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Volumn 14, Issue 8, 2007, Pages 738-745

CFTR regulatory region interacts with NBD1 predominantly via multiple transient helices

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEOTIDE BINDING PROTEIN; TRANSMEMBRANE CONDUCTANCE REGULATOR;

EID: 34547652267     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb1278     Document Type: Article
Times cited : (245)

References (50)
  • 1
    • 0024424270 scopus 로고
    • Identification of the cystic fibrosis gene: Cloning and characterization of complementary DNA
    • Riordan, J.R. et al. Identification of the cystic fibrosis gene: cloning and characterization of complementary DNA. Science 245, 1066-1072 (1989).
    • (1989) Science , vol.245 , pp. 1066-1072
    • Riordan, J.R.1
  • 2
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • Dawson, R.J. & Locher, K.P. Structure of a bacterial multidrug ABC transporter. Nature 443, 180-185 (2006).
    • (2006) Nature , vol.443 , pp. 180-185
    • Dawson, R.J.1    Locher, K.P.2
  • 3
    • 0034625153 scopus 로고    scopus 로고
    • A functional R domain from cystic fibrosis transmembrane conductance regulator is predominantly unstructured in solution
    • Ostedgaard, L.S., Baldursson, O., Vermeer, D.W., Welsh, M.J. & Robertson, A.D. A functional R domain from cystic fibrosis transmembrane conductance regulator is predominantly unstructured in solution. Proc. Natl. Acad. Sci. USA 97, 5657-5662 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5657-5662
    • Ostedgaard, L.S.1    Baldursson, O.2    Vermeer, D.W.3    Welsh, M.J.4    Robertson, A.D.5
  • 4
    • 0028328645 scopus 로고
    • Phosphorylation by cAMP-dependent protein kinase causes a conformational change in the R domain of the cystic fibrosis transmembrane conductance regulator
    • Dulhanty, A.M. & Riordan, J.R. Phosphorylation by cAMP-dependent protein kinase causes a conformational change in the R domain of the cystic fibrosis transmembrane conductance regulator. Biochemistry 33, 4072-4079 (1994).
    • (1994) Biochemistry , vol.33 , pp. 4072-4079
    • Dulhanty, A.M.1    Riordan, J.R.2
  • 5
    • 0036342413 scopus 로고    scopus 로고
    • ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer
    • Smith, P.C. et al. ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer. Mol. Cell 10, 139-149 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 139-149
    • Smith, P.C.1
  • 6
    • 10744230777 scopus 로고    scopus 로고
    • Structure of nucleotide-binding domain 1 of the cystic fibrosis transmembrane conductance regulator
    • Lewis, H.A. et al. Structure of nucleotide-binding domain 1 of the cystic fibrosis transmembrane conductance regulator. EMBO J. 23, 282-293 (2004).
    • (2004) EMBO J , vol.23 , pp. 282-293
    • Lewis, H.A.1
  • 7
    • 0027171978 scopus 로고
    • Regulation of the cystic fibrosis transmembrane conductance regulator Cl- channel by negative charge in the R domain
    • Rich, D.P. et al. Regulation of the cystic fibrosis transmembrane conductance regulator Cl- channel by negative charge in the R domain. J. Biol. Chem. 268, 20259-20267 (1993).
    • (1993) J. Biol. Chem , vol.268 , pp. 20259-20267
    • Rich, D.P.1
  • 8
    • 0027311276 scopus 로고
    • Protein kinase A (PKA) still activates CFTR chloride channel after mutagenesis of all 10 PKA consensus phosphorylation sites
    • Chang, X.B. et al. Protein kinase A (PKA) still activates CFTR chloride channel after mutagenesis of all 10 PKA consensus phosphorylation sites. J. Biol. Chem. 268, 11304-11311 (1993).
    • (1993) J. Biol. Chem , vol.268 , pp. 11304-11311
    • Chang, X.B.1
  • 9
    • 0025987020 scopus 로고
    • Phosphorylation of the R domain by cAMP-dependent protein kinase regulates the CFTR chloride channel
    • Cheng, S.H. et al. Phosphorylation of the R domain by cAMP-dependent protein kinase regulates the CFTR chloride channel. Cell 66, 1027-1036 (1991).
    • (1991) Cell , vol.66 , pp. 1027-1036
    • Cheng, S.H.1
  • 10
    • 0030816586 scopus 로고    scopus 로고
    • CFTR activation: Additive effects of stimulatory and inhibitory phosphorylation sites in the R domain
    • Wilkinson, D.J. et al. CFTR activation: additive effects of stimulatory and inhibitory phosphorylation sites in the R domain. Am. J. Physiol. 273, L127-L133 (1997).
    • (1997) Am. J. Physiol , vol.273
    • Wilkinson, D.J.1
  • 11
    • 4143102419 scopus 로고    scopus 로고
    • Dibasic phosphorylation sites in the R domain of CFTR have stimulatory and inhibitory effects on channel activation
    • Vais, H., Zhang, R. & Reenstra, W.W. Dibasic phosphorylation sites in the R domain of CFTR have stimulatory and inhibitory effects on channel activation. Am. J. Physiol. Cell Physiol. 287, C737-C745 (2004).
    • (2004) Am. J. Physiol. Cell Physiol , vol.287
    • Vais, H.1    Zhang, R.2    Reenstra, W.W.3
  • 12
    • 0035910510 scopus 로고    scopus 로고
    • Cystic fibrosis transmembrane conductance regulator Cl- channels with R domain deletions and translocations show phosphorylation-dependent and -independent activity
    • Baldursson, O., Ostedgaard, L.S., Rokhlina, T., Cotten, J.F. & Welsh, M.J. Cystic fibrosis transmembrane conductance regulator Cl- channels with R domain deletions and translocations show phosphorylation-dependent and -independent activity. J. Biol. Chem. 276, 1904-1910 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 1904-1910
    • Baldursson, O.1    Ostedgaard, L.S.2    Rokhlina, T.3    Cotten, J.F.4    Welsh, M.J.5
  • 13
    • 0037151094 scopus 로고    scopus 로고
    • A short segment of the R domain of cystic fibrosis transmembrane conductance regulator contains channel stimulatory and inhibitory activities that are separable by sequence modification
    • Xie, J. et al. A short segment of the R domain of cystic fibrosis transmembrane conductance regulator contains channel stimulatory and inhibitory activities that are separable by sequence modification. J. Biol. Chem. 277, 23019-23027 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 23019-23027
    • Xie, J.1
  • 14
    • 0033817333 scopus 로고    scopus 로고
    • Severed channels probe regulation of gating of cystic fibrosis transmembrane conductance regulator by its cytoplasmic domains
    • Csanady, L. et al. Severed channels probe regulation of gating of cystic fibrosis transmembrane conductance regulator by its cytoplasmic domains. J. Gen. Physiol. 116, 477-500 (2000).
    • (2000) J. Gen. Physiol , vol.116 , pp. 477-500
    • Csanady, L.1
  • 15
    • 0030931648 scopus 로고    scopus 로고
    • Stimulation of CFTR activity by its phosphorylated R domain
    • Winter, M.C. & Welsh, M.J. Stimulation of CFTR activity by its phosphorylated R domain. Nature 389, 294-296 (1997).
    • (1997) Nature , vol.389 , pp. 294-296
    • Winter, M.C.1    Welsh, M.J.2
  • 16
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • Wright, P.E. & Dyson, H.J. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J. Mol. Biol. 293, 321-331 (1999).
    • (1999) J. Mol. Biol , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 17
    • 0035188314 scopus 로고    scopus 로고
    • Sequence complexity of disordered protein
    • Romero, P. et al. Sequence complexity of disordered protein. Proteins 42, 38-48 (2001).
    • (2001) Proteins , vol.42 , pp. 38-48
    • Romero, P.1
  • 20
    • 33748074139 scopus 로고    scopus 로고
    • Intrinsic disorder is a common feature of hub proteins from four eukaryotic interactomes
    • Haynes, C. et al. Intrinsic disorder is a common feature of hub proteins from four eukaryotic interactomes. PLoS Comput. Biol. 2, e100 (2006).
    • (2006) PLoS Comput. Biol , vol.2
    • Haynes, C.1
  • 21
    • 0032936619 scopus 로고    scopus 로고
    • Control of CFTR channel gating by phosphorylation and nucleotide hydrolysis
    • Gadsby, D.C. & Nairn, A.C. Control of CFTR channel gating by phosphorylation and nucleotide hydrolysis. Physiol. Rev. 79, S77-S107 (1999).
    • (1999) Physiol. Rev , vol.79
    • Gadsby, D.C.1    Nairn, A.C.2
  • 22
    • 0034912536 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for elucidation of structure and dynamics in disordered states
    • Dyson, H.J. & Wright, P.E. Nuclear magnetic resonance methods for elucidation of structure and dynamics in disordered states. Methods Enzymol. 339, 258-270 (2001).
    • (2001) Methods Enzymol , vol.339 , pp. 258-270
    • Dyson, H.J.1    Wright, P.E.2
  • 23
    • 0033377656 scopus 로고    scopus 로고
    • Random-coil chemical shifts of phosphorylated amino acids
    • Bienkiewicz, E.A. & Lumb, K.J. Random-coil chemical shifts of phosphorylated amino acids. J. Biomol. NMR 15, 203-206 (1999).
    • (1999) J. Biomol. NMR , vol.15 , pp. 203-206
    • Bienkiewicz, E.A.1    Lumb, K.J.2
  • 24
    • 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, D.C. et al. 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).
    • (1997) Protein Sci , vol.6 , pp. 2436-2445
    • Neville, D.C.1
  • 25
    • 0029838141 scopus 로고    scopus 로고
    • Identification of protein kinase A phosphorylation sites on NBD1 and R domains of CFTR using electrospray mass spectrometry with selective phosphate ion monitoring
    • Townsend, R.R., Lipniunas, P.H., Tulk, B.M. & Verkman, A.S. Identification of protein kinase A phosphorylation sites on NBD1 and R domains of CFTR using electrospray mass spectrometry with selective phosphate ion monitoring. Protein Sci. 5, 1865-1873 (1996).
    • (1996) Protein Sci , vol.5 , pp. 1865-1873
    • Townsend, R.R.1    Lipniunas, P.H.2    Tulk, B.M.3    Verkman, A.S.4
  • 26
    • 33751552347 scopus 로고    scopus 로고
    • Sensitivity of secondary structure propensities to sequence differences between alpha and gamma synuclein: Implications for fibrillation
    • Marsh, J.A., Singh, V.K., Jia, Z. & Forman-Kay, J.D. Sensitivity of secondary structure propensities to sequence differences between alpha and gamma synuclein: implications for fibrillation. Protein Sci. 15, 2795-2804 (2006).
    • (2006) Protein Sci , vol.15 , pp. 2795-2804
    • Marsh, J.A.1    Singh, V.K.2    Jia, Z.3    Forman-Kay, J.D.4
  • 27
    • 0037065734 scopus 로고    scopus 로고
    • Effect of phosphorylation on alpha-helix stability as a function of position
    • Andrew, C.D., Warwicker, J., Jones, G.R. & Doig, A.J. Effect of phosphorylation on alpha-helix stability as a function of position. Biochemistry 41, 1897-1905 (2002).
    • (2002) Biochemistry , vol.41 , pp. 1897-1905
    • Andrew, C.D.1    Warwicker, J.2    Jones, G.R.3    Doig, A.J.4
  • 28
    • 0028282555 scopus 로고
    • Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation
    • Farrow, N.A. et al. Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation. Biochemistry 33, 5984-6003 (1994).
    • (1994) Biochemistry , vol.33 , pp. 5984-6003
    • Farrow, N.A.1
  • 29
    • 0030759665 scopus 로고    scopus 로고
    • Structural and dynamical properties of a denatured protein. Heteronuclear 3D NMR experiments and theoretical simulations of lysozyme in 8 M urea
    • Schwalbe, H. et al. Structural and dynamical properties of a denatured protein. Heteronuclear 3D NMR experiments and theoretical simulations of lysozyme in 8 M urea. Biochemistry 36, 8977-8991 (1997).
    • (1997) Biochemistry , vol.36 , pp. 8977-8991
    • Schwalbe, H.1
  • 30
    • 0026545547 scopus 로고
    • Characterization of the cystic fibrosis transmembrane conductance regulator in a colonocyte cell line
    • Cohn, J.A., Nairn, A.C., Marino, C.R., Melhus, O. & Kole, J. Characterization of the cystic fibrosis transmembrane conductance regulator in a colonocyte cell line. Proc. Natl. Acad. Sci. USA 89, 2340-2344 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 2340-2344
    • Cohn, J.A.1    Nairn, A.C.2    Marino, C.R.3    Melhus, O.4    Kole, J.5
  • 31
    • 0026681083 scopus 로고
    • Phosphorylation of the cystic fibrosis transmembrane conductance regulator
    • Picciotto, M.R., Cohn, J.A., Bertuzzi, G., Greengard, P. & Nairn, A.C. Phosphorylation of the cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 267, 12742-12752 (1992).
    • (1992) J. Biol. Chem , vol.267 , pp. 12742-12752
    • Picciotto, M.R.1    Cohn, J.A.2    Bertuzzi, G.3    Greengard, P.4    Nairn, A.C.5
  • 32
    • 19944432524 scopus 로고    scopus 로고
    • Impact of the deltaF508 mutation in first nucleotide-binding domain of human cystic fibrosis transmembrane conductance regulator on domain folding and structure
    • Lewis, H.A. et al. Impact of the deltaF508 mutation in first nucleotide-binding domain of human cystic fibrosis transmembrane conductance regulator on domain folding and structure. J. Biol. Chem. 280, 1346-1353 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 1346-1353
    • Lewis, H.A.1
  • 34
    • 20844457435 scopus 로고    scopus 로고
    • Preferential phosphorylation of R-domain Serine 768 dampens activation of CFTR channels by PKA
    • Csanady, L. et al. Preferential phosphorylation of R-domain Serine 768 dampens activation of CFTR channels by PKA. J. Gen. Physiol. 125, 171-186 (2005).
    • (2005) J. Gen. Physiol , vol.125 , pp. 171-186
    • Csanady, L.1
  • 35
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson, H.J. & Wright, P.E. Coupling of folding and binding for unstructured proteins. Curr. Opin. Struct. Biol. 12, 54-60 (2002).
    • (2002) Curr. Opin. Struct. Biol , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 36
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson, T. Protein modules and signalling networks. Nature 373, 573-580 (1995).
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 37
    • 2142757231 scopus 로고    scopus 로고
    • Preformed structural elements feature in partner recognition by intrinsically unstructured proteins
    • Fuxreiter, M., Simon, I., Friedrich, P. & Tompa, P. Preformed structural elements feature in partner recognition by intrinsically unstructured proteins. J. Mol. Biol. 338, 1015-1026 (2004).
    • (2004) J. Mol. Biol , vol.338 , pp. 1015-1026
    • Fuxreiter, M.1    Simon, I.2    Friedrich, P.3    Tompa, P.4
  • 38
    • 24944546549 scopus 로고    scopus 로고
    • Coupled folding and binding with alpha-helix-forming molecular recognition elements
    • Oldfield, C.J. et al. Coupled folding and binding with alpha-helix-forming molecular recognition elements. Biochemistry 44, 12454-12470 (2005).
    • (2005) Biochemistry , vol.44 , pp. 12454-12470
    • Oldfield, C.J.1
  • 39
    • 1542314828 scopus 로고    scopus 로고
    • Protein kinase A regulates ATP hydrolysis and dimerization by a cystic fibrosis transmembrane conductance regulator (CFTR) domain
    • Howell, L.D. et al. Protein kinase A regulates ATP hydrolysis and dimerization by a cystic fibrosis transmembrane conductance regulator (CFTR) domain. Biochem. J. 378, 151-159 (2004).
    • (2004) Biochem. J , vol.378 , pp. 151-159
    • Howell, L.D.1
  • 40
    • 33750222000 scopus 로고    scopus 로고
    • In vivo phosphorylation of CFTR promotes formation of a nucleotide-binding domain heterodimer
    • Mense, M. et al. In vivo phosphorylation of CFTR promotes formation of a nucleotide-binding domain heterodimer. EMBO J. 25, 4728-4739 (2006).
    • (2006) EMBO J , vol.25 , pp. 4728-4739
    • Mense, M.1
  • 41
    • 12344263101 scopus 로고    scopus 로고
    • Functional roles of nonconserved structural segments in CFTR's NH2-terminal nucleotide binding domain
    • Csanady, L., Chan, K.W., Nairn, A.C. & Gadsby, D.C. Functional roles of nonconserved structural segments in CFTR's NH2-terminal nucleotide binding domain. J. Gen. Physiol. 125, 43-55 (2005).
    • (2005) J. Gen. Physiol , vol.125 , pp. 43-55
    • Csanady, L.1    Chan, K.W.2    Nairn, A.C.3    Gadsby, D.C.4
  • 42
    • 0030836234 scopus 로고    scopus 로고
    • Function of the R domain in the cystic fibrosis transmembrane conductance regulator chloride channel
    • Ma, J., Zhao, J., Drumm, M.L., Xie, J. & Davis, P.B. Function of the R domain in the cystic fibrosis transmembrane conductance regulator chloride channel. J. Biol. Chem. 272, 28133-28141 (1997).
    • (1997) J. Biol. Chem , vol.272 , pp. 28133-28141
    • Ma, J.1    Zhao, J.2    Drumm, M.L.3    Xie, J.4    Davis, P.B.5
  • 43
    • 0035969559 scopus 로고    scopus 로고
    • Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication
    • Nash, P. et al. Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication. Nature 414, 514-521 (2001).
    • (2001) Nature , vol.414 , pp. 514-521
    • Nash, P.1
  • 44
    • 21744436606 scopus 로고    scopus 로고
    • Variable control of Ets-1 DNA binding by multiple phosphates in an unstructured region
    • Pufall, M.A. et al. Variable control of Ets-1 DNA binding by multiple phosphates in an unstructured region. Science 309, 142-145 (2005).
    • (2005) Science , vol.309 , pp. 142-145
    • Pufall, M.A.1
  • 45
    • 0033569511 scopus 로고    scopus 로고
    • CFTR chloride channel regulation by an interdomain interaction
    • Naren, A.P. CFTR chloride channel regulation by an interdomain interaction. Science 286, 544-548 (1999).
    • (1999) Science , vol.286 , pp. 544-548
    • Naren, A.P.1
  • 46
    • 2342449944 scopus 로고    scopus 로고
    • Gating of CFTR by the STAS domain of SLC26 transporters
    • Ko, S.B. et al. Gating of CFTR by the STAS domain of SLC26 transporters. Nat. Cell Biol. 6, 343-350 (2004).
    • (2004) Nat. Cell Biol , vol.6 , pp. 343-350
    • Ko, S.B.1
  • 47
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
    • Sattler, M., Schleucher, J. & Griesinger, C. Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Prog. Nucl. Magn. Reson. Spectrosc. 34, 93-158 (1999).
    • (1999) Prog. Nucl. Magn. Reson. Spectrosc , vol.34 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Griesinger, C.3
  • 48
    • 0036189601 scopus 로고    scopus 로고
    • Multidimensional NMR methods for protein structure determination
    • Kanelis, V., Forman-Kay, J.D. & Kay, L.E. Multidimensional NMR methods for protein structure determination. IUBMB Life 52, 291-302 (2001).
    • (2001) IUBMB Life , vol.52 , pp. 291-302
    • Kanelis, V.1    Forman-Kay, J.D.2    Kay, L.E.3
  • 49
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F. et al. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293 (1995).
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1
  • 50
    • 34249765651 scopus 로고
    • NMRView - a computer program for the visualization and analysis of NMR data
    • Johnson, B.A. & Blevins, R.A. NMRView - a computer program for the visualization and analysis of NMR data. J. Biol. NMR 4, 603-614 (1994).
    • (1994) J. Biol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2


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