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Volumn 7, Issue 10, 2012, Pages

Restoration of Proper Trafficking to the Cell Surface for Membrane Proteins Harboring Cysteine Mutations

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; CYCLIC AMP; CYSTEINE; MEMBRANE PROTEIN; VOLTAGE GATED POTASSIUM CHANNEL;

EID: 84867638129     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0047693     Document Type: Article
Times cited : (7)

References (43)
  • 1
    • 0141668884 scopus 로고    scopus 로고
    • Achromatopsia-associated mutation in the human cone photoreceptor cyclic nucleotide-gated channel CNGB3 subunit alters the ligand sensitivity and pore properties of heteromeric channels
    • Peng C, Rich ED, Varnum MD, (2003) Achromatopsia-associated mutation in the human cone photoreceptor cyclic nucleotide-gated channel CNGB3 subunit alters the ligand sensitivity and pore properties of heteromeric channels. J Biol Chem 278: 34533-34540.
    • (2003) J Biol Chem , vol.278 , pp. 34533-34540
    • Peng, C.1    Rich, E.D.2    Varnum, M.D.3
  • 2
    • 2442713977 scopus 로고    scopus 로고
    • The Arg451Cys-neuroligin-3 mutation associated with autism reveals a defect in protein processing
    • Comoletti D, De Jaco A, Jennings LL, Flynn RE, Gaietta G, et al. (2004) The Arg451Cys-neuroligin-3 mutation associated with autism reveals a defect in protein processing. J Neurosci 24: 4889-4893.
    • (2004) J Neurosci , vol.24 , pp. 4889-4893
    • Comoletti, D.1    de Jaco, A.2    Jennings, L.L.3    Flynn, R.E.4    Gaietta, G.5
  • 3
    • 42549108564 scopus 로고    scopus 로고
    • Functional analysis of human CNGA3 mutations associated with colour blindness suggests impaired surface expression of channel mutants A3(R427C) and A3(R563C)
    • Koeppen K, Reuter P, Kohl S, Baumann B, Ladewig T, et al. (2008) Functional analysis of human CNGA3 mutations associated with colour blindness suggests impaired surface expression of channel mutants A3(R427C) and A3(R563C). Eur J Neurosci 27: 2391-2401.
    • (2008) Eur J Neurosci , vol.27 , pp. 2391-2401
    • Koeppen, K.1    Reuter, P.2    Kohl, S.3    Baumann, B.4    Ladewig, T.5
  • 4
    • 21144442266 scopus 로고    scopus 로고
    • Functional consequences of progressive cone dystrophy-associated mutations in the human cone photoreceptor cyclic nucleotide-gated channel CNGA3 subunit
    • Liu C, Varnum MD, (2005) Functional consequences of progressive cone dystrophy-associated mutations in the human cone photoreceptor cyclic nucleotide-gated channel CNGA3 subunit. Am J Physiol Cell Physiol 289: C187-198.
    • (2005) Am J Physiol Cell Physiol , vol.289
    • Liu, C.1    Varnum, M.D.2
  • 5
    • 42449114511 scopus 로고    scopus 로고
    • Mannosidase I inhibition rescues the human alpha-sarcoglycan R77C recurrent mutation
    • Bartoli M, Gicquel E, Barrault L, Soheili T, Malissen M, et al. (2008) Mannosidase I inhibition rescues the human alpha-sarcoglycan R77C recurrent mutation. Hum Mol Genet 17: 1214-1221.
    • (2008) Hum Mol Genet , vol.17 , pp. 1214-1221
    • Bartoli, M.1    Gicquel, E.2    Barrault, L.3    Soheili, T.4    Malissen, M.5
  • 6
    • 55349114752 scopus 로고    scopus 로고
    • Mutations in CNGA3 impair trafficking or function of cone cyclic nucleotide-gated channels, resulting in achromatopsia
    • Reuter P, Koeppen K, Ladewig T, Kohl S, Baumann B, et al. (2008) Mutations in CNGA3 impair trafficking or function of cone cyclic nucleotide-gated channels, resulting in achromatopsia. Hum Mutat 29: 1228-1236.
    • (2008) Hum Mutat , vol.29 , pp. 1228-1236
    • Reuter, P.1    Koeppen, K.2    Ladewig, T.3    Kohl, S.4    Baumann, B.5
  • 7
    • 0033510368 scopus 로고    scopus 로고
    • The red blood cell band 3 variant (band 3Biceetrel:R490C) associated with dominant hereditary spherocytosis causes defective membrane targeting of the molecule and a dominant negative effect
    • Dhermy D, Burnier O, Bourgeois M, Grandchamp B, (1999) The red blood cell band 3 variant (band 3Biceetrel:R490C) associated with dominant hereditary spherocytosis causes defective membrane targeting of the molecule and a dominant negative effect. Mol Membr Biol 16: 305-312.
    • (1999) Mol Membr Biol , vol.16 , pp. 305-312
    • Dhermy, D.1    Burnier, O.2    Bourgeois, M.3    Grandchamp, B.4
  • 8
    • 33748075893 scopus 로고    scopus 로고
    • The human NBCe1-A mutant R881C, associated with proximal renal tubular acidosis, retains function but is mistargeted in polarized renal epithelia
    • Toye AM, Parker MD, Daly CM, Lu J, Virkki LV, et al. (2006) The human NBCe1-A mutant R881C, associated with proximal renal tubular acidosis, retains function but is mistargeted in polarized renal epithelia. Am J Physiol Cell Physiol 291: C788-801.
    • (2006) Am J Physiol Cell Physiol , vol.291
    • Toye, A.M.1    Parker, M.D.2    Daly, C.M.3    Lu, J.4    Virkki, L.V.5
  • 9
    • 1842740905 scopus 로고    scopus 로고
    • A novel missense mutation in AE1 causing autosomal dominant distal renal tubular acidosis retains normal transport function but is mistargeted in polarized epithelial cells
    • Rungroj N, Devonald MA, Cuthbert AW, Reimann F, Akkarapatumwong V, et al. (2004) A novel missense mutation in AE1 causing autosomal dominant distal renal tubular acidosis retains normal transport function but is mistargeted in polarized epithelial cells. J Biol Chem 279: 13833-13838.
    • (2004) J Biol Chem , vol.279 , pp. 13833-13838
    • Rungroj, N.1    Devonald, M.A.2    Cuthbert, A.W.3    Reimann, F.4    Akkarapatumwong, V.5
  • 10
    • 0034822311 scopus 로고    scopus 로고
    • CNGA3 mutations in hereditary cone photoreceptor disorders
    • Wissinger B, Gamer D, Jagle H, Giorda R, Marx T, et al. (2001) CNGA3 mutations in hereditary cone photoreceptor disorders. Am J Hum Genet 69: 722-737.
    • (2001) Am J Hum Genet , vol.69 , pp. 722-737
    • Wissinger, B.1    Gamer, D.2    Jagle, H.3    Giorda, R.4    Marx, T.5
  • 11
    • 23244464493 scopus 로고    scopus 로고
    • Transmembrane S1 mutations in CNGA3 from achromatopsia 2 patients cause loss of function and impaired cellular trafficking of the cone CNG channel
    • Patel KA, Bartoli KM, Fandino RA, Ngatchou AN, Woch G, et al. (2005) Transmembrane S1 mutations in CNGA3 from achromatopsia 2 patients cause loss of function and impaired cellular trafficking of the cone CNG channel. Invest Ophthalmol Vis Sci 46: 2282-2290.
    • (2005) Invest Ophthalmol Vis Sci , vol.46 , pp. 2282-2290
    • Patel, K.A.1    Bartoli, K.M.2    Fandino, R.A.3    Ngatchou, A.N.4    Woch, G.5
  • 12
    • 2542485279 scopus 로고    scopus 로고
    • Cellular processing of cone photoreceptor cyclic GMP-gated ion channels: a role for the S4 structural motif
    • Faillace MP, Bernabeu RO, Korenbrot JI, (2004) Cellular processing of cone photoreceptor cyclic GMP-gated ion channels: a role for the S4 structural motif. J Biol Chem 279: 22643-22653.
    • (2004) J Biol Chem , vol.279 , pp. 22643-22653
    • Faillace, M.P.1    Bernabeu, R.O.2    Korenbrot, J.I.3
  • 13
    • 0029998701 scopus 로고    scopus 로고
    • Structure and function of cyclic nucleotide-gated channels
    • Zagotta WN, Siegelbaum SA, (1996) Structure and function of cyclic nucleotide-gated channels. Annu Rev Neurosci 19: 235-263.
    • (1996) Annu Rev Neurosci , vol.19 , pp. 235-263
    • Zagotta, W.N.1    Siegelbaum, S.A.2
  • 14
    • 0036301043 scopus 로고    scopus 로고
    • Cyclic nucleotide-gated ion channels
    • Kaupp UB, Seifert R, (2002) Cyclic nucleotide-gated ion channels. Physiol Rev 82: 769-824.
    • (2002) Physiol Rev , vol.82 , pp. 769-824
    • Kaupp, U.B.1    Seifert, R.2
  • 15
    • 0024154942 scopus 로고
    • Molecular basis of visual excitation
    • Stryer L, (1988) Molecular basis of visual excitation. Cold Spring Harb Symp Quant Biol 53 Pt 1: 283-294.
    • (1988) Cold Spring Harb Symp Quant Biol , vol.53 , Issue.Pt 1 , pp. 283-294
    • Stryer, L.1
  • 16
    • 2342548656 scopus 로고    scopus 로고
    • Subunit configuration of heteromeric cone cyclic nucleotide-gated channels
    • Peng C, Rich ED, Varnum MD, (2004) Subunit configuration of heteromeric cone cyclic nucleotide-gated channels. Neuron 42: 401-410.
    • (2004) Neuron , vol.42 , pp. 401-410
    • Peng, C.1    Rich, E.D.2    Varnum, M.D.3
  • 17
    • 0037078979 scopus 로고    scopus 로고
    • The heteromeric cyclic nucleotide-gated channel adopts a 3A: 1B stoichiometry
    • Zhong H, Molday LL, Molday RS, Yau KW, (2002) The heteromeric cyclic nucleotide-gated channel adopts a 3A: 1B stoichiometry. Nature 420: 193-198.
    • (2002) Nature , vol.420 , pp. 193-198
    • Zhong, H.1    Molday, L.L.2    Molday, R.S.3    Yau, K.W.4
  • 18
    • 2342554303 scopus 로고    scopus 로고
    • Stoichiometry and assembly of olfactory cyclic nucleotide-gated channels
    • Zheng J, Zagotta WN, (2004) Stoichiometry and assembly of olfactory cyclic nucleotide-gated channels. Neuron 42: 411-421.
    • (2004) Neuron , vol.42 , pp. 411-421
    • Zheng, J.1    Zagotta, W.N.2
  • 19
    • 0037028016 scopus 로고    scopus 로고
    • Rod cyclic nucleotide-gated channels have a stoichiometry of three CNGA1 subunits and one CNGB1 subunit
    • Zheng J, Trudeau MC, Zagotta WN, (2002) Rod cyclic nucleotide-gated channels have a stoichiometry of three CNGA1 subunits and one CNGB1 subunit. Neuron 36: 891-896.
    • (2002) Neuron , vol.36 , pp. 891-896
    • Zheng, J.1    Trudeau, M.C.2    Zagotta, W.N.3
  • 20
    • 0037028014 scopus 로고    scopus 로고
    • Subunit stoichiometry of the CNG channel of rod photoreceptors
    • Weitz D, Ficek N, Kremmer E, Bauer PJ, Kaupp UB, (2002) Subunit stoichiometry of the CNG channel of rod photoreceptors. Neuron 36: 881-889.
    • (2002) Neuron , vol.36 , pp. 881-889
    • Weitz, D.1    Ficek, N.2    Kremmer, E.3    Bauer, P.J.4    Kaupp, U.B.5
  • 21
    • 0034050157 scopus 로고    scopus 로고
    • Coexpression of alpha and beta subunits of the rod cyclic GMP-gated channel restores native sensitivity to cyclic AMP: role of D604/N1201
    • Pages F, Ildefonse M, Ragno M, Crouzy S, Bennett N, (2000) Coexpression of alpha and beta subunits of the rod cyclic GMP-gated channel restores native sensitivity to cyclic AMP: role of D604/N1201. Biophys J 78: 1227-1239.
    • (2000) Biophys J , vol.78 , pp. 1227-1239
    • Pages, F.1    Ildefonse, M.2    Ragno, M.3    Crouzy, S.4    Bennett, N.5
  • 22
    • 0027193853 scopus 로고
    • Rod and cone photoreceptor cells express distinct genes for cGMP-gated channels
    • Bonigk W, Altenhofen W, Muller F, Dose A, Illing M, et al. (1993) Rod and cone photoreceptor cells express distinct genes for cGMP-gated channels. Neuron 10: 865-877.
    • (1993) Neuron , vol.10 , pp. 865-877
    • Bonigk, W.1    Altenhofen, W.2    Muller, F.3    Dose, A.4    Illing, M.5
  • 23
    • 0025073835 scopus 로고
    • Primary structure and functional expression of a cyclic nucleotide-activated channel from olfactory neurons
    • Dhallan RS, Yau KW, Schrader KA, Reed RR, (1990) Primary structure and functional expression of a cyclic nucleotide-activated channel from olfactory neurons. Nature 347: 184-187.
    • (1990) Nature , vol.347 , pp. 184-187
    • Dhallan, R.S.1    Yau, K.W.2    Schrader, K.A.3    Reed, R.R.4
  • 24
    • 0024805680 scopus 로고
    • Primary structure and functional expression from complementary DNA of the rod photoreceptor cyclic GMP-gated channel
    • Kaupp UB, Niidome T, Tanabe T, Terada S, Bonigk W, et al. (1989) Primary structure and functional expression from complementary DNA of the rod photoreceptor cyclic GMP-gated channel. Nature 342: 762-766.
    • (1989) Nature , vol.342 , pp. 762-766
    • Kaupp, U.B.1    Niidome, T.2    Tanabe, T.3    Terada, S.4    Bonigk, W.5
  • 25
    • 0034977038 scopus 로고    scopus 로고
    • Conformational changes in S6 coupled to the opening of cyclic nucleotide-gated channels
    • Flynn GE, Zagotta WN, (2001) Conformational changes in S6 coupled to the opening of cyclic nucleotide-gated channels. Neuron 30: 689-698.
    • (2001) Neuron , vol.30 , pp. 689-698
    • Flynn, G.E.1    Zagotta, W.N.2
  • 26
    • 0029860763 scopus 로고    scopus 로고
    • On the use of thiol-modifying agents to determine channel topology
    • Holmgren M, Liu Y, Xu Y, Yellen G, (1996) On the use of thiol-modifying agents to determine channel topology. Neuropharmacology 35: 797-804.
    • (1996) Neuropharmacology , vol.35 , pp. 797-804
    • Holmgren, M.1    Liu, Y.2    Xu, Y.3    Yellen, G.4
  • 28
    • 0033213381 scopus 로고    scopus 로고
    • Molecular rearrangements in the ligand-binding domain of cyclic nucleotide-gated channels
    • Matulef K, Flynn GE, Zagotta WN, (1999) Molecular rearrangements in the ligand-binding domain of cyclic nucleotide-gated channels. Neuron 24: 443-452.
    • (1999) Neuron , vol.24 , pp. 443-452
    • Matulef, K.1    Flynn, G.E.2    Zagotta, W.N.3
  • 29
    • 23244456428 scopus 로고    scopus 로고
    • Crystal structure of a mammalian voltage-dependent Shaker family K+ channel
    • Long SB, Campbell EB, Mackinnon R, (2005) Crystal structure of a mammalian voltage-dependent Shaker family K+ channel. Science 309: 897-903.
    • (2005) Science , vol.309 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    Mackinnon, R.3
  • 30
    • 0030175348 scopus 로고    scopus 로고
    • Contribution of the S4 segment to gating charge in the Shaker K+ channel
    • Aggarwal SK, MacKinnon R, (1996) Contribution of the S4 segment to gating charge in the Shaker K+ channel. Neuron 16: 1169-1177.
    • (1996) Neuron , vol.16 , pp. 1169-1177
    • Aggarwal, S.K.1    MacKinnon, R.2
  • 31
    • 0023225798 scopus 로고
    • Cloning of genomic and complementary DNA from Shaker, a putative potassium channel gene from Drosophila
    • Papazian DM, Schwarz TL, Tempel BL, Jan YN, Jan LY, (1987) Cloning of genomic and complementary DNA from Shaker, a putative potassium channel gene from Drosophila. Science 237: 749-753.
    • (1987) Science , vol.237 , pp. 749-753
    • Papazian, D.M.1    Schwarz, T.L.2    Tempel, B.L.3    Jan, Y.N.4    Jan, L.Y.5
  • 32
    • 0030175867 scopus 로고    scopus 로고
    • Voltage-sensing residues in the S2 and S4 segments of the Shaker K+ channel
    • Seoh SA, Sigg D, Papazian DM, Bezanilla F, (1996) Voltage-sensing residues in the S2 and S4 segments of the Shaker K+ channel. Neuron 16: 1159-1167.
    • (1996) Neuron , vol.16 , pp. 1159-1167
    • Seoh, S.A.1    Sigg, D.2    Papazian, D.M.3    Bezanilla, F.4
  • 33
    • 0028998041 scopus 로고
    • Electrostatic interactions of S4 voltage sensor in Shaker K+ channel
    • Papazian DM, Shao XM, Seoh SA, Mock AF, Huang Y, et al. (1995) Electrostatic interactions of S4 voltage sensor in Shaker K+ channel. Neuron 14: 1293-1301.
    • (1995) Neuron , vol.14 , pp. 1293-1301
    • Papazian, D.M.1    Shao, X.M.2    Seoh, S.A.3    Mock, A.F.4    Huang, Y.5
  • 34
    • 0141884309 scopus 로고    scopus 로고
    • The birth of a channel
    • Deutsch C, (2003) The birth of a channel. Neuron 40: 265-276.
    • (2003) Neuron , vol.40 , pp. 265-276
    • Deutsch, C.1
  • 35
    • 0037167878 scopus 로고    scopus 로고
    • Voltage-sensing mechanism is conserved among ion channels gated by opposite voltages
    • Mannikko R, Elinder F, Larsson HP, (2002) Voltage-sensing mechanism is conserved among ion channels gated by opposite voltages. Nature 419: 837-841.
    • (2002) Nature , vol.419 , pp. 837-841
    • Mannikko, R.1    Elinder, F.2    Larsson, H.P.3
  • 36
    • 0037131381 scopus 로고    scopus 로고
    • The gate of the influenza virus M2 proton channel is formed by a single tryptophan residue
    • Tang Y, Zaitseva F, Lamb RA, Pinto LH, (2002) The gate of the influenza virus M2 proton channel is formed by a single tryptophan residue. J Biol Chem 277: 39880-39886.
    • (2002) J Biol Chem , vol.277 , pp. 39880-39886
    • Tang, Y.1    Zaitseva, F.2    Lamb, R.A.3    Pinto, L.H.4
  • 37
    • 0033615646 scopus 로고    scopus 로고
    • Correction of defective protein trafficking of a mutant HERG potassium channel in human long QT syndrome. Pharmacological and temperature effects
    • Zhou Z, Gong Q, January CT, (1999) Correction of defective protein trafficking of a mutant HERG potassium channel in human long QT syndrome. Pharmacological and temperature effects. J Biol Chem 274: 31123-31126.
    • (1999) J Biol Chem , vol.274 , pp. 31123-31126
    • Zhou, Z.1    Gong, Q.2    January, C.T.3
  • 38
    • 33845240108 scopus 로고    scopus 로고
    • Chemical chaperones and permissive temperatures alter localization of Gaucher disease associated glucocerebrosidase variants
    • Sawkar AR, Schmitz M, Zimmer KP, Reczek D, Edmunds T, et al. (2006) Chemical chaperones and permissive temperatures alter localization of Gaucher disease associated glucocerebrosidase variants. ACS Chem Biol 1: 235-251.
    • (2006) ACS Chem Biol , vol.1 , pp. 235-251
    • Sawkar, A.R.1    Schmitz, M.2    Zimmer, K.P.3    Reczek, D.4    Edmunds, T.5
  • 39
    • 85047683541 scopus 로고    scopus 로고
    • Chemical chaperones: a pharmacological strategy for disorders of protein folding and trafficking
    • Perlmutter DH, (2002) Chemical chaperones: a pharmacological strategy for disorders of protein folding and trafficking. Pediatr Res 52: 832-836.
    • (2002) Pediatr Res , vol.52 , pp. 832-836
    • Perlmutter, D.H.1
  • 40
    • 34748914170 scopus 로고    scopus 로고
    • Pharmacologic chaperoning as a strategy to treat Gaucher disease
    • Yu Z, Sawkar AR, Kelly JW, (2007) Pharmacologic chaperoning as a strategy to treat Gaucher disease. FEBS J 274: 4944-4950.
    • (2007) FEBS J , vol.274 , pp. 4944-4950
    • Yu, Z.1    Sawkar, A.R.2    Kelly, J.W.3
  • 41
    • 67650732710 scopus 로고    scopus 로고
    • Lipid-dependent membrane protein topogenesis
    • Dowhan W, Bogdanov M, (2009) Lipid-dependent membrane protein topogenesis. Annu Rev Biochem 78: 515-540.
    • (2009) Annu Rev Biochem , vol.78 , pp. 515-540
    • Dowhan, W.1    Bogdanov, M.2
  • 42
    • 0030791975 scopus 로고    scopus 로고
    • Anionic phospholipids are determinants of membrane protein topology
    • van Klompenburg W, Nilsson I, von Heijne G, de Kruijff B, (1997) Anionic phospholipids are determinants of membrane protein topology. EMBO J 16: 4261-4266.
    • (1997) EMBO J , vol.16 , pp. 4261-4266
    • van Klompenburg, W.1    Nilsson, I.2    von Heijne, G.3    de Kruijff, B.4
  • 43
    • 84555189151 scopus 로고    scopus 로고
    • Defective trafficking of cone photoreceptor CNG channels induces the unfolded protein response and ER-stress-associated cell death
    • Duricka DL, Brown RL, Varnum MD, (2012) Defective trafficking of cone photoreceptor CNG channels induces the unfolded protein response and ER-stress-associated cell death. Biochem J 441: 685-696.
    • (2012) Biochem J , vol.441 , pp. 685-696
    • Duricka, D.L.1    Brown, R.L.2    Varnum, M.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.