544-554
    • (2007) Mol. Cell , vol.28 , pp. 544-554
    • Okuda-Shimizu, Y.1    Hendershot, L.M.2
  • 39
    • 31944450850 scopus 로고    scopus 로고
    • Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation
    • Oda, Y., Okada, T., Yoshida, H., Kaufman, R. J., Nagata, K., and Mori, K. (2006) Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation. J. Cell Biol. 172, 383-393
    • (2006) J. Cell Biol. , vol.172 , pp. 383-393
    • Oda, Y.1    Okada, T.2    Yoshida, H.3    Kaufman, R.J.4    Nagata, K.5    Mori, K.6
  • 40
    • 33746253687 scopus 로고    scopus 로고
    • Have you HRD? Understanding ERAD is DOAble!
    • Ismail, N., and Ng, D. T. (2006) Have you HRD? Understanding ERAD is DOAble! Cell 126, 237-239
    • (2006) Cell , vol.126 , pp. 237-239
    • Ismail, N.1    Ng, D.T.2
  • 41
    • 64749087257 scopus 로고    scopus 로고
    • Misfolded membrane proteins are specifically recognized by the transmembrane domain of the Hrd1p ubiquitin ligase
    • Sato, B. K., Schulz, D., Do, P. H., and Hampton, R. Y. (2009) Misfolded membrane proteins are specifically recognized by the transmembrane domain of the Hrd1p ubiquitin ligase. Mol. Cell 34, 212-222
    • (2009) Mol. Cell , vol.34 , pp. 212-222
    • Sato, B.K.1    Schulz, D.2    Do, P.H.3    Hampton, R.Y.4
  • 42
    • 2442451126 scopus 로고    scopus 로고
    • Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control
    • Vashist, S., and Ng, D. T. (2004) Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control. J. Cell Biol. 165, 41-52
    • (2004) J. Cell Biol. , vol.165 , pp. 41-52
    • Vashist, S.1    Ng, D.T.2
  • 43
    • 0035798623 scopus 로고    scopus 로고
    • Transmembrane topology of the sulfonylurea receptor SUR1
    • Conti, L. R., Radeke, C. M., Shyng, S. L., and Vandenberg, C. A. (2001) Transmembrane topology of the sulfonylurea receptor SUR1. J. Biol. Chem. 276, 41270-41278
    • (2001) J. Biol. Chem. , vol.276 , pp. 41270-41278
    • Conti, L.R.1    Radeke, C.M.2    Shyng, S.L.3    Vandenberg, C.A.4
  • 44
    • 79953133519 scopus 로고    scopus 로고
    • Conserved intramolecular disulfide bond is critical to trafficking and fate of ATP-binding cassette (ABC) transporters ABCB6 and sulfonylurea receptor 1 (SUR1)/ABCC8
    • Fukuda, Y., Aguilar-Bryan, L., Vaxillaire, M., Dechaume, A., Wang, Y., Dean, M., Moitra, K., Bryan, J., and Schuetz, J. D. (2011) Conserved intramolecular disulfide bond is critical to trafficking and fate of ATP-binding cassette (ABC) transporters ABCB6 and sulfonylurea receptor 1 (SUR1)/ABCC8. J. Biol. Chem. 286, 8481-8492
    • (2011) J. Biol. Chem. , vol.286 , pp. 8481-8492
    • Fukuda, Y.1    Aguilar-Bryan, L.2    Vaxillaire, M.3    Dechaume, A.4    Wang, Y.5    Dean, M.6    Moitra, K.7    Bryan, J.8    Schuetz, J.D.9
  • 45
    • 44049086392 scopus 로고    scopus 로고
    • Destabilization of ATP-sensitive potassium channel activity by novel KCNJ11 mutations identified in congenital hyperinsulinism
    • Lin, Y. W., Bushman, J. D., Yan, F. F., Haidar, S., MacMullen, C., Ganguly, A., Stanley, C. A., and Shyng, S. L. (2008) Destabilization of ATP-sensitive potassium channel activity by novel KCNJ11 mutations identified in congenital hyperinsulinism. J. Biol. Chem. 283, 9146-9156
    • (2008) J. Biol. Chem. , vol.283 , pp. 9146-9156
    • Lin, Y.W.1    Bushman, J.D.2    Yan, F.F.3    Haidar, S.4    MacMullen, C.5    Ganguly, A.6    Stanley, C.A.7    Shyng, S.L.8
  • 47
    • 40849147267 scopus 로고    scopus 로고
    • Derlin-1 and p97/valosin-containing protein mediate the endoplasmic reticulum-associated degradation of human V2 vasopressin receptors
    • Schwieger, I., Lautz, K., Krause, E., Rosenthal, W., Wiesner, B., and Hermosilla, R. (2008) Derlin-1 and p97/valosin-containing protein mediate the endoplasmic reticulum-associated degradation of human V2 vasopressin receptors. Mol. Pharmacol. 73, 697-708
    • (2008) Mol. Pharmacol. , vol.73 , pp. 697-708
    • Schwieger, I.1    Lautz, K.2    Krause, E.3    Rosenthal, W.4    Wiesner, B.5    Hermosilla, R.6
  • 48
    • 0142180199 scopus 로고    scopus 로고
    • Sur domains that associate with and gate KATP pores define a novel gatekeeper
    • Babenko, A. P., and Bryan, J. (2003) Sur domains that associate with and gate KATP pores define a novel gatekeeper. J. Biol. Chem. 278, 41577-41580
    • (2003) J. Biol. Chem. , vol.278 , pp. 41577-41580
    • Babenko, A.P.1    Bryan, J.2
  • 49
    • 0042025073 scopus 로고    scopus 로고
    • N-terminal transmembrane domain of the SUR controls trafficking and gating of Kir6 channel subunits
    • Chan, K. W., Zhang, H., and Logothetis, D. E. (2003) N-terminal transmembrane domain of the SUR controls trafficking and gating of Kir6 channel subunits. EMBO J. 22, 3833-3843
    • (2003) EMBO J. , vol.22 , pp. 3833-3843
    • Chan, K.W.1    Zhang, H.2    Logothetis, D.E.3
  • 51
    • 44849118218 scopus 로고    scopus 로고
    • Derlin-1 is overexpressed in human breast carcinoma and protects cancer cells from endoplasmic reticulum stress-induced apoptosis
    • Wang, J., Hua, H., Ran, Y., Zhang, H., Liu, W., Yang, Z., and Jiang, Y. (2008) Derlin-1 is overexpressed in human breast carcinoma and protects cancer cells from endoplasmic reticulum stress-induced apoptosis. Breast Cancer Res. 10, R7
    • (2008) Breast Cancer Res. , vol.10
    • Wang, J.1    Hua, H.2    Ran, Y.3    Zhang, H.4    Liu, W.5    Yang, Z.6    Jiang, Y.7
  • 52
    • 34247326506 scopus 로고    scopus 로고
    • The oligomeric state of Derlin-1 is modulated by endoplasmic reticulum stress
    • Crawshaw, S. G., Cross, B. C., Wilson, C. M., and High, S. (2007) The oligomeric state of Derlin-1 is modulated by endoplasmic reticulum stress. Mol. Membr. Biol. 24, 113-120
    • (2007) Mol. Membr. Biol. , vol.24 , pp. 113-120
    • Crawshaw, S.G.1    Cross, B.C.2    Wilson, C.M.3    High, S.4
  • 53
    • 45449101527 scopus 로고    scopus 로고
    • TOPDOM. Database of domains and motifs with conservative location in transmembrane proteins
    • Tusnády, G. E., Kalmár, L., Hegyi, H., Tompa, P., and Simon, I. (2008) TOPDOM. Database of domains and motifs with conservative location in transmembrane proteins. Bioinformatics 24, 1469-1470
    • (2008) Bioinformatics , vol.24 , pp. 1469-1470
    • Tusnády, G.E.1    Kalmár, L.2    Hegyi, H.3    Tompa, P.4    Simon, I.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.