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Volumn 113, Issue 9, 2016, Pages E1152-E1161

Characterization and small-molecule stabilization of the multisite tandem binding between 14-3-3 and the R domain of CFTR

Author keywords

Disordered protein; Multivalency; Protein protein interaction

Indexed keywords

CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; FUSICOCCIN A; NATURAL PRODUCT; PROTEIN 14 3 3; UNCLASSIFIED DRUG;

EID: 84959472285     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1516631113     Document Type: Article
Times cited : (113)

References (54)
  • 1
    • 0024453308 scopus 로고
    • Identification of the cystic fibrosis gene: Chromosome walking and jumping
    • Rommens JM, et al. (1989) Identification of the cystic fibrosis gene: Chromosome walking and jumping. Science 245(4922):1059-1065.
    • (1989) Science , vol.245 , Issue.4922 , pp. 1059-1065
    • Rommens, J.M.1
  • 2
    • 32544435783 scopus 로고    scopus 로고
    • Mechanism of chloride permeation in the cystic fibrosis transmembrane conductance regulator chloride channel
    • Linsdell P (2006) Mechanism of chloride permeation in the cystic fibrosis transmembrane conductance regulator chloride channel. Exp Physiol 91(1):123-129.
    • (2006) Exp Physiol , vol.91 , Issue.1 , pp. 123-129
    • Linsdell, P.1
  • 3
    • 60549083963 scopus 로고    scopus 로고
    • Mechanism of direct bicarbonate transport by the CFTR anion channel
    • Tang L, Fatehi M, Linsdell P (2009) Mechanism of direct bicarbonate transport by the CFTR anion channel. J Cyst Fibros 8(2):115-121.
    • (2009) J Cyst Fibros , vol.8 , Issue.2 , pp. 115-121
    • Tang, L.1    Fatehi, M.2    Linsdell, P.3
  • 6
    • 84901588779 scopus 로고    scopus 로고
    • Genetics of cystic fibrosis: CFTR mutation classifications toward genotype-based CF therapies
    • Fanen P, Wohlhuter-Haddad A, Hinzpeter A (2014) Genetics of cystic fibrosis: CFTR mutation classifications toward genotype-based CF therapies. Int J Biochem Cell Biol 52:94-102.
    • (2014) Int J Biochem Cell Biol , vol.52 , pp. 94-102
    • Fanen, P.1    Wohlhuter-Haddad, A.2    Hinzpeter, A.3
  • 7
    • 33847053615 scopus 로고    scopus 로고
    • Cystic fibrosis transmembrane regulator protein mutations: 'Class' opportunity for novel drug innovation
    • MacDonald KD, McKenzie KR, Zeitlin PL (2007) Cystic fibrosis transmembrane regulator protein mutations: 'Class' opportunity for novel drug innovation. Paediatr Drugs 9(1):1-10.
    • (2007) Paediatr Drugs , vol.9 , Issue.1 , pp. 1-10
    • MacDonald, K.D.1    McKenzie, K.R.2    Zeitlin, P.L.3
  • 8
    • 0036258208 scopus 로고    scopus 로고
    • Cystic fibrosis: A worldwide analysis of CFTR mutations - Correlation with incidence data and application to screening
    • Bobadilla JL, Macek M, Jr, Fine JP, Farrell PM (2002) Cystic fibrosis: A worldwide analysis of CFTR mutations - Correlation with incidence data and application to screening. Hum Mutat 19(6):575-606.
    • (2002) Hum Mutat , vol.19 , Issue.6 , pp. 575-606
    • Bobadilla, J.L.1    Macek, M.2    Fine, J.P.3    Farrell, P.M.4
  • 9
    • 0025242929 scopus 로고
    • Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis
    • Cheng SH, et al. (1990) Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis. Cell 63(4):827-834.
    • (1990) Cell , vol.63 , Issue.4 , pp. 827-834
    • Cheng, S.H.1
  • 10
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 cochaperone CHIP targets immature CFTR for proteasomal degradation
    • Meacham GC, Patterson C, Zhang W, Younger JM, Cyr DM (2001) The Hsc70 cochaperone CHIP targets immature CFTR for proteasomal degradation. Nat Cell Biol 3(1):100-105.
    • (2001) Nat Cell Biol , vol.3 , Issue.1 , pp. 100-105
    • Meacham, G.C.1    Patterson, C.2    Zhang, W.3    Younger, J.M.4    Cyr, D.M.5
  • 11
    • 37549067350 scopus 로고    scopus 로고
    • Low temperature induces the delivery of mature and immature CFTR to the plasma membrane
    • Rennolds J, Boyaka PN, Bellis SL, Cormet-Boyaka E (2008) Low temperature induces the delivery of mature and immature CFTR to the plasma membrane. Biochem Biophys Res Commun 366(4):1025-1029.
    • (2008) Biochem Biophys Res Commun , vol.366 , Issue.4 , pp. 1025-1029
    • Rennolds, J.1    Boyaka, P.N.2    Bellis, S.L.3    Cormet-Boyaka, E.4
  • 12
    • 0034811871 scopus 로고    scopus 로고
    • Control of the cystic fibrosis transmembrane conductance regulator by alphaG(i) and RGS proteins
    • Schreiber R, Kindle P, Benzing T, Walz G, Kunzelmann K (2001) Control of the cystic fibrosis transmembrane conductance regulator by alphaG(i) and RGS proteins. Biochem Biophys Res Commun 281(4):917-923.
    • (2001) Biochem Biophys Res Commun , vol.281 , Issue.4 , pp. 917-923
    • Schreiber, R.1    Kindle, P.2    Benzing, T.3    Walz, G.4    Kunzelmann, K.5
  • 13
    • 84863377687 scopus 로고    scopus 로고
    • Phosphorylation-dependent 14-3-3 protein interactions regulate CFTR biogenesis
    • Liang X, et al. (2012) Phosphorylation-dependent 14-3-3 protein interactions regulate CFTR biogenesis. Mol Biol Cell 23(6):996-1009.
    • (2012) Mol Biol Cell , vol.23 , Issue.6 , pp. 996-1009
    • Liang, X.1
  • 14
    • 24344460521 scopus 로고    scopus 로고
    • 14-3-3 proteins - An update
    • Mhawech P (2005) 14-3-3 proteins - An update. Cell Res 15(4):228-236.
    • (2005) Cell Res , vol.15 , Issue.4 , pp. 228-236
    • Mhawech, P.1
  • 15
    • 0037112329 scopus 로고    scopus 로고
    • Forward transport: 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals
    • O'Kelly I, Butler MH, Zilberberg N, Goldstein SA (2002) Forward transport: 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals. Cell 111(4): 577-588.
    • (2002) Cell , vol.111 , Issue.4 , pp. 577-588
    • O'Kelly, I.1    Butler, M.H.2    Zilberberg, N.3    Goldstein, S.A.4
  • 16
    • 33748741016 scopus 로고    scopus 로고
    • 14-3-3 proteins in membrane protein transport
    • Mrowiec T, Schwappach B (2006) 14-3-3 proteins in membrane protein transport. Biol Chem 387(9):1227-1236.
    • (2006) Biol Chem , vol.387 , Issue.9 , pp. 1227-1236
    • Mrowiec, T.1    Schwappach, B.2
  • 17
    • 84897711870 scopus 로고    scopus 로고
    • Protein intrinsic disorder and network connectivity. The case of 14-3-3 proteins
    • Uhart M, Bustos DM (2014) Protein intrinsic disorder and network connectivity. The case of 14-3-3 proteins. Front Genet 5:10.
    • (2014) Front Genet , vol.5 , pp. 10
    • Uhart, M.1    Bustos, D.M.2
  • 19
    • 69949148383 scopus 로고    scopus 로고
    • Recognition of an intra-chain tandem 14-3-3 binding site within PKCepsilon
    • Kostelecky B, Saurin AT, Purkiss A, Parker PJ, McDonald NQ (2009) Recognition of an intra-chain tandem 14-3-3 binding site within PKCepsilon. EMBO Rep 10(9):983-989.
    • (2009) EMBO Rep , vol.10 , Issue.9 , pp. 983-989
    • Kostelecky, B.1    Saurin, A.T.2    Purkiss, A.3    Parker, P.J.4    McDonald, N.Q.5
  • 20
    • 84888085224 scopus 로고    scopus 로고
    • Regulatory R region of the CFTR chloride channel is a dynamic integrator of phospho-dependent intra- and intermolecular interactions
    • Bozoky Z, et al. (2013) Regulatory R region of the CFTR chloride channel is a dynamic integrator of phospho-dependent intra- and intermolecular interactions. Proc Natl Acad Sci USA 110(47):E4427-E4436.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.47 , pp. E4427-E4436
    • Bozoky, Z.1
  • 21
    • 0031470652 scopus 로고    scopus 로고
    • The structural basis for 14-3-3:phosphopeptide binding specificity
    • Yaffe MB, et al. (1997) The structural basis for 14-3-3:phosphopeptide binding specificity. Cell 91(7):961-971.
    • (1997) Cell , vol.91 , Issue.7 , pp. 961-971
    • Yaffe, M.B.1
  • 22
    • 33846701051 scopus 로고    scopus 로고
    • Structure of a 14-3-3 coordinated hexamer of the plant plasma membrane H+-ATPase by combining X-ray crystallography and electron cryomicroscopy
    • Ottmann C, et al. (2007) Structure of a 14-3-3 coordinated hexamer of the plant plasma membrane H+-ATPase by combining X-ray crystallography and electron cryomicroscopy. Mol Cell 25(3):427-440.
    • (2007) Mol Cell , vol.25 , Issue.3 , pp. 427-440
    • Ottmann, C.1
  • 23
    • 84856315533 scopus 로고    scopus 로고
    • Structural insights of the MLF1/ 14-3-3 interaction
    • Molzan M, Weyand M, Rose R, Ottmann C (2012) Structural insights of the MLF1/ 14-3-3 interaction. FEBS J 279(4):563-571.
    • (2012) FEBS J , vol.279 , Issue.4 , pp. 563-571
    • Molzan, M.1    Weyand, M.2    Rose, R.3    Ottmann, C.4
  • 24
    • 84872513683 scopus 로고    scopus 로고
    • Stabilization and inhibition of proteinprotein interactions: The 14-3-3 case study
    • Milroy LG, Brunsveld L, Ottmann C (2013) Stabilization and inhibition of proteinprotein interactions: The 14-3-3 case study. ACS Chem Biol 8(1):27-35.
    • (2013) ACS Chem Biol , vol.8 , Issue.1 , pp. 27-35
    • Milroy, L.G.1    Brunsveld, L.2    Ottmann, C.3
  • 25
    • 84881493413 scopus 로고    scopus 로고
    • The phytotoxin fusicoccin, a selective stabilizer of 14-3-3 interactions?
    • Camoni L, Visconti S, Aducci P (2013) The phytotoxin fusicoccin, a selective stabilizer of 14-3-3 interactions? IUBMB Life 65(6):513-517.
    • (2013) IUBMB Life , vol.65 , Issue.6 , pp. 513-517
    • Camoni, L.1    Visconti, S.2    Aducci, P.3
  • 26
    • 0037416221 scopus 로고    scopus 로고
    • Structural view of a fungal toxin acting on a 14-3-3 regulatory complex
    • Würtele M, Jelich-Ottmann C, Wittinghofer A, Oecking C (2003) Structural view of a fungal toxin acting on a 14-3-3 regulatory complex. EMBO J 22(5):987-994.
    • (2003) EMBO J , vol.22 , Issue.5 , pp. 987-994
    • Würtele, M.1    Jelich-Ottmann, C.2    Wittinghofer, A.3    Oecking, C.4
  • 27
    • 34547557698 scopus 로고    scopus 로고
    • Correctors of protein trafficking defects identified by a novel high-throughput screening assay
    • Carlile GW, et al. (2007) Correctors of protein trafficking defects identified by a novel high-throughput screening assay. ChemBioChem 8(9):1012-1020.
    • (2007) ChemBioChem , vol.8 , Issue.9 , pp. 1012-1020
    • Carlile, G.W.1
  • 28
    • 84879410121 scopus 로고    scopus 로고
    • Mechanism-based corrector combination restores Δf508- CFTR folding and function
    • Okiyoneda T, et al. (2013) Mechanism-based corrector combination restores ΔF508- CFTR folding and function. Nat Chem Biol 9(7):444-454.
    • (2013) Nat Chem Biol , vol.9 , Issue.7 , pp. 444-454
    • Okiyoneda, T.1
  • 30
    • 77951296388 scopus 로고    scopus 로고
    • Structure of the p53 C-terminus bound to 14-3-3: Implications for stabilization of the p53 tetramer
    • Schumacher B, Mondry J, Thiel P, Weyand M, Ottmann C (2010) Structure of the p53 C-terminus bound to 14-3-3: Implications for stabilization of the p53 tetramer. FEBS Lett 584(8):1443-1448.
    • (2010) FEBS Lett , vol.584 , Issue.8 , pp. 1443-1448
    • Schumacher, B.1    Mondry, J.2    Thiel, P.3    Weyand, M.4    Ottmann, C.5
  • 31
    • 33846999287 scopus 로고    scopus 로고
    • Phosphorylation-independent interaction between 14-3-3 and exoenzyme S: From structure to pathogenesis
    • Ottmann C, et al. (2007) Phosphorylation-independent interaction between 14-3-3 and exoenzyme S: From structure to pathogenesis. EMBO J 26(3):902-913.
    • (2007) EMBO J , vol.26 , Issue.3 , pp. 902-913
    • Ottmann, C.1
  • 32
    • 33751248527 scopus 로고    scopus 로고
    • Structural basis for protein-protein interactions in the 14-3-3 protein family
    • Yang X, et al. (2006) Structural basis for protein-protein interactions in the 14-3-3 protein family. Proc Natl Acad Sci USA 103(46):17237-17242.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.46 , pp. 17237-17242
    • Yang, X.1
  • 33
    • 84891904255 scopus 로고    scopus 로고
    • Parkinson-related LRRK2 mutation R1441C/G/H impairs PKA phosphorylation of LRRK2 and disrupts its interaction with 14-3-3
    • Muda K, et al. (2014) Parkinson-related LRRK2 mutation R1441C/G/H impairs PKA phosphorylation of LRRK2 and disrupts its interaction with 14-3-3. Proc Natl Acad Sci USA 111(1):E34-E43.
    • (2014) Proc Natl Acad Sci USA , vol.111 , Issue.1 , pp. E34-E43
    • Muda, K.1
  • 34
    • 84935077167 scopus 로고    scopus 로고
    • LRRK2 dephosphorylation increases its ubiquitination
    • Zhao J, Molitor TP, Langston JW, Nichols RJ (2015) LRRK2 dephosphorylation increases its ubiquitination. Biochem J 469(1):107-120.
    • (2015) Biochem J , vol.469 , Issue.1 , pp. 107-120
    • Zhao, J.1    Molitor, T.P.2    Langston, J.W.3    Nichols, R.J.4
  • 35
    • 32944458740 scopus 로고    scopus 로고
    • Pim kinases phosphorylate multiple sites on Bad and promote 14-3-3 binding and dissociation from Bcl-XL
    • Macdonald A, et al. (2006) Pim kinases phosphorylate multiple sites on Bad and promote 14-3-3 binding and dissociation from Bcl-XL. BMC Cell Biol 7:1.
    • (2006) BMC Cell Biol , vol.7 , pp. 1
    • Macdonald, A.1
  • 36
    • 0030584088 scopus 로고    scopus 로고
    • Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)
    • Zha J, Harada H, Yang E, Jockel J, Korsmeyer SJ (1996) Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L). Cell 87(4):619-628.
    • (1996) Cell , vol.87 , Issue.4 , pp. 619-628
    • Zha, J.1    Harada, H.2    Yang, E.3    Jockel, J.4    Korsmeyer, S.J.5
  • 37
    • 33646926129 scopus 로고    scopus 로고
    • 14-3-3 proteins: A historic overview
    • Aitken A (2006) 14-3-3 proteins: A historic overview. Semin Cancer Biol 16(3):162-172.
    • (2006) Semin Cancer Biol , vol.16 , Issue.3 , pp. 162-172
    • Aitken, A.1
  • 38
    • 0037138389 scopus 로고    scopus 로고
    • How do 14-3-3 proteins work? - Gatekeeper phosphorylation and the molecular anvil hypothesis
    • Yaffe MB (2002) How do 14-3-3 proteins work? - Gatekeeper phosphorylation and the molecular anvil hypothesis. FEBS Lett 513(1):53-57.
    • (2002) FEBS Lett , vol.513 , Issue.1 , pp. 53-57
    • Yaffe, M.B.1
  • 39
    • 84939417963 scopus 로고    scopus 로고
    • The role of protein-protein interactions in the intracellular traffic of the potassium channels TASK-1 and TASK-3
    • Kilisch M, Lytovchenko O, Schwappach B, Renigunta V, Daut J (2015) The role of protein-protein interactions in the intracellular traffic of the potassium channels TASK-1 and TASK-3. Pflugers Arch 467(5):1105-1120.
    • (2015) Pflugers Arch , vol.467 , Issue.5 , pp. 1105-1120
    • Kilisch, M.1    Lytovchenko, O.2    Schwappach, B.3    Renigunta, V.4    Daut, J.5
  • 40
    • 84875940159 scopus 로고    scopus 로고
    • Rules for the recognition of dilysine retrieval motifs by coatomer
    • Ma W, Goldberg J (2013) Rules for the recognition of dilysine retrieval motifs by coatomer. EMBO J 32(7):926-937.
    • (2013) EMBO J , vol.32 , Issue.7 , pp. 926-937
    • Ma, W.1    Goldberg, J.2
  • 41
    • 0037101946 scopus 로고    scopus 로고
    • Vesicular transport: The core machinery of COPI recruitment and budding
    • Nickel W, Brügger B, Wieland FT (2002) Vesicular transport: The core machinery of COPI recruitment and budding. J Cell Sci 115(Pt 16):3235-3240.
    • (2002) J Cell Sci , vol.115 , pp. 3235-3240
    • Nickel, W.1    Brügger, B.2    Wieland, F.T.3
  • 42
    • 52649145895 scopus 로고    scopus 로고
    • GPS 2.0, a tool to predict kinase-specific phosphorylation sites in hierarchy
    • Xue Y, et al. (2008) GPS 2.0, a tool to predict kinase-specific phosphorylation sites in hierarchy. Mol Cell Proteomics 7(9):1598-1608.
    • (2008) Mol Cell Proteomics , vol.7 , Issue.9 , pp. 1598-1608
    • Xue, Y.1
  • 43
    • 77950872530 scopus 로고    scopus 로고
    • Bioinformatic and experimental survey of 14-3-3-binding sites
    • Johnson C, et al. (2010) Bioinformatic and experimental survey of 14-3-3-binding sites. Biochem J 427(1):69-78.
    • (2010) Biochem J , vol.427 , Issue.1 , pp. 69-78
    • Johnson, C.1
  • 44
    • 84918819267 scopus 로고    scopus 로고
    • Ultrasensitivity part II: Multisite phosphorylation, stoichiometric inhibitors, and positive feedback
    • Ferrell JE, Jr, Ha SH (2014) Ultrasensitivity part II: Multisite phosphorylation, stoichiometric inhibitors, and positive feedback. Trends Biochem Sci 39(11):556-569.
    • (2014) Trends Biochem Sci , vol.39 , Issue.11 , pp. 556-569
    • Ferrell, J.E.1    Ha, S.H.2
  • 45
    • 77952093377 scopus 로고    scopus 로고
    • The scaffold protein Ste5 directly controls a switch-like mating decision in yeast
    • Malleshaiah MK, Shahrezaei V, Swain PS, Michnick SW (2010) The scaffold protein Ste5 directly controls a switch-like mating decision in yeast. Nature 465(7294): 101-105.
    • (2010) Nature , vol.465 , Issue.7294 , pp. 101-105
    • Malleshaiah, M.K.1    Shahrezaei, V.2    Swain, P.S.3    Michnick, S.W.4
  • 47
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • Evans P (2006) Scaling and assessment of data quality. Acta Crystallogr D Biol Crystallogr 62(Pt 1):72-82.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 72-82
    • Evans, P.1
  • 48
    • 0033180582 scopus 로고    scopus 로고
    • Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding
    • Rittinger K, et al. (1999) Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding. Mol Cell 4(2):153-166.
    • (1999) Mol Cell , vol.4 , Issue.2 , pp. 153-166
    • Rittinger, K.1
  • 49
    • 84861730836 scopus 로고    scopus 로고
    • Sequence-specific recognition of a PxLPxI/L motif by an ankyrin repeat tumbler lock
    • Xu C, et al. (2012) Sequence-specific recognition of a PxLPxI/L motif by an ankyrin repeat tumbler lock. Sci Signal 5(226):ra39.
    • (2012) Sci Signal , vol.5 , Issue.226 , pp. ra39
    • Xu, C.1
  • 50
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy AJ, et al. (2007) Phaser crystallographic software. J Appl Crystallogr 40(Pt 4): 658-674.
    • (2007) J Appl Crystallogr , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 51
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Pt 1
    • Emsley P, Cowtan K (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60(Pt 12 Pt 1):2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 52
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams PD, et al. (2010) PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66(Pt 2):213-221.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 53
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-atom structure validation for macromolecular crystallography
    • Chen VB, et al. (2010) MolProbity: all-atom structure validation for macromolecular crystallography. Acta Cryst D66:12-21.
    • (2010) Acta Cryst , vol.D66 , pp. 12-21
    • Chen, V.B.1
  • 54
    • 84879367781 scopus 로고    scopus 로고
    • How good are my data and what is the resolution?
    • Evans PR, Murshudov GN (2013) How good are my data and what is the resolution? Acta Cryst D69:1204-1214.
    • (2013) Acta Cryst , vol.D69 , pp. 1204-1214
    • Evans, P.R.1    Murshudov, G.N.2


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