메뉴 건너뛰기




Volumn 22, Issue 5-6, 2008, Pages 591-600

Modulation of the voltage-gated potassium channel Kv1.5 by the SGK1 protein kinase involves inhibition of channel ubiquitination

Author keywords

Insulin; Nedd4 2; Phosphorylation; Trafficking; Voltage gated potassium channel

Indexed keywords

BREFELDIN A; POTASSIUM CHANNEL KV1.5; SERUM AND GLUCOCORTICOID REGULATED KINASE 1; UBIQUITIN PROTEIN LIGASE; UBIQUITIN PROTEIN LIGASE NEDD4; VOLTAGE GATED POTASSIUM CHANNEL;

EID: 57649231743     PISSN: 10158987     EISSN: None     Source Type: Journal    
DOI: 10.1159/000185543     Document Type: Article
Times cited : (73)

References (40)
  • 1
    • 0042879951 scopus 로고    scopus 로고
    • Insulin granule dynamics in pancreatic beta cells
    • Rorsman P, Renstrom E: Insulin granule dynamics in pancreatic beta cells. Diabetologia 2003;46:1029-1045.
    • (2003) Diabetologia , vol.46 , pp. 1029-1045
    • Rorsman, P.1    Renstrom, E.2
  • 3
    • 0042879894 scopus 로고    scopus 로고
    • Voltage-dependent K(+) channels in pancreatic beta cells: Role, regulation and potential as therapeutic targets
    • MacDonald PE, Wheeler MB: Voltage-dependent K(+) channels in pancreatic beta cells: role, regulation and potential as therapeutic targets. Diabetologia 2003;46:1046-1062.
    • (2003) Diabetologia , vol.46 , pp. 1046-1062
    • MacDonald, P.E.1    Wheeler, M.B.2
  • 4
    • 0028061930 scopus 로고
    • Delayed rectifier K+ channel overexpression in transgenic islets and beta-cells associated with impaired glucose responsiveness
    • Philipson LH, Rosenberg MP, Kuznetsov A, Lancaster ME, Worley JF, III, Roe MW, Dukes ID: Delayed rectifier K+ channel overexpression in transgenic islets and beta-cells associated with impaired glucose responsiveness. J Biol Chem 1994;269:27787-27790.
    • (1994) J Biol Chem , vol.269 , pp. 27787-27790
    • Philipson, L.H.1    Rosenberg, M.P.2    Kuznetsov, A.3    Lancaster, M.E.4    Worley III, J.F.5    Roe, M.W.6    Dukes, I.D.7
  • 5
    • 0035046504 scopus 로고    scopus 로고
    • The expression and regulation of depolarization-activated K+ channels in the insulin-secreting cell line INS-1
    • Su J, Yu H, Lenka N, Hescheler J, Ullrich S: The expression and regulation of depolarization-activated K+ channels in the insulin-secreting cell line INS-1. Pflugers Arch 2001;442:49-56.
    • (2001) Pflugers Arch , vol.442 , pp. 49-56
    • Su, J.1    Yu, H.2    Lenka, N.3    Hescheler, J.4    Ullrich, S.5
  • 7
    • 0030866606 scopus 로고    scopus 로고
    • Direct glucocorticoid inhibition of insulin secretion. An in vitro study of dexamethasone effects in mouse islets
    • Lambillotte C, Gilon P, Henquin JC: Direct glucocorticoid inhibition of insulin secretion. An in vitro study of dexamethasone effects in mouse islets. J Clin Invest 1997;99:414-423.
    • (1997) J Clin Invest , vol.99 , pp. 414-423
    • Lambillotte, C.1    Gilon, P.2    Henquin, J.C.3
  • 8
    • 0022608081 scopus 로고
    • Effect of adrenal steroids on insulin release from cultured rat islets of Langerhans
    • Pierluissi J, Navas FO, Ashcroft SJ: Effect of adrenal steroids on insulin release from cultured rat islets of Langerhans. Diabetologia 1986;29:119-121.
    • (1986) Diabetologia , vol.29 , pp. 119-121
    • Pierluissi, J.1    Navas, F.O.2    Ashcroft, S.J.3
  • 9
    • 0027534990 scopus 로고
    • Characterization of sgk, a novel member of the serine/threonine protein kinase gene family which is transcriptionally induced by glucocorticoids and serum
    • Webster MK, Goya L, Ge Y, Maiyar AC, Firestone GL: Characterization of sgk, a novel member of the serine/threonine protein kinase gene family which is transcriptionally induced by glucocorticoids and serum. Mol Cell Biol 1993;13:2031-2040.
    • (1993) Mol Cell Biol , vol.13 , pp. 2031-2040
    • Webster, M.K.1    Goya, L.2    Ge, Y.3    Maiyar, A.C.4    Firestone, G.L.5
  • 11
    • 0033560707 scopus 로고    scopus 로고
    • Activation of serum- and glucocorticoid-regulated protein kinase by agonists that activate phosphatidylinositide 3-kinase is mediated by 3-phosphoinositide-dependent protein kinase-1 (PDK1) and PDK2
    • Kobayashi T, Cohen P: Activation of serum- and glucocorticoid-regulated protein kinase by agonists that activate phosphatidylinositide 3-kinase is mediated by 3-phosphoinositide-dependent protein kinase-1 (PDK1) and PDK2. Biochem J 1999;339 (Pt 2):319-328.
    • (1999) Biochem J , vol.339 , Issue.PART 2 , pp. 319-328
    • Kobayashi, T.1    Cohen, P.2
  • 12
    • 0035882103 scopus 로고    scopus 로고
    • The PIF-binding pocket in PDK1 is essential for activation of S6K and SGK, but not PKB
    • Biondi RM, Kieloch A, Currie RA, Deak M, Alessi DR: The PIF-binding pocket in PDK1 is essential for activation of S6K and SGK, but not PKB. EMBO J 2001;20:4380-4390.
    • (2001) EMBO J , vol.20 , pp. 4380-4390
    • Biondi, R.M.1    Kieloch, A.2    Currie, R.A.3    Deak, M.4    Alessi, D.R.5
  • 13
    • 0037107414 scopus 로고    scopus 로고
    • A phosphoserine/threonine-binding pocket in AGC kinases and PDK1 mediates activation by hydrophobic motif phosphorylation
    • Frodin M, Antal TL, Dummler BA, Jensen CJ, Deak M, Gammeltoft S, Biondi RM: A phosphoserine/threonine-binding pocket in AGC kinases and PDK1 mediates activation by hydrophobic motif phosphorylation. EMBO J 2002;21:5396-5407.
    • (2002) EMBO J , vol.21 , pp. 5396-5407
    • Frodin, M.1    Antal, T.L.2    Dummler, B.A.3    Jensen, C.J.4    Deak, M.5    Gammeltoft, S.6    Biondi, R.M.7
  • 14
    • 0033151832 scopus 로고    scopus 로고
    • Serum and glucocorticoid-inducible kinase (SGK) is a target of the PI 3-kinase-stimulated signaling pathway
    • Park J, Leong ML, Buse P, Maiyar AC, Firestone GL, Hemmings BA: Serum and glucocorticoid-inducible kinase (SGK) is a target of the PI 3-kinase-stimulated signaling pathway. EMBO J 1999;18:3024-3033.
    • (1999) EMBO J , vol.18 , pp. 3024-3033
    • Park, J.1    Leong, M.L.2    Buse, P.3    Maiyar, A.C.4    Firestone, G.L.5    Hemmings, B.A.6
  • 15
    • 33749500123 scopus 로고    scopus 로고
    • (Patho)physiological significance of the serum- and glucocorticoid-inducible kinase isoforms
    • Lang F, Bohmer C, Palmada M, Seebohm G, Strutz-Seebohm N, Vallon V: (Patho)physiological significance of the serum- and glucocorticoid-inducible kinase isoforms. Physiol Rev 2006;86:1151-1178.
    • (2006) Physiol Rev , vol.86 , pp. 1151-1178
    • Lang, F.1    Bohmer, C.2    Palmada, M.3    Seebohm, G.4    Strutz-Seebohm, N.5    Vallon, V.6
  • 17
    • 1842525944 scopus 로고    scopus 로고
    • Regulation of the voltage gated K+ channel Kv1.3 by the ubiquitin ligase Nedd4-2 and the serum and glucocorticoid inducible kinase SGK1
    • Henke G, Maier G, Wallisch S, Boehmer C, Lang F: Regulation of the voltage gated K+ channel Kv1.3 by the ubiquitin ligase Nedd4-2 and the serum and glucocorticoid inducible kinase SGK1. J Cell Physiol 2004;199:194-199.
    • (2004) J Cell Physiol , vol.199 , pp. 194-199
    • Henke, G.1    Maier, G.2    Wallisch, S.3    Boehmer, C.4    Lang, F.5
  • 18
    • 0034008744 scopus 로고    scopus 로고
    • The use of Xenopus laevis oocytes for the functional characterization of heterologously expressed membrane proteins
    • Wagner CA, Friedrich B, Setiawan I, Lang F, Broer S: The use of Xenopus laevis oocytes for the functional characterization of heterologously expressed membrane proteins. Cell Physiol Biochem 2000;10:1-12.
    • (2000) Cell Physiol Biochem , vol.10 , pp. 1-12
    • Wagner, C.A.1    Friedrich, B.2    Setiawan, I.3    Lang, F.4    Broer, S.5
  • 19
    • 0035813093 scopus 로고    scopus 로고
    • The classical progesterone receptor associates with p42 MAPK and is involved in phosphatidylinositol 3-kinase signaling in Xenopus oocytes
    • Bagowski CP, Myers JW, Ferrell JE, Jr.: The classical progesterone receptor associates with p42 MAPK and is involved in phosphatidylinositol 3-kinase signaling in Xenopus oocytes. J Biol Chem 2001;276:37708-37714.
    • (2001) J Biol Chem , vol.276 , pp. 37708-37714
    • Bagowski, C.P.1    Myers, J.W.2    Ferrell Jr., J.E.3
  • 24
    • 0041932135 scopus 로고    scopus 로고
    • Regulation of the glutamate transporter EAAT1 by the ubiquitin ligase Nedd4-2 and the serum and glucocorticoid-inducible kinase isoforms SGK1/3 and protein kinase B
    • Boehmer C, Henke G, Schniepp R, Palmada M, Rothstein JD, Broer S, Lang F: Regulation of the glutamate transporter EAAT1 by the ubiquitin ligase Nedd4-2 and the serum and glucocorticoid-inducible kinase isoforms SGK1/3 and protein kinase B. J Neurochem 2003;86:1181-1188.
    • (2003) J Neurochem , vol.86 , pp. 1181-1188
    • Boehmer, C.1    Henke, G.2    Schniepp, R.3    Palmada, M.4    Rothstein, J.D.5    Broer, S.6    Lang, F.7
  • 25
    • 34447324628 scopus 로고    scopus 로고
    • EAAT4 phosphorylation at the SGK1 consensus site is required for transport modulation by the kinase
    • Rajamanickam J, Palmada M, Lang F, Boehmer C: EAAT4 phosphorylation at the SGK1 consensus site is required for transport modulation by the kinase. J Neurochem 2007;102:858-866.
    • (2007) J Neurochem , vol.102 , pp. 858-866
    • Rajamanickam, J.1    Palmada, M.2    Lang, F.3    Boehmer, C.4
  • 26
    • 33646113826 scopus 로고    scopus 로고
    • Posttranslational regulation of EAAT2 function by co-expressed ubiquitin ligase Nedd4-2 is impacted by SGK kinases
    • Boehmer C, Palmada M, Rajamanickam J, Schniepp R, Amara S, Lang F: Posttranslational regulation of EAAT2 function by co-expressed ubiquitin ligase Nedd4-2 is impacted by SGK kinases. J Neurochem 2006;97:911-921.
    • (2006) J Neurochem , vol.97 , pp. 911-921
    • Boehmer, C.1    Palmada, M.2    Rajamanickam, J.3    Schniepp, R.4    Amara, S.5    Lang, F.6
  • 27
    • 12444307413 scopus 로고    scopus 로고
    • Requirement of PDZ domains for the stimulation of the epithelial Ca2+ channel TRPV5 by the NHE regulating factor NHERF2 and the serum and glucocorticoid inducible kinase SGK1
    • Palmada M, Poppendieck S, Embark HM, van de Graaf SF, Boehmer C, Bindels RJ, Lang F: Requirement of PDZ domains for the stimulation of the epithelial Ca2+ channel TRPV5 by the NHE regulating factor NHERF2 and the serum and glucocorticoid inducible kinase SGK1. Cell Physiol Biochem 2005;15:175-182.
    • (2005) Cell Physiol Biochem , vol.15 , pp. 175-182
    • Palmada, M.1    Poppendieck, S.2    Embark, H.M.3    van de Graaf, S.F.4    Boehmer, C.5    Bindels, R.J.6    Lang, F.7
  • 29
    • 0028940828 scopus 로고
    • Phosphorylation by protein kinase A enhances delayed rectifier K+ current in rabbit vascular smooth muscle cells
    • Aiello EA, Walsh MP, Cole WC: Phosphorylation by protein kinase A enhances delayed rectifier K+ current in rabbit vascular smooth muscle cells. Am J Physiol 1995;268:H926-H934.
    • (1995) Am J Physiol , vol.268
    • Aiello, E.A.1    Walsh, M.P.2    Cole, W.C.3
  • 30
    • 0030346307 scopus 로고    scopus 로고
    • Regulation of 4-aminopyridine-sensitive, delayed rectifier K+ channels in vascular smooth muscle by phosphorylation
    • Cole WC, Clement-Chomienne O, Aiello EA: Regulation of 4-aminopyridine-sensitive, delayed rectifier K+ channels in vascular smooth muscle by phosphorylation. Biochem Cell Biol 1996;74:439-447.
    • (1996) Biochem Cell Biol , vol.74 , pp. 439-447
    • Cole, W.C.1    Clement-Chomienne, O.2    Aiello, E.A.3
  • 31
    • 0036156336 scopus 로고    scopus 로고
    • Modulation of Kv1.5 currents by protein kinase A, tyrosine kinase, and protein tyrosine phosphatase requires an intact cytoskeleton
    • Mason HS, Latten MJ, Godoy LD, Horowitz B, Kenyon JL: Modulation of Kv1.5 currents by protein kinase A, tyrosine kinase, and protein tyrosine phosphatase requires an intact cytoskeleton. Mol Pharmacol 2002;61:285-293.
    • (2002) Mol Pharmacol , vol.61 , pp. 285-293
    • Mason, H.S.1    Latten, M.J.2    Godoy, L.D.3    Horowitz, B.4    Kenyon, J.L.5
  • 32
    • 0029082517 scopus 로고
    • Localization of the Kv1.5 K+ channel protein in explanted cardiac tissue
    • Mays DJ, Foose JM, Philipson LH, Tamkun MM: Localization of the Kv1.5 K+ channel protein in explanted cardiac tissue. J Clin Invest 1995;96:282-292.
    • (1995) J Clin Invest , vol.96 , pp. 282-292
    • Mays, D.J.1    Foose, J.M.2    Philipson, L.H.3    Tamkun, M.M.4
  • 33
    • 0033553567 scopus 로고    scopus 로고
    • Protein kinase A phosphorylation alters Kvbeta1.3 subunit-mediated inactivation of the Kv1.5 potassium channel
    • Kwak YG, Hu N, Wei J, George AL, Jr., Grobaski TD, Tamkun MM, Murray KT: Protein kinase A phosphorylation alters Kvbeta1.3 subunit-mediated inactivation of the Kv1.5 potassium channel. J Biol Chem 1999;274:13928-13932.
    • (1999) J Biol Chem , vol.274 , pp. 13928-13932
    • Kwak, Y.G.1    Hu, N.2    Wei, J.3    George Jr., A.L.4    Grobaski, T.D.5    Tamkun, M.M.6    Murray, K.T.7
  • 34
    • 0028841492 scopus 로고
    • Make it or break it: The role of ubiquitin-dependent proteolysis in cellular regulation
    • Deshaies RJ: Make it or break it: the role of ubiquitin-dependent proteolysis in cellular regulation. Trends Cell Biol 1995;5:428-434.
    • (1995) Trends Cell Biol , vol.5 , pp. 428-434
    • Deshaies, R.J.1
  • 35
    • 0029870836 scopus 로고    scopus 로고
    • Protein degradation or regulation: Ub the judge
    • Hochstrasser M: Protein degradation or regulation: Ub the judge. Cell 1996;84:813-815.
    • (1996) Cell , vol.84 , pp. 813-815
    • Hochstrasser, M.1
  • 36
    • 34547107368 scopus 로고    scopus 로고
    • Nedd4-2 catalyzes ubiquitination and degradation of cell surface ENaC
    • Zhou R, Patel SV, Snyder PM: Nedd4-2 catalyzes ubiquitination and degradation of cell surface ENaC. J Biol Chem 2007;282:20207-20212.
    • (2007) J Biol Chem , vol.282 , pp. 20207-20212
    • Zhou, R.1    Patel, S.V.2    Snyder, P.M.3
  • 39
    • 0034697296 scopus 로고    scopus 로고
    • Surface expression of Kv1 channels is governed by a C-terminal motif
    • Li D, Takimoto K, Levitan ES: Surface expression of Kv1 channels is governed by a C-terminal motif. J Biol Chem 2000;275:11597-11602.
    • (2000) J Biol Chem , vol.275 , pp. 11597-11602
    • Li, D.1    Takimoto, K.2    Levitan, E.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.