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Volumn 8, Issue 9, 2013, Pages

Detection of Phospho-Sites Generated by Protein Kinase CK2 in CFTR: Mechanistic Aspects of Thr1471 Phosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXY TERMINAL TELOPEPTIDE; CASEIN KINASE I; CASEIN KINASE II; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; POLO LIKE KINASE 2; POLO LIKE KINASE 3; PROTEIN KINASE INHIBITOR; SERINE; THREONINE;

EID: 84884239437     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0074232     Document Type: Article
Times cited : (31)

References (45)
  • 1
    • 38349050413 scopus 로고    scopus 로고
    • Solubilizing mutations used to crystallize one CFTR domain attenuate the trafficking and channel defects caused by the major cystic fibrosis mutation
    • Pissarra LS, Farinha CM, Xu Z, Schmidt A, Thibodeau PH, et al. (2008) Solubilizing mutations used to crystallize one CFTR domain attenuate the trafficking and channel defects caused by the major cystic fibrosis mutation. Chem Biol 15: 62-69.
    • (2008) Chem Biol , vol.15 , pp. 62-69
    • Pissarra, L.S.1    Farinha, C.M.2    Xu, Z.3    Schmidt, A.4    Thibodeau, P.H.5
  • 3
    • 0028858161 scopus 로고
    • Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
    • Jensen TJ, Loo MA, Pind S, Williams DB, Goldberg AL, et al. (1995) Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell 83: 129-135.
    • (1995) Cell , vol.83 , pp. 129-135
    • Jensen, T.J.1    Loo, M.A.2    Pind, S.3    Williams, D.B.4    Goldberg, A.L.5
  • 4
    • 0035013543 scopus 로고    scopus 로고
    • The Delta F508 mutation shortens the biochemical half-life of plasma membrane CFTR in polarized epithelial cells
    • Heda GD, Tanwani M, Marino CR, (2001) The Delta F508 mutation shortens the biochemical half-life of plasma membrane CFTR in polarized epithelial cells. Am J Physiol, Cell Physiol 280: C166-174.
    • (2001) Am J Physiol, Cell Physiol , vol.280
    • Heda, G.D.1    Tanwani, M.2    Marino, C.R.3
  • 5
    • 0030667705 scopus 로고    scopus 로고
    • Evidence for phosphorylation of serine 753 in CFTR using a novel metal-ion affinity resin and matrix-assisted laser desorption mass spectrometry
    • Neville DC, Rozanas CR, Price EM, Gruis DB, Verkman AS, et al. (1997) Evidence for phosphorylation of serine 753 in CFTR using a novel metal-ion affinity resin and matrix-assisted laser desorption mass spectrometry. Protein Sci 6: 2436-2445.
    • (1997) Protein Sci , vol.6 , pp. 2436-2445
    • Neville, D.C.1    Rozanas, C.R.2    Price, E.M.3    Gruis, D.B.4    Verkman, A.S.5
  • 6
    • 20844457435 scopus 로고    scopus 로고
    • Preferential phosphorylation of R-domain Serine 768 dampens activation of CFTR channels by PKA
    • Csanády L, Seto-Young D, Chan KW, Cenciarelli C, Angel BB, et al. (2005) Preferential phosphorylation of R-domain Serine 768 dampens activation of CFTR channels by PKA. J Gen Physiol 125: 171-186.
    • (2005) J Gen Physiol , vol.125 , pp. 171-186
    • Csanády, L.1    Seto-Young, D.2    Chan, K.W.3    Cenciarelli, C.4    Angel, B.B.5
  • 7
    • 84555194937 scopus 로고    scopus 로고
    • Purification of CFTR for mass spectrometry analysis: identification of palmitoylation and other post-translational modifications
    • McClure M, DeLucas LJ, Wilson L, Ray M, Rowe SM, et al. (2012) Purification of CFTR for mass spectrometry analysis: identification of palmitoylation and other post-translational modifications. Protein Eng Des Sel 25: 7-14.
    • (2012) Protein Eng Des Sel , vol.25 , pp. 7-14
    • McClure, M.1    DeLucas, L.J.2    Wilson, L.3    Ray, M.4    Rowe, S.M.5
  • 8
    • 0037107552 scopus 로고    scopus 로고
    • Protein kinase CK2: a challenge to canons
    • Pinna LA, (2002) Protein kinase CK2: a challenge to canons. J Cell Sci 115: 3873-3878.
    • (2002) J Cell Sci , vol.115 , pp. 3873-3878
    • Pinna, L.A.1
  • 9
    • 48249106644 scopus 로고    scopus 로고
    • Modulation of protein kinase CK2 activity by fragments of CFTR encompassing F508 may reflect functional links with cystic fibrosis pathogenesis
    • Pagano MA, Arrigoni G, Marin O, Sarno S, Meggio F, et al. (2008) Modulation of protein kinase CK2 activity by fragments of CFTR encompassing F508 may reflect functional links with cystic fibrosis pathogenesis. Biochemistry 47: 7925-7936.
    • (2008) Biochemistry , vol.47 , pp. 7925-7936
    • Pagano, M.A.1    Arrigoni, G.2    Marin, O.3    Sarno, S.4    Meggio, F.5
  • 10
    • 0035847102 scopus 로고    scopus 로고
    • The tumor suppressor PTEN is phosphorylated by the protein kinase CK2 at its C terminus. Implications for PTEN stability to proteasome-mediated degradation
    • Torres J, Pulido R, (2001) The tumor suppressor PTEN is phosphorylated by the protein kinase CK2 at its C terminus. Implications for PTEN stability to proteasome-mediated degradation. J Biol Chem 276: 993-998.
    • (2001) J Biol Chem , vol.276 , pp. 993-998
    • Torres, J.1    Pulido, R.2
  • 11
    • 0242298578 scopus 로고    scopus 로고
    • CK2 Is a C-Terminal IkappaB Kinase Responsible for NF-kappaB Activation during the UV Response
    • Kato T Jr, Delhase M, Hoffmann A, Karin M, (2003) CK2 Is a C-Terminal IkappaB Kinase Responsible for NF-kappaB Activation during the UV Response. Mol Cell 12: 829-839.
    • (2003) Mol Cell , vol.12 , pp. 829-839
    • Kato Jr., T.1    Delhase, M.2    Hoffmann, A.3    Karin, M.4
  • 13
    • 83255187903 scopus 로고    scopus 로고
    • Contribution of casein kinase 2 and spleen tyrosine kinase to CFTR trafficking and protein kinase A-induced activity
    • Luz S, Kongsuphol P, Mendes AI, Romeiras F, Sousa M, et al. (2011) Contribution of casein kinase 2 and spleen tyrosine kinase to CFTR trafficking and protein kinase A-induced activity. Mol Cell Biol 31: 4392-4404.
    • (2011) Mol Cell Biol , vol.31 , pp. 4392-4404
    • Luz, S.1    Kongsuphol, P.2    Mendes, A.I.3    Romeiras, F.4    Sousa, M.5
  • 15
    • 0032957204 scopus 로고    scopus 로고
    • Biosynthesis and Degradation of CFTR
    • Kopito RR, (1999) Biosynthesis and Degradation of CFTR. Physiol Rev 79: S167-S173.
    • (1999) Physiol Rev , vol.79
    • Kopito, R.R.1
  • 16
    • 0033559258 scopus 로고    scopus 로고
    • The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis
    • Meacham GC, Lu Z, King S, Sorscher E, Tousson A, et al. (1999) The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis. EMBO J 18: 1492-1505.
    • (1999) EMBO J , vol.18 , pp. 1492-1505
    • Meacham, G.C.1    Lu, Z.2    King, S.3    Sorscher, E.4    Tousson, A.5
  • 17
    • 20344378216 scopus 로고    scopus 로고
    • Most F508del-CFTR is targeted to degradation at an early folding checkpoint and independently of calnexin
    • Farinha CM, Amaral MD, (2005) Most F508del-CFTR is targeted to degradation at an early folding checkpoint and independently of calnexin. Mol Cell Biol 25: 5242-5252.
    • (2005) Mol Cell Biol , vol.25 , pp. 5242-5252
    • Farinha, C.M.1    Amaral, M.D.2
  • 18
    • 2542480784 scopus 로고    scopus 로고
    • Endocytic trafficking routes of wild type and DeltaF508 cystic fibrosis transmembrane conductance regulator
    • Gentzsch M, Chang X-B, Cui L, Wu Y, Ozols VV, et al. (2004) Endocytic trafficking routes of wild type and DeltaF508 cystic fibrosis transmembrane conductance regulator. Mol Biol Cell 15: 2684-2696.
    • (2004) Mol Biol Cell , vol.15 , pp. 2684-2696
    • Gentzsch, M.1    Chang, X.-B.2    Cui, L.3    Wu, Y.4    Ozols, V.V.5
  • 20
    • 84863767664 scopus 로고    scopus 로고
    • Expression and purification of the cystic fibrosis transmembrane conductance regulator protein in Saccharomyces cerevisiae
    • O'Ryan L, Rimington T, Cant N, Ford RC, (2012) Expression and purification of the cystic fibrosis transmembrane conductance regulator protein in Saccharomyces cerevisiae. J Vis Exp. 61: e3860.
    • (2012) J Vis Exp , vol.61
    • O'Ryan, L.1    Rimington, T.2    Cant, N.3    Ford, R.C.4
  • 22
    • 84856507495 scopus 로고    scopus 로고
    • Superiority of PLK-2 as α-synuclein phosphorylating agent relies on unique specificity determinants
    • Salvi M, Trashi E, Marin O, Negro A, Sarno S, et al. (2012) Superiority of PLK-2 as α-synuclein phosphorylating agent relies on unique specificity determinants. Biochem Biophys Res Commun 418: 156-160.
    • (2012) Biochem Biophys Res Commun , vol.418 , pp. 156-160
    • Salvi, M.1    Trashi, E.2    Marin, O.3    Negro, A.4    Sarno, S.5
  • 24
    • 34248640261 scopus 로고    scopus 로고
    • Highly selective enrichment of phosphorylated peptides using titanium dioxide
    • Thingholm TE, Jørgensen TJD, Jensen ON, Larsen MR, (2006) Highly selective enrichment of phosphorylated peptides using titanium dioxide. Nat Protoc 1: 1929-1935.
    • (2006) Nat Protoc , vol.1 , pp. 1929-1935
    • Thingholm, T.E.1    Jørgensen, T.J.D.2    Jensen, O.N.3    Larsen, M.R.4
  • 25
    • 82755182013 scopus 로고    scopus 로고
    • Universal and Confident Phosphorylation Site Localization Using phosphoRS
    • Taus T, Köcher T, Pichler P, Paschke C, Schmidt A, et al. (2011) Universal and Confident Phosphorylation Site Localization Using phosphoRS. J Proteome Res 10: 5354-5362.
    • (2011) J Proteome Res , vol.10 , pp. 5354-5362
    • Taus, T.1    Köcher, T.2    Pichler, P.3    Paschke, C.4    Schmidt, A.5
  • 26
    • 34248679167 scopus 로고    scopus 로고
    • Tricine-SDS-PAGE
    • Schägger H, (2006) Tricine-SDS-PAGE. Nat Protoc 1: 16-22.
    • (2006) Nat Protoc , vol.1 , pp. 16-22
    • Schägger, H.1
  • 28
    • 33749020839 scopus 로고    scopus 로고
    • PIPER: an FFT-based protein docking program with pairwise potentials
    • Kozakov D, Brenke R, Comeau SR, Vajda S, (2006) PIPER: an FFT-based protein docking program with pairwise potentials. Proteins 65: 392-406.
    • (2006) Proteins , vol.65 , pp. 392-406
    • Kozakov, D.1    Brenke, R.2    Comeau, S.R.3    Vajda, S.4
  • 31
    • 0033933777 scopus 로고    scopus 로고
    • Inhibition of cystic fibrosis transmembrane conductance regulator by novel interaction with the metabolic sensor AMP-activated protein kinase
    • Hallows KR, Raghuram V, Kemp BE, Witters LA, Foskett JK, (2000) Inhibition of cystic fibrosis transmembrane conductance regulator by novel interaction with the metabolic sensor AMP-activated protein kinase. J Clin Invest 105: 1711-1721.
    • (2000) J Clin Invest , vol.105 , pp. 1711-1721
    • Hallows, K.R.1    Raghuram, V.2    Kemp, B.E.3    Witters, L.A.4    Foskett, J.K.5
  • 32
    • 0032584744 scopus 로고    scopus 로고
    • An apical PDZ protein anchors the cystic fibrosis transmembrane conductance regulator to the cytoskeleton
    • Short DB, Trotter KW, Reczek D, Kreda SM, Bretscher A, et al. (1998) An apical PDZ protein anchors the cystic fibrosis transmembrane conductance regulator to the cytoskeleton. J Biol Chem 273: 19797-19801.
    • (1998) J Biol Chem , vol.273 , pp. 19797-19801
    • Short, D.B.1    Trotter, K.W.2    Reczek, D.3    Kreda, S.M.4    Bretscher, A.5
  • 33
    • 0032080043 scopus 로고    scopus 로고
    • Peptide binding consensus of the NHE-RF-PDZ1 domain matches the C-terminal sequence of cystic fibrosis transmembrane conductance regulator (CFTR)
    • Wang S, Raab RW, Schatz PJ, Guggino WB, Li M, (1998) Peptide binding consensus of the NHE-RF-PDZ1 domain matches the C-terminal sequence of cystic fibrosis transmembrane conductance regulator (CFTR). FEBS Lett 427: 103-108.
    • (1998) FEBS Lett , vol.427 , pp. 103-108
    • Wang, S.1    Raab, R.W.2    Schatz, P.J.3    Guggino, W.B.4    Li, M.5
  • 34
    • 0037452680 scopus 로고    scopus 로고
    • Effects of C-terminal deletions on cystic fibrosis transmembrane conductance regulator function in cystic fibrosis airway epithelia
    • Ostedgaard LS, Randak C, Rokhlina T, Karp P, Vermeer D, et al. (2003) Effects of C-terminal deletions on cystic fibrosis transmembrane conductance regulator function in cystic fibrosis airway epithelia. Proc Natl Acad Sci USA 100: 1937-1942.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 1937-1942
    • Ostedgaard, L.S.1    Randak, C.2    Rokhlina, T.3    Karp, P.4    Vermeer, D.5
  • 35
    • 84861658918 scopus 로고    scopus 로고
    • Secreted kinase phosphorylates extracellular proteins that regulate biomineralization
    • Tagliabracci VS, Engel JL, Wen J, Wiley SE, Worby CA, et al. (2012) Secreted kinase phosphorylates extracellular proteins that regulate biomineralization. Science 336: 1150-1153.
    • (2012) Science , vol.336 , pp. 1150-1153
    • Tagliabracci, V.S.1    Engel, J.L.2    Wen, J.3    Wiley, S.E.4    Worby, C.A.5
  • 36
    • 84864713987 scopus 로고    scopus 로고
    • Inhibition of Protein Kinase CK2 by Flavonoids and Tyrphostins. A Structural Insight
    • Lolli G, Cozza G, Mazzorana M, Tibaldi E, Cesaro L, et al. (2012) Inhibition of Protein Kinase CK2 by Flavonoids and Tyrphostins. A Structural Insight. Biochemistry 51: 6097-6107.
    • (2012) Biochemistry , vol.51 , pp. 6097-6107
    • Lolli, G.1    Cozza, G.2    Mazzorana, M.3    Tibaldi, E.4    Cesaro, L.5
  • 38
    • 34548058372 scopus 로고    scopus 로고
    • Pharmacological and Functional Comparison of the Polo-like Kinase Family: Insight into Inhibitor and Substrate Specificity
    • Johnson EF, Stewart KD, Woods KW, Giranda VL, Luo Y, (2007) Pharmacological and Functional Comparison of the Polo-like Kinase Family: Insight into Inhibitor and Substrate Specificity. Biochemistry 46: 9551-9563.
    • (2007) Biochemistry , vol.46 , pp. 9551-9563
    • Johnson, E.F.1    Stewart, K.D.2    Woods, K.W.3    Giranda, V.L.4    Luo, Y.5
  • 39
    • 0036479131 scopus 로고    scopus 로고
    • A Golgi-associated PDZ domain protein modulates cystic fibrosis transmembrane regulator plasma membrane expression
    • Cheng J, Moyer BD, Milewski M, Loffing J, Ikeda M, et al. (2002) A Golgi-associated PDZ domain protein modulates cystic fibrosis transmembrane regulator plasma membrane expression. J Biol Chem 277: 3520-3529.
    • (2002) J Biol Chem , vol.277 , pp. 3520-3529
    • Cheng, J.1    Moyer, B.D.2    Milewski, M.3    Loffing, J.4    Ikeda, M.5
  • 40
    • 84876938552 scopus 로고    scopus 로고
    • MAST205 Competes with Cystic Fibrosis Transmembrane Conductance Regulator (CFTR)-associated Ligand for Binding to CFTR to Regulate CFTR-mediated Fluid Transport
    • Ren A, Zhang W, Yarlagadda S, Sinha C, Arora K, et al. (2013) MAST205 Competes with Cystic Fibrosis Transmembrane Conductance Regulator (CFTR)-associated Ligand for Binding to CFTR to Regulate CFTR-mediated Fluid Transport. J Biol Chem 288: 12325-12334.
    • (2013) J Biol Chem , vol.288 , pp. 12325-12334
    • Ren, A.1    Zhang, W.2    Yarlagadda, S.3    Sinha, C.4    Arora, K.5
  • 41
    • 0037334895 scopus 로고    scopus 로고
    • One-thousand-and-one substrates of protein kinase CK2?
    • Meggio F, Pinna LA, (2003) One-thousand-and-one substrates of protein kinase CK2? FASEB J 17: 349-368.
    • (2003) FASEB J , vol.17 , pp. 349-368
    • Meggio, F.1    Pinna, L.A.2
  • 42
    • 18744377185 scopus 로고    scopus 로고
    • The PEST sequence does not contribute to the stability of the cystic fibrosis transmembrane conductance regulator
    • Chen EY, Clarke DM, (2002) The PEST sequence does not contribute to the stability of the cystic fibrosis transmembrane conductance regulator. BMC Biochem 3: 29.
    • (2002) BMC Biochem , vol.3 , pp. 29
    • Chen, E.Y.1    Clarke, D.M.2
  • 43
    • 80053397576 scopus 로고    scopus 로고
    • Unprecedented selectivity and structural determinants of a new class of protein kinase CK2 inhibitors in clinical trials for the treatment of cancer
    • Battistutta R, Cozza G, Pierre F, Papinutto E, Lolli G, et al. (2011) Unprecedented selectivity and structural determinants of a new class of protein kinase CK2 inhibitors in clinical trials for the treatment of cancer. Biochemistry 50: 8478-8488.
    • (2011) Biochemistry , vol.50 , pp. 8478-8488
    • Battistutta, R.1    Cozza, G.2    Pierre, F.3    Papinutto, E.4    Lolli, G.5
  • 44
    • 33750842131 scopus 로고    scopus 로고
    • Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis
    • Wang X, Venable J, LaPointe P, Hutt DM, Koulov AV, et al. (2006) Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis. Cell 127: 803-815.
    • (2006) Cell , vol.127 , pp. 803-815
    • Wang, X.1    Venable, J.2    LaPointe, P.3    Hutt, D.M.4    Koulov, A.V.5
  • 45
    • 84885854021 scopus 로고    scopus 로고
    • Subverted signalling by protein kinase CK2 in ΔF508 CFTR expressing cells. Poster presentation
    • Venerando A, Pagano MA, Cozza G, Arrigoni G, Mehta A, Pinna LA, (2011) Subverted signalling by protein kinase CK2 in ΔF508 CFTR expressing cells. Poster presentation. FEBS Journal 278: 387.
    • (2011) FEBS Journal , vol.278 , pp. 387
    • Venerando, A.1    Pagano, M.A.2    Cozza, G.3    Arrigoni, G.4    Mehta, A.5    Pinna, L.A.6


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