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Volumn 54, Issue 14, 2015, Pages 2303-2313

Role of positively charged residues of the second transmembrane domain in the ion transport activity and conformation of human uncoupling protein-2

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; AMINO ACIDS; BIOSYNTHESIS; CELL MEMBRANES; CHLORINE COMPOUNDS; FATTY ACIDS; LIPOSOMES; MITOCHONDRIA; NEGATIVE IONS; NUCLEOTIDES; PROTEINS; PROTONS;

EID: 84927740393     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.5b00177     Document Type: Article
Times cited : (9)

References (49)
  • 2
    • 34948890043 scopus 로고    scopus 로고
    • Mitochondrial uncoupling proteins - What is their physiological role?
    • Echtay, K. S. (2007) Mitochondrial uncoupling proteins-what is their physiological role? Free Radical Biol. Med. 43, 1351-1371
    • (2007) Free Radical Biol. Med. , vol.43 , pp. 1351-1371
    • Echtay, K.S.1
  • 3
    • 27644448810 scopus 로고    scopus 로고
    • Mitochondrial uncoupling proteins in the CNS: In support of function and survival
    • Andrews, Z. B., Diano, S., and Horvath, T. L. (2005) Mitochondrial uncoupling proteins in the CNS: in support of function and survival Nat. Rev. Neurosci. 6, 829-840
    • (2005) Nat. Rev. Neurosci. , vol.6 , pp. 829-840
    • Andrews, Z.B.1    Diano, S.2    Horvath, T.L.3
  • 4
    • 0017927437 scopus 로고
    • The identification of the component in the inner membrane of brown adipose tissue mitochondria responsible for regulating energy dissipation
    • Nicholls, D. G., Bernson, V. S., and Heaton, G. M. (1978) The identification of the component in the inner membrane of brown adipose tissue mitochondria responsible for regulating energy dissipation Exp. Suppl. 32, 89-93
    • (1978) Exp. Suppl. , vol.32 , pp. 89-93
    • Nicholls, D.G.1    Bernson, V.S.2    Heaton, G.M.3
  • 5
    • 0035852755 scopus 로고    scopus 로고
    • Uncoupling proteins 2 and 3 are highly active H+ transporters and highly nucleotide sensitive when activated by coenzyme Q (ubiquinone)
    • Echtay, K. S., Winkler, E., Frischmuth, K., and Klingenberg, M. (2001) Uncoupling proteins 2 and 3 are highly active H+ transporters and highly nucleotide sensitive when activated by coenzyme Q (ubiquinone) Proc. Natl. Acad. Sci. U.S.A. 98, 1416-1421
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 1416-1421
    • Echtay, K.S.1    Winkler, E.2    Frischmuth, K.3    Klingenberg, M.4
  • 7
    • 0034990987 scopus 로고    scopus 로고
    • Increased uncoupling protein-2 levels in beta-cells are associated with impaired glucose-stimulated insulin secretion: Mechanism of action
    • Chan, C. B., De Leo, D., Joseph, J. W., McQuaid, T. S., Ha, X. F., Xu, F., Tsushima, R. G., Pennefather, P. S., Salapatek, A. M., and Wheeler, M. B. (2001) Increased uncoupling protein-2 levels in beta-cells are associated with impaired glucose-stimulated insulin secretion: mechanism of action Diabetes 50, 1302-1310
    • (2001) Diabetes , vol.50 , pp. 1302-1310
    • Chan, C.B.1    De Leo, D.2    Joseph, J.W.3    McQuaid, T.S.4    Ha, X.F.5    Xu, F.6    Tsushima, R.G.7    Pennefather, P.S.8    Salapatek, A.M.9    Wheeler, M.B.10
  • 8
    • 0035282920 scopus 로고    scopus 로고
    • Uncoupling proteins: The issues from a biochemist point of view
    • Klingenberg, M. and Echtay, K. S. (2001) Uncoupling proteins: the issues from a biochemist point of view Biochim. Biophys. Acta 1504, 128-143
    • (2001) Biochim. Biophys. Acta , vol.1504 , pp. 128-143
    • Klingenberg, M.1    Echtay, K.S.2
  • 9
    • 79961168437 scopus 로고    scopus 로고
    • Mitochondrial uncoupling protein 2 structure determined by NMR molecular fragment searching
    • Berardi, M. J., Shih, W. M., Harrison, S. C., and Chou, J. J. (2011) Mitochondrial uncoupling protein 2 structure determined by NMR molecular fragment searching Nature 476, 109-113
    • (2011) Nature , vol.476 , pp. 109-113
    • Berardi, M.J.1    Shih, W.M.2    Harrison, S.C.3    Chou, J.J.4
  • 10
    • 0038168520 scopus 로고    scopus 로고
    • Reconstitution of recombinant uncoupling proteins UCP1, -2, and -3 have similar affinities for ATP and are unaffected by coenzyme Q10
    • Jabůrek, M. and Garlid, K. D. (2003) Reconstitution of recombinant uncoupling proteins UCP1, -2, and -3 have similar affinities for ATP and are unaffected by coenzyme Q10 J. Biol. Chem. 278, 25825-25831
    • (2003) J. Biol. Chem. , vol.278 , pp. 25825-25831
    • Jabůrek, M.1    Garlid, K.D.2
  • 11
    • 0030039607 scopus 로고    scopus 로고
    • On the mechanism of fatty acid-induced proton transport by mitochondrial uncoupling protein
    • Garlid, K. D., Orosz, D. E., Modriansky, M., Vassanelli, S., and Jezek, P. (1996) On the mechanism of fatty acid-induced proton transport by mitochondrial uncoupling protein J. Biol. Chem. 271, 2615-2620
    • (1996) J. Biol. Chem. , vol.271 , pp. 2615-2620
    • Garlid, K.D.1    Orosz, D.E.2    Modriansky, M.3    Vassanelli, S.4    Jezek, P.5
  • 12
    • 0034724170 scopus 로고    scopus 로고
    • Site-directed mutagenesis identifies residues in uncoupling protein (UCP1) involved in three different functions
    • Echtay, K. S., Winkler, E., Bienengraeber, M., and Klingenberg, M. (2000) Site-directed mutagenesis identifies residues in uncoupling protein (UCP1) involved in three different functions Biochemistry 39, 3311-3317
    • (2000) Biochemistry , vol.39 , pp. 3311-3317
    • Echtay, K.S.1    Winkler, E.2    Bienengraeber, M.3    Klingenberg, M.4
  • 13
    • 0035340729 scopus 로고    scopus 로고
    • Role of intrahelical arginine residues in functional properties of uncoupling protein (UCP1)
    • Echtay, K. S., Bienengraeber, M., and Klingenberg, M. (2001) Role of intrahelical arginine residues in functional properties of uncoupling protein (UCP1) Biochemistry 40, 5243-5248
    • (2001) Biochemistry , vol.40 , pp. 5243-5248
    • Echtay, K.S.1    Bienengraeber, M.2    Klingenberg, M.3
  • 14
    • 0030479543 scopus 로고    scopus 로고
    • Chloride channel properties of the uncoupling protein from brown adipose tissue mitochondria: A patch-clamp study
    • Huang, S. G. and Klingenberg, M. (1996) Chloride channel properties of the uncoupling protein from brown adipose tissue mitochondria: a patch-clamp study Biochemistry 35, 16806-16814
    • (1996) Biochemistry , vol.35 , pp. 16806-16814
    • Huang, S.G.1    Klingenberg, M.2
  • 15
    • 84867564026 scopus 로고    scopus 로고
    • Mechanism of fatty-acid-dependent UCP1 uncoupling in brown fat mitochondria
    • Fedorenko, A., Lishko, P. V., and Kirichok, Y. (2012) Mechanism of fatty-acid-dependent UCP1 uncoupling in brown fat mitochondria Cell 151, 400-413
    • (2012) Cell , vol.151 , pp. 400-413
    • Fedorenko, A.1    Lishko, P.V.2    Kirichok, Y.3
  • 16
    • 7544231406 scopus 로고    scopus 로고
    • Second transmembrane domain of human uncoupling protein 2 is essential for its anion channel formation
    • Yamaguchi, H., Jelokhani-Niaraki, M., and Kodama, H. (2004) Second transmembrane domain of human uncoupling protein 2 is essential for its anion channel formation FEBS Lett. 577, 299-304
    • (2004) FEBS Lett. , vol.577 , pp. 299-304
    • Yamaguchi, H.1    Jelokhani-Niaraki, M.2    Kodama, H.3
  • 17
    • 34248559599 scopus 로고    scopus 로고
    • Gene splicing and mutagenesis by PCR-driven overlap extension
    • Heckman, K. L. and Pease, L. R. (2007) Gene splicing and mutagenesis by PCR-driven overlap extension Nat. Protoc. 2, 924-932
    • (2007) Nat. Protoc. , vol.2 , pp. 924-932
    • Heckman, K.L.1    Pease, L.R.2
  • 18
    • 84861134135 scopus 로고    scopus 로고
    • Toward understanding the mechanism of ion transport activity of neuronal uncoupling proteins UCP2, UCP4, and UCP5
    • Hoang, T., Smith, M. D., and Jelokhani-Niaraki, M. (2012) Toward understanding the mechanism of ion transport activity of neuronal uncoupling proteins UCP2, UCP4, and UCP5 Biochemistry 51, 4004-4014
    • (2012) Biochemistry , vol.51 , pp. 4004-4014
    • Hoang, T.1    Smith, M.D.2    Jelokhani-Niaraki, M.3
  • 19
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • Whitmore, L. and Wallace, B. A. (2004) DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data Nucleic Acids Res. 32, W668-673
    • (2004) Nucleic Acids Res. , vol.32 , pp. 668-673
    • Whitmore, L.1    Wallace, B.A.2
  • 20
    • 33747855587 scopus 로고    scopus 로고
    • A reference database for circular dichroism spectroscopy covering fold and secondary structure space
    • Lees, J. G., Miles, A. J., Wien, F., and Wallace, B. A. (2006) A reference database for circular dichroism spectroscopy covering fold and secondary structure space Bioinformatics. 22, 1955-1962
    • (2006) Bioinformatics. , vol.22 , pp. 1955-1962
    • Lees, J.G.1    Miles, A.J.2    Wien, F.3    Wallace, B.A.4
  • 22
    • 65449188232 scopus 로고    scopus 로고
    • Jalview Version 2-A multiple sequence alignment editor and analysis workbench
    • Waterhouse, A. M., Procter, J. B., Martin, D. M. A., Clamp, M., and Barton, G. J. (2009) Jalview Version 2-a multiple sequence alignment editor and analysis workbench Bioinformatics 25, 1189-1191
    • (2009) Bioinformatics , vol.25 , pp. 1189-1191
    • Waterhouse, A.M.1    Procter, J.B.2    Martin, D.M.A.3    Clamp, M.4    Barton, G.J.5
  • 23
    • 0012293235 scopus 로고    scopus 로고
    • DeLano Scientific, San Carlos, CA
    • DeLano, W. L. (2002) PyMOL; DeLano Scientific, San Carlos, CA.
    • (2002) PyMOL
    • Delano, W.L.1
  • 24
    • 34547559704 scopus 로고    scopus 로고
    • PDB2PQR: Expanding and upgrading automated preparation of biomolecular structures for molecular simulations
    • Dolinsky, T. J., Czodrowski, P., Li, H., Nielsen, J. E., Jensen, J. H., Klebe, G., and Baker, N. A. (2007) PDB2PQR: expanding and upgrading automated preparation of biomolecular structures for molecular simulations Nucleic Acids Res. 35, W522-525
    • (2007) Nucleic Acids Res. , vol.35 , pp. 522-525
    • Dolinsky, T.J.1    Czodrowski, P.2    Li, H.3    Nielsen, J.E.4    Jensen, J.H.5    Klebe, G.6    Baker, N.A.7
  • 25
    • 3242886771 scopus 로고    scopus 로고
    • PDB2PQR: An automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations
    • Dolinsky, T. J., Nielsen, J. E., McCammon, J. A., and Baker, N. A. (2004) PDB2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations Nucleic Acids Res. 32, W665-667
    • (2004) Nucleic Acids Res. , vol.32 , pp. 665-667
    • Dolinsky, T.J.1    Nielsen, J.E.2    McCammon, J.A.3    Baker, N.A.4
  • 27
    • 0021755639 scopus 로고
    • Differential light scattering and absorption flattening optical effects are minimal in the circular dichroism spectra of small unilamellar vesicles
    • Mao, D. and Wallace, B. A. (1984) Differential light scattering and absorption flattening optical effects are minimal in the circular dichroism spectra of small unilamellar vesicles Biochemistry 23, 2667-2673
    • (1984) Biochemistry , vol.23 , pp. 2667-2673
    • Mao, D.1    Wallace, B.A.2
  • 28
    • 74949093836 scopus 로고    scopus 로고
    • A comparative study on conformation and ligand binding of the neuronal uncoupling proteins
    • Ivanova, M. V., Hoang, T., McSorley, F. R., Krnac, G., Smith, M. D., and Jelokhani-Niaraki, M. (2009) A comparative study on conformation and ligand binding of the neuronal uncoupling proteins Biochemistry 49, 512-521
    • (2009) Biochemistry , vol.49 , pp. 512-521
    • Ivanova, M.V.1    Hoang, T.2    McSorley, F.R.3    Krnac, G.4    Smith, M.D.5    Jelokhani-Niaraki, M.6
  • 29
    • 84890928961 scopus 로고    scopus 로고
    • Expression, folding and proton transport activity of human uncoupling protein-1 (UCP1) in lipid membranes: Evidence for associated functional forms
    • Hoang, T., Smith, M. D., and Jelokhani-Niaraki, M. (2013) Expression, folding and proton transport activity of human uncoupling protein-1 (UCP1) in lipid membranes: evidence for associated functional forms J. Biol. Chem. 288, 36244-36258
    • (2013) J. Biol. Chem. , vol.288 , pp. 36244-36258
    • Hoang, T.1    Smith, M.D.2    Jelokhani-Niaraki, M.3
  • 30
    • 0027265825 scopus 로고
    • Conformational intermediates in the folding of a coiled-coil model peptide of the N-terminus of tropomyosin and alpha alpha-tropomyosin
    • Greenfield, N. J. and Hitchcock-DeGregori, S. E. (1993) Conformational intermediates in the folding of a coiled-coil model peptide of the N-terminus of tropomyosin and alpha alpha-tropomyosin Protein Sci. 2, 1263-1273
    • (1993) Protein Sci. , vol.2 , pp. 1263-1273
    • Greenfield, N.J.1    Hitchcock-Degregori, S.E.2
  • 31
    • 0025689272 scopus 로고
    • The effect of conformation on the CD of interacting helices: A theoretical study of tropomyosin
    • Cooper, T. M. and Woody, R. W. (1990) The effect of conformation on the CD of interacting helices: a theoretical study of tropomyosin Biopolymers 30, 657-676
    • (1990) Biopolymers , vol.30 , pp. 657-676
    • Cooper, T.M.1    Woody, R.W.2
  • 32
    • 0034700255 scopus 로고    scopus 로고
    • PH-dependent tetramerization and amantadine binding of the transmembrane helix of M2 from the influenza A virus
    • Salom, D., Hill, B. R., Lear, J. D., and DeGrado, W. F. (2000) pH-dependent tetramerization and amantadine binding of the transmembrane helix of M2 from the influenza A virus Biochemistry 39, 14160-14170
    • (2000) Biochemistry , vol.39 , pp. 14160-14170
    • Salom, D.1    Hill, B.R.2    Lear, J.D.3    Degrado, W.F.4
  • 34
    • 47749085530 scopus 로고    scopus 로고
    • Electrostatic funneling of substrate in mitochondrial inner membrane carriers
    • Wang, Y. and Tajkhorshid, E. (2008) Electrostatic funneling of substrate in mitochondrial inner membrane carriers Proc. Natl. Acad. Sci. U. S. A. 105, 9598-9603
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 9598-9603
    • Wang, Y.1    Tajkhorshid, E.2
  • 35
    • 77952741625 scopus 로고    scopus 로고
    • Mitochondrial chloride channels - What are they for?
    • Tomaskova, Z. and Ondrias, K. (2010) Mitochondrial chloride channels-What are they for? FEBS Lett. 584, 2085-2092
    • (2010) FEBS Lett. , vol.584 , pp. 2085-2092
    • Tomaskova, Z.1    Ondrias, K.2
  • 37
  • 39
    • 0020477232 scopus 로고
    • The mitochondrial phosphate carrier has an essential requirement for cardiolipin
    • Kadenbach, B., Mende, P., Kolbe, H. V., Stipani, I., and Palmieri, F. (1982) The mitochondrial phosphate carrier has an essential requirement for cardiolipin FEBS Lett. 139, 109-112
    • (1982) FEBS Lett. , vol.139 , pp. 109-112
    • Kadenbach, B.1    Mende, P.2    Kolbe, H.V.3    Stipani, I.4    Palmieri, F.5
  • 41
    • 79955025448 scopus 로고    scopus 로고
    • Cardiolipin microdomains localize to negatively curved regions of Escherichia coli membranes
    • Renner, L. D. and Weibel, D. B. (2011) Cardiolipin microdomains localize to negatively curved regions of Escherichia coli membranes Proc. Natl. Acad. Sci. U. S. A. 108, 6264-6269
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 6264-6269
    • Renner, L.D.1    Weibel, D.B.2
  • 42
    • 56649103828 scopus 로고    scopus 로고
    • The mechanism of transport by mitochondrial carriers based on analysis of symmetry
    • Robinson, A. J., Overy, C., and Kunji, E. R. S. (2008) The mechanism of transport by mitochondrial carriers based on analysis of symmetry Proc. Natl. Acad. Sci. U. S. A. 105, 17766-17771
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 17766-17771
    • Robinson, A.J.1    Overy, C.2    Kunji, E.R.S.3
  • 43
    • 0034711953 scopus 로고    scopus 로고
    • The GxxxG motif: A framework for transmembrane helix-helix association
    • Russ, W. P. and Engelman, D. M. (2000) The GxxxG motif: a framework for transmembrane helix-helix association J. Mol. Biol. 296, 911-919
    • (2000) J. Mol. Biol. , vol.296 , pp. 911-919
    • Russ, W.P.1    Engelman, D.M.2
  • 45
    • 69249091013 scopus 로고    scopus 로고
    • Structural polymorphism and multifunctionality of myelin basic protein
    • Harauz, G., Ladizhansky, V., and Boggs, J. M. (2009) Structural polymorphism and multifunctionality of myelin basic protein Biochemistry 48, 8094-8104
    • (2009) Biochemistry , vol.48 , pp. 8094-8104
    • Harauz, G.1    Ladizhansky, V.2    Boggs, J.M.3
  • 46
    • 0242490833 scopus 로고    scopus 로고
    • Assembly of TolC, a structurally unique and multifunctional outer membrane protein of e scherichia coli K-12
    • Werner, J., Augustus, A. M., and Misra, R. (2003) Assembly of TolC, a structurally unique and multifunctional outer membrane protein of E scherichia coli K-12 J. Bacteriol. 185, 6540-6547
    • (2003) J. Bacteriol. , vol.185 , pp. 6540-6547
    • Werner, J.1    Augustus, A.M.2    Misra, R.3
  • 47
    • 47249145524 scopus 로고    scopus 로고
    • Plant inner membrane anion channel (PIMAC) function in plant mitochondria
    • Laus, M. N., Soccio, M., Trono, D., Cattivelli, L., and Pastore, D. (2008) Plant inner membrane anion channel (PIMAC) function in plant mitochondria Plant Cell Physiol. 49, 1039-1055
    • (2008) Plant Cell Physiol. , vol.49 , pp. 1039-1055
    • Laus, M.N.1    Soccio, M.2    Trono, D.3    Cattivelli, L.4    Pastore, D.5
  • 48
    • 0027945163 scopus 로고
    • The reconstituted ADP/ATP carrier can mediate H+ transport by free fatty acids, which is further stimulated by mersalyl
    • Brustovetsky, N. and Klingenberg, M. (1994) The reconstituted ADP/ATP carrier can mediate H+ transport by free fatty acids, which is further stimulated by mersalyl J. Biol. Chem. 269, 27329-27336
    • (1994) J. Biol. Chem. , vol.269 , pp. 27329-27336
    • Brustovetsky, N.1    Klingenberg, M.2
  • 49
    • 33947630244 scopus 로고    scopus 로고
    • Polyunsaturated fatty acids activate human uncoupling proteins 1 and 2 in planar lipid bilayers
    • Beck, V., Jaburek, M., Demina, T., Rupprecht, A., Porter, R. K., Jezek, P., and Pohl, E. E. (2007) Polyunsaturated fatty acids activate human uncoupling proteins 1 and 2 in planar lipid bilayers FASEB J. 21, 1137-1144
    • (2007) FASEB J. , vol.21 , pp. 1137-1144
    • Beck, V.1    Jaburek, M.2    Demina, T.3    Rupprecht, A.4    Porter, R.K.5    Jezek, P.6    Pohl, E.E.7


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