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Volumn 279, Issue 15, 2012, Pages 2632-2644

N-glycosylation promotes the cell surface expression of Kv1.3 potassium channels

Author keywords

cell surface expression; monosaccharide supplementation; N glycosylation; potassium channel; trafficking

Indexed keywords

CELL MEMBRANE PROTEIN; CELL SURFACE PROTEIN; FUCOSE; GALACTOSE; GLUCOSE; GLYCAN; MANNOSE; N ACETYLGLUCOSAMINE; N ACETYLNEURAMINIC ACID; N GLYCAN; POTASSIUM CHANNEL KV1.3; SIALIC ACID; UNCLASSIFIED DRUG;

EID: 84863838923     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2012.08642.x     Document Type: Article
Times cited : (24)

References (49)
  • 1
    • 54049100752 scopus 로고    scopus 로고
    • Kv1.3 channels in postganglionic sympathetic neurons: Expression, function, and modulation
    • Doczi MA, Morielli AD, &, Damon DH, (2008) Kv1.3 channels in postganglionic sympathetic neurons: expression, function, and modulation. Am J Physiol Regul Integr Comp Physiol 295, R733-R740.
    • (2008) Am J Physiol Regul Integr Comp Physiol , vol.295
    • Doczi, M.A.1    Morielli, A.D.2    Damon, D.H.3
  • 3
    • 0036185291 scopus 로고    scopus 로고
    • Recombinant Kv13. potassium channels stabilize tonic firing of cultured rat hippocampal neurons
    • Kupper J, Prinz AA, &, Fromherz P, (2002) Recombinant Kv13. potassium channels stabilize tonic firing of cultured rat hippocampal neurons. Pflügers Arch 443, 541-547.
    • (2002) Pflügers Arch , vol.443 , pp. 541-547
    • Kupper, J.1    Prinz, A.A.2    Fromherz, P.3
  • 8
    • 27544454783 scopus 로고    scopus 로고
    • Design of PAP-1, a selective small molecule Kv1.3 blocker, for the suppression of effector memory T cells in autoimmune diseases
    • Schmitz A, Sankaranarayanan A, Azam P, Schmidt-Lassen K, Homerick D, Hansel W, &, Wulff H, (2005) Design of PAP-1, a selective small molecule Kv1.3 blocker, for the suppression of effector memory T cells in autoimmune diseases. Mol Pharmacol 68, 1254-1270.
    • (2005) Mol Pharmacol , vol.68 , pp. 1254-1270
    • Schmitz, A.1    Sankaranarayanan, A.2    Azam, P.3    Schmidt-Lassen, K.4    Homerick, D.5    Hansel, W.6    Wulff, H.7
  • 10
    • 34447130413 scopus 로고    scopus 로고
    • Reduced Kv1.3 potassium channel expression in human prostate cancer
    • Abdul M, &, Hoosein N, (2006) Reduced Kv1.3 potassium channel expression in human prostate cancer. J Membr Biol 214, 99-102.
    • (2006) J Membr Biol , vol.214 , pp. 99-102
    • Abdul, M.1    Hoosein, N.2
  • 11
    • 70349564255 scopus 로고    scopus 로고
    • + channel subunit as a potential diagnostic marker and therapeutic target for breast cancer
    • + channel subunit as a potential diagnostic marker and therapeutic target for breast cancer. Biochem Mol Biol Rep 42, 535-539.
    • (2009) Biochem Mol Biol Rep , vol.42 , pp. 535-539
    • Jang, S.H.1    Kang, K.S.2    Ryu, P.D.3    Lee, S.Y.4
  • 14
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
    • Apweiler R, Hermjakob H, &, Sharon N, (1999) On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim Biophys Acta 1473, 4-8.
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 15
    • 34248997838 scopus 로고    scopus 로고
    • N-glycan structure dictates extension of protein folding or onset of disposal
    • Molinari M, (2007) N-glycan structure dictates extension of protein folding or onset of disposal. Nat Chem Biol 3, 313-320.
    • (2007) Nat Chem Biol , vol.3 , pp. 313-320
    • Molinari, M.1
  • 16
    • 23844433274 scopus 로고    scopus 로고
    • Glycosylation of Eag1 (Kv10.1) potassium channels: Intracellular trafficking and functional consequences
    • Napp J, Monje F, Stuhmer W, &, Pardo L, (2005) Glycosylation of Eag1 (Kv10.1) potassium channels: intracellular trafficking and functional consequences. J Biol Chem 280, 29506-29512.
    • (2005) J Biol Chem , vol.280 , pp. 29506-29512
    • Napp, J.1    Monje, F.2    Stuhmer, W.3    Pardo, L.4
  • 17
    • 1542275414 scopus 로고    scopus 로고
    • Glycosylation affects the protein stability and cell surface expression of Kv1.4 but not Kv1.1 potassium channels. A pore region determinant dictates the effect of glycosylation on trafficking
    • Watanabe I, Zhu J, Recio-Pinto E, &, Thornhill WB, (2004) Glycosylation affects the protein stability and cell surface expression of Kv1.4 but not Kv1.1 potassium channels. A pore region determinant dictates the effect of glycosylation on trafficking. J Biol Chem 279, 8879-8885.
    • (2004) J Biol Chem , vol.279 , pp. 8879-8885
    • Watanabe, I.1    Zhu, J.2    Recio-Pinto, E.3    Thornhill, W.B.4
  • 18
    • 74949125668 scopus 로고    scopus 로고
    • Role of asparagine-linked glycosylation in cell surface expression and function of the human adrenocorticotropin receptor (melanocortin 2 receptor) in 293/FRT cells
    • Roy S, Perron B, &, Gallo-Payet N, (2010) Role of asparagine-linked glycosylation in cell surface expression and function of the human adrenocorticotropin receptor (melanocortin 2 receptor) in 293/FRT cells. Endocrinology 151, 660-670.
    • (2010) Endocrinology , vol.151 , pp. 660-670
    • Roy, S.1    Perron, B.2    Gallo-Payet, N.3
  • 19
    • 0029742881 scopus 로고    scopus 로고
    • Expression of Kv1.1 delayed-rectifier potassium channels in Lec mutant CHO cell lines reveals a role for sialylation in channel function
    • Thornhill WB, Wu MB, Jiang X, Wu X, Morgan P, &, Margiiotta J, (1996) Expression of Kv1.1 delayed-rectifier potassium channels in Lec mutant CHO cell lines reveals a role for sialylation in channel function. J Biol Chem 271, 19093-19098.
    • (1996) J Biol Chem , vol.271 , pp. 19093-19098
    • Thornhill, W.B.1    Wu, M.B.2    Jiang, X.3    Wu, X.4    Morgan, P.5    Margiiotta, J.6
  • 20
    • 33947302602 scopus 로고    scopus 로고
    • The glycosylation state of Kv1.2 potassium channels affects trafficking, gating, and simulated action potentials
    • Watanabe I, Zhu J, Sutachan JJ, Gottschalk A, Recio-Pinto E, &, Thornhill WB, (2007) The glycosylation state of Kv1.2 potassium channels affects trafficking, gating, and simulated action potentials. Brain Res 1144, 1-18.
    • (2007) Brain Res , vol.1144 , pp. 1-18
    • Watanabe, I.1    Zhu, J.2    Sutachan, J.J.3    Gottschalk, A.4    Recio-Pinto, E.5    Thornhill, W.B.6
  • 22
    • 0034871051 scopus 로고    scopus 로고
    • Congenital disorders involving defective N-glycosylation of proteins
    • Schachter H, (2001) Congenital disorders involving defective N-glycosylation of proteins. Cell Mol Life Sci 58, 1085-1104.
    • (2001) Cell Mol Life Sci , vol.58 , pp. 1085-1104
    • Schachter, H.1
  • 23
    • 0001686632 scopus 로고    scopus 로고
    • Endogenous voltage-gated potassium channels in human embryonic kidney (HEK293) cells
    • Yu SP, &, Kerchner GA, (1998) Endogenous voltage-gated potassium channels in human embryonic kidney (HEK293) cells. J Neurosci Res 52, 612-617.
    • (1998) J Neurosci Res , vol.52 , pp. 612-617
    • Yu, S.P.1    Kerchner, G.A.2
  • 24
    • 0031036380 scopus 로고    scopus 로고
    • Characterization of a CNS cell line, CAD, in which morphological differentiation is initiated by serum deprivation
    • Qi Y, Wang JKT, McMillian M, &, Chikaraishi DM, (1997) Characterization of a CNS cell line, CAD, in which morphological differentiation is initiated by serum deprivation. J Neurosci 17, 1217-1225.
    • (1997) J Neurosci , vol.17 , pp. 1217-1225
    • Qi, Y.1    Wang, J.K.T.2    McMillian, M.3    Chikaraishi, D.M.4
  • 25
    • 38349191968 scopus 로고    scopus 로고
    • Inverse correlation between the extent of N-glycan branching and intercellular adhesion in epithelia: Contribution of the Na,K-ATPase β1 subunit
    • Vagin O, Tokhtaeva E, Yakubov I, Shevchenko E, &, Sachs G, (2008) Inverse correlation between the extent of N-glycan branching and intercellular adhesion in epithelia: contribution of the Na,K-ATPase β1 subunit. J Biol Chem 283, 2192-2202.
    • (2008) J Biol Chem , vol.283 , pp. 2192-2202
    • Vagin, O.1    Tokhtaeva, E.2    Yakubov, I.3    Shevchenko, E.4    Sachs, G.5
  • 26
    • 0042266719 scopus 로고    scopus 로고
    • A genetic approach to Mammalian glycan function
    • Lowe JB, &, Marth JD, (2003) A genetic approach to Mammalian glycan function. Annu Rev Biochem 72, 643-691.
    • (2003) Annu Rev Biochem , vol.72 , pp. 643-691
    • Lowe, J.B.1    Marth, J.D.2
  • 27
    • 0033392596 scopus 로고    scopus 로고
    • Diabetes mellitus induces long lasting changes in the glucose transporter of rat heart endothelial cells
    • Hirsch B, &, Rösen P, (1999) Diabetes mellitus induces long lasting changes in the glucose transporter of rat heart endothelial cells. Horm Metab Res 31, 645-652.
    • (1999) Horm Metab Res , vol.31 , pp. 645-652
    • Hirsch, B.1    Rösen, P.2
  • 28
    • 0028175781 scopus 로고
    • Glycosylation of shaker potassium channel protein in insect cell culture and in Xenopus oocytes
    • Santacruz-Toloza L, Huang Y, John SA, &, Papazian DM, (1994) Glycosylation of shaker potassium channel protein in insect cell culture and in Xenopus oocytes. Biochemistry 33, 5607-5613.
    • (1994) Biochemistry , vol.33 , pp. 5607-5613
    • Santacruz-Toloza, L.1    Huang, Y.2    John, S.A.3    Papazian, D.M.4
  • 30
    • 0028040839 scopus 로고
    • Asparagine-linked oligosaccharides are localized to single extracytosolic segments in multi-span membrane glycoproteins
    • Landolt-Marticorena C, &, Reithmeier RA, (1994) Asparagine-linked oligosaccharides are localized to single extracytosolic segments in multi-span membrane glycoproteins. Biochem J 302, 253-260.
    • (1994) Biochem J , vol.302 , pp. 253-260
    • Landolt-Marticorena, C.1    Reithmeier, R.A.2
  • 31
    • 0023663543 scopus 로고
    • Oligosaccharyl transferase: The central enzyme in the pathway of glycoprotein assembly
    • Kaplan HA, Welply JK, &, Lennarz WJ, (1987) Oligosaccharyl transferase: the central enzyme in the pathway of glycoprotein assembly. Biochim Biophys Acta 906, 161-173.
    • (1987) Biochim Biophys Acta , vol.906 , pp. 161-173
    • Kaplan, H.A.1    Welply, J.K.2    Lennarz, W.J.3
  • 32
    • 0029041308 scopus 로고
    • The hydroxy amino acid in an Asn-X-Ser/Thr sequon can influence N-linked core glycosylation efficiency and the level of expression of a cell surface glycoprotein
    • Kasturi L, Eshleman JR, Wunner WH, &, Shakin-Eshleman SH, (1995) The hydroxy amino acid in an Asn-X-Ser/Thr sequon can influence N-linked core glycosylation efficiency and the level of expression of a cell surface glycoprotein. J Biol Chem 270, 14756-14761.
    • (1995) J Biol Chem , vol.270 , pp. 14756-14761
    • Kasturi, L.1    Eshleman, J.R.2    Wunner, W.H.3    Shakin-Eshleman, S.H.4
  • 33
    • 0242637036 scopus 로고    scopus 로고
    • Allowed N-glycosylation sites on the Kv1.2 potassium channel S1-S2 linker: Implications for linker secondary structure and the glycosylation effect on channel function
    • Zhu J, Watanabe I, Poholek A, Koss M, Gomez B, Yan C, Recio-Pinto E, &, Thornhill WB, (2003) Allowed N-glycosylation sites on the Kv1.2 potassium channel S1-S2 linker: implications for linker secondary structure and the glycosylation effect on channel function. Biochem J 375, 769-775.
    • (2003) Biochem J , vol.375 , pp. 769-775
    • Zhu, J.1    Watanabe, I.2    Poholek, A.3    Koss, M.4    Gomez, B.5    Yan, C.6    Recio-Pinto, E.7    Thornhill, W.B.8
  • 34
    • 33947724303 scopus 로고    scopus 로고
    • Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation
    • Lau KS, Partridge EA, Grigorian A, Silvescu CI, Reinhold VN, Demetriou M, &, Dennis JW, (2007) Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation. Cell 129, 123-134.
    • (2007) Cell , vol.129 , pp. 123-134
    • Lau, K.S.1    Partridge, E.A.2    Grigorian, A.3    Silvescu, C.I.4    Reinhold, V.N.5    Demetriou, M.6    Dennis, J.W.7
  • 36
    • 0029786969 scopus 로고    scopus 로고
    • Metabolic processing of gangliosides by normal and salla human fibroblasts in culture
    • Chigorno V, Tettamanti G, &, Sonnino S, (1996) Metabolic processing of gangliosides by normal and salla human fibroblasts in culture. J Biol Chem 271, 21738-21744.
    • (1996) J Biol Chem , vol.271 , pp. 21738-21744
    • Chigorno, V.1    Tettamanti, G.2    Sonnino, S.3
  • 37
    • 1642458114 scopus 로고    scopus 로고
    • Cloning and expression of murine enzymes involved in the salvage pathway of GDP-L-fucose L-fucokinase and GDP-L-fucose pyrophosphorylase
    • Niittymaki J, Mattila P, Roos C, Huopaniemi L, Sjoblom S, &, Renkonen R, (2004) Cloning and expression of murine enzymes involved in the salvage pathway of GDP-L-fucose L-fucokinase and GDP-L-fucose pyrophosphorylase. Eur J Biochem 271, 78-86.
    • (2004) Eur J Biochem , vol.271 , pp. 78-86
    • Niittymaki, J.1    Mattila, P.2    Roos, C.3    Huopaniemi, L.4    Sjoblom, S.5    Renkonen, R.6
  • 39
    • 0036233290 scopus 로고    scopus 로고
    • UDP-GlcNAc concentration is an important factor in the biosynthesis of β1,6-branched oligosaccharides: Regulation based on the kinetic properties of N-acetylglucosaminyltransferase v
    • Sasai K, Ikeda Y, Fujii T, Tsuda T, &, Taniguchi N, (2002) UDP-GlcNAc concentration is an important factor in the biosynthesis of β1,6-branched oligosaccharides: regulation based on the kinetic properties of N-acetylglucosaminyltransferase V. Glycobiology 12, 119-127.
    • (2002) Glycobiology , vol.12 , pp. 119-127
    • Sasai, K.1    Ikeda, Y.2    Fujii, T.3    Tsuda, T.4    Taniguchi, N.5
  • 40
    • 0038495798 scopus 로고    scopus 로고
    • Fucose: Biosynthesis and biological function in mammals
    • Becker DJ, &, Lowe JB, (2003) Fucose: biosynthesis and biological function in mammals. Glycobiology 13, 41R-53R.
    • (2003) Glycobiology , vol.13
    • Becker, D.J.1    Lowe, J.B.2
  • 42
    • 0031736329 scopus 로고    scopus 로고
    • Alpha 1,6-linked fucose affects the expression and stability of polysialic acid-carrying glycoproteins in Chinese hamster ovary cells
    • Kojima N, Tachida Y, &, Tsuji S, (1998) Alpha 1,6-linked fucose affects the expression and stability of polysialic acid-carrying glycoproteins in Chinese hamster ovary cells. J Biochem 124, 726-737.
    • (1998) J Biochem , vol.124 , pp. 726-737
    • Kojima, N.1    Tachida, Y.2    Tsuji, S.3
  • 43
    • 0030064740 scopus 로고    scopus 로고
    • Influence of core fucosylation on the flexibility of a biantennary N-linked oligosaccharide
    • Stubbs HJ, Lih JJ, Gustafson TL, &, Rice KG, (1996) Influence of core fucosylation on the flexibility of a biantennary N-linked oligosaccharide. Biochemistry 35, 937-947.
    • (1996) Biochemistry , vol.35 , pp. 937-947
    • Stubbs, H.J.1    Lih, J.J.2    Gustafson, T.L.3    Rice, K.G.4
  • 44
    • 70349878950 scopus 로고    scopus 로고
    • Sialic acids as regulators of molecular and cellular interactions
    • Schauer R, (2009) Sialic acids as regulators of molecular and cellular interactions. Curr Opin Struct Biol 19, 507-514.
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 507-514
    • Schauer, R.1
  • 45
    • 33846169715 scopus 로고    scopus 로고
    • α2,6-Linked sialic acid acts as a receptor for Feline calicivirus
    • Stuart AD, &, Brown TDK, (2007) α2,6-Linked sialic acid acts as a receptor for Feline calicivirus. J Gen Virol 88, 177-186.
    • (2007) J Gen Virol , vol.88 , pp. 177-186
    • Stuart, A.D.1    Brown, T.D.K.2
  • 47
    • 0025789618 scopus 로고
    • Structural analysis and functional role of the carbohydrate component of somatostatin receptors
    • Rens-Domiano S, &, Reisine T, (1991) Structural analysis and functional role of the carbohydrate component of somatostatin receptors. J Biol Chem 266, 20094-20102.
    • (1991) J Biol Chem , vol.266 , pp. 20094-20102
    • Rens-Domiano, S.1    Reisine, T.2
  • 48
    • 25144524257 scopus 로고    scopus 로고
    • Sialylation of human thyrotropin receptor improves and prolongs its cell-surface expression
    • Frenzel R, Krohn K, Eszlinger M, Tonjes A, &, Paschke R, (2005) Sialylation of human thyrotropin receptor improves and prolongs its cell-surface expression. Mol Pharmacol 68, 1106-1113.
    • (2005) Mol Pharmacol , vol.68 , pp. 1106-1113
    • Frenzel, R.1    Krohn, K.2    Eszlinger, M.3    Tonjes, A.4    Paschke, R.5
  • 49
    • 47749148805 scopus 로고    scopus 로고
    • Removal of sialic acid involving Klotho causes cell-surface retention of TRPV5 channel via binding to galectin-1
    • Cha S, Ortega B, Kurosu H, Rosenblatt KP, Kuro-o M, &, Huang C, (2008) Removal of sialic acid involving Klotho causes cell-surface retention of TRPV5 channel via binding to galectin-1. PNAS 105, 9805-9810.
    • (2008) PNAS , vol.105 , pp. 9805-9810
    • Cha, S.1    Ortega, B.2    Kurosu, H.3    Rosenblatt, K.P.4    Kuro-O, M.5    Huang, C.6


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