메뉴 건너뛰기




Volumn 288, Issue 1, 2013, Pages 111-121

Dual function of mitochondrial Nm23-H4 protein in phosphotransfer and intermembrane lipid transfer: A cardiolipin-dependent switch

Author keywords

[No Author keywords available]

Indexed keywords

ANIONIC PHOSPHOLIPIDS; ANNEXINS; APOPTOTIC SIGNALING; CARDIOLIPINS; CASPASES; COMPLEX FORMATIONS; CYTOCHROME C; CYTOSOLS; DUAL FUNCTION; HELA CELL; IN-VITRO; IN-VIVO; INNER MITOCHONDRIAL MEMBRANES; INTERMEMBRANE SPACE; INTERMEMBRANES; LIPID DISTRIBUTIONS; LIPID TRANSFER; LIQUID CHROMATOGRAPHY-MASS SPECTROMETRY; MUTANT ENZYMES; NUCLEOSIDE TRIPHOSPHATES; NUCLEOSIDE-DIPHOSPHATE KINASE; OUTER MITOCHONDRIAL MEMBRANES; PHOSPHATIDYLCHOLINE; PHOSPHO-TRANSFER; RAT LIVERS; TRANSFER MECHANISMS; WILD TYPES; WILD-TYPE ENZYMES;

EID: 84872094603     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.408633     Document Type: Article
Times cited : (91)

References (49)
  • 1
    • 84858376953 scopus 로고    scopus 로고
    • Mitochondria. In sickness and in health
    • Nunnari, J., and Suomalainen, A. (2012) Mitochondria. In sickness and in health. Cell 148, 1145-1159
    • (2012) Cell , vol.148 , pp. 1145-1159
    • Nunnari, J.1    Suomalainen, A.2
  • 2
    • 84859433796 scopus 로고    scopus 로고
    • Non-apoptotic functions of apoptosis-regulatory proteins
    • Galluzzi, L., Kepp, O., Trojel-Hansen, C., and Kroemer, G. (2012) Non-apoptotic functions of apoptosis-regulatory proteins. EMBO Rep. 13, 322-330
    • (2012) EMBO Rep. , vol.13 , pp. 322-330
    • Galluzzi, L.1    Kepp, O.2    Trojel-Hansen, C.3    Kroemer, G.4
  • 4
    • 79953745644 scopus 로고    scopus 로고
    • The multiple functions of cytochrome c and their regulation in life and death decisions of the mammalian cell. From respiration to apoptosis
    • Hüttemann, M., Pecina, P., Rainbolt, M., Sanderson, T. H., Kagan, V. E., Samavati, L., Doan, J. W., and Lee, I. (2011) The multiple functions of cytochrome c and their regulation in life and death decisions of the mammalian cell. From respiration to apoptosis. Mitochondrion 11, 369-381
    • (2011) Mitochondrion , vol.11 , pp. 369-381
    • Hüttemann, M.1    Pecina, P.2    Rainbolt, M.3    Sanderson, T.H.4    Kagan, V.E.5    Samavati, L.6    Doan, J.W.7    Lee, I.8
  • 6
    • 33846023675 scopus 로고    scopus 로고
    • Novel lipid transfer property of two mitochondrial proteins that bridge the inner and outer membranes
    • DOI 10.1529/biophysj.106.092353
    • Epand, R. F., Schlattner, U., Wallimann, T., Lacombe, M. L., and Epand, R. M. (2007) Novel lipid transfer property of two mitochondrial proteins that bridge the inner and outer membranes. Biophys. J. 92, 126-137 (Pubitemid 46048422)
    • (2007) Biophysical Journal , vol.92 , Issue.1 , pp. 126-137
    • Epand, R.F.1    Schlattner, U.2    Wallimann, T.3    Lacombe, M.-L.4    Epand, R.M.5
  • 7
    • 0030976107 scopus 로고    scopus 로고
    • nm23-H4, a new member of the family of human nm23/nucleoside diphosphate kinase genes localised on chromosome 16p13
    • DOI 10.1007/s004390050405
    • Milon, L., Rousseau-Merck, M. F., Munier, A., Erent, M., Lascu, I., Capeau, J., and Lacombe, M. L. (1997) nm23-H4, a new member of the family of human nm23/nucleoside diphosphate kinase genes localized on chromosome 16p13. Hum. Genet. 99, 550-557 (Pubitemid 27152109)
    • (1997) Human Genetics , vol.99 , Issue.4 , pp. 550-557
    • Milon, L.1    Rousseau-Merck, M.-F.2    Munier, A.3    Erent, M.4    Lascu, L.5    Capeau, J.6    Lacombe, M.-L.7
  • 8
    • 54449101307 scopus 로고    scopus 로고
    • The nucleoside diphosphate kinase D (NM23-H4) binds the inner mitochondrial membrane with high affinity to cardiolipin and couples nucleotide transfer with respiration
    • Tokarska-Schlattner, M., Boissan, M., Munier, A., Borot, C., Mailleau, C., Speer, O., Schlattner, U., and Lacombe, M. L. (2008) The nucleoside diphosphate kinase D (NM23-H4) binds the inner mitochondrial membrane with high affinity to cardiolipin and couples nucleotide transfer with respiration. J. Biol. Chem. 283, 26198-26207
    • (2008) J. Biol. Chem. , vol.283 , pp. 26198-26207
    • Tokarska-Schlattner, M.1    Boissan, M.2    Munier, A.3    Borot, C.4    Mailleau, C.5    Speer, O.6    Schlattner, U.7    Lacombe, M.L.8
  • 9
    • 67349166562 scopus 로고    scopus 로고
    • Interaction of NDPK-D with cardiolipin-containing membranes. Structural basis and implications for mitochondrial physiology
    • Lacombe, M. L., Tokarska-Schlattner, M., Epand, R. F., Boissan, M., Epand, R. M., and Schlattner, U. (2009) Interaction of NDPK-D with cardiolipin-containing membranes. Structural basis and implications for mitochondrial physiology. Biochimie 91, 779-783
    • (2009) Biochimie , vol.91 , pp. 779-783
    • Lacombe, M.L.1    Tokarska-Schlattner, M.2    Epand, R.F.3    Boissan, M.4    Epand, R.M.5    Schlattner, U.6
  • 13
    • 77953123212 scopus 로고    scopus 로고
    • The BH3-only Bnip3 binds to the dynamin Opa1 to promote mitochondrial fragmentation and apoptosis by distinct mechanisms
    • Landes, T., Emorine, L. J., Courilleau, D., Rojo, M., Belenguer, P., and Arnauné-Pelloquin, L. (2010) The BH3-only Bnip3 binds to the dynamin Opa1 to promote mitochondrial fragmentation and apoptosis by distinct mechanisms. EMBO Rep. 11, 459-465
    • (2010) EMBO Rep. , vol.11 , pp. 459-465
    • Landes, T.1    Emorine, L.J.2    Courilleau, D.3    Rojo, M.4    Belenguer, P.5    Arnauné-Pelloquin, L.6
  • 14
    • 83055173020 scopus 로고    scopus 로고
    • Overexpression of optic atrophy 1 protein increases cisplatin resistance via inactivation of caspase-dependent apoptosis in lung adenocarcinoma cells
    • Fang, H. Y., Chen, C. Y., Chiou, S. H., Wang, Y. T., Lin, T. Y., Chang, H. W., Chiang, I. P., Lan, K. J., and Chow, K. C. (2012) Overexpression of optic atrophy 1 protein increases cisplatin resistance via inactivation of caspase-dependent apoptosis in lung adenocarcinoma cells. Hum. Pathol. 43, 105-114
    • (2012) Hum. Pathol. , vol.43 , pp. 105-114
    • Fang, H.Y.1    Chen, C.Y.2    Chiou, S.H.3    Wang, Y.T.4    Lin, T.Y.5    Chang, H.W.6    Chiang, I.P.7    Lan, K.J.8    Chow, K.C.9
  • 16
    • 84855581252 scopus 로고    scopus 로고
    • The complexity of cardiolipin in health and disease
    • Claypool, S. M., and Koehler, C. M. (2012) The complexity of cardiolipin in health and disease. Trends Biochem. Sci. 37, 32-41
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 32-41
    • Claypool, S.M.1    Koehler, C.M.2
  • 17
    • 78651287877 scopus 로고    scopus 로고
    • Making heads or tails of phospholipids in mitochondria
    • Osman, C., Voelker, D. R., and Langer, T. (2011) Making heads or tails of phospholipids in mitochondria. J. Cell. Biol. 192, 7-16
    • (2011) J. Cell. Biol. , vol.192 , pp. 7-16
    • Osman, C.1    Voelker, D.R.2    Langer, T.3
  • 18
    • 0036850312 scopus 로고    scopus 로고
    • Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane
    • DOI 10.1016/S0092-8674(02)01036-X
    • Kuwana, T., Mackey, M. R., Perkins, G., Ellisman, M. H., Latterich, M., Schneiter, R., Green, D. R., and Newmeyer, D. D. (2002) Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane. Cell 111, 331-342 (Pubitemid 35341388)
    • (2002) Cell , vol.111 , Issue.3 , pp. 331-342
    • Kuwana, T.1    Mackey, M.R.2    Perkins, G.3    Ellisman, M.H.4    Latterich, M.5    Schneiter, R.6    Green, D.R.7    Newmeyer, D.D.8
  • 21
    • 67849133020 scopus 로고    scopus 로고
    • Cardiolipin-enriched raft-like microdomains are essential activating platforms for apoptotic signals on mitochondria
    • Sorice, M., Manganelli, V., Matarrese, P., Tinari, A., Misasi, R., Malorni, W., and Garofalo, T. (2009) Cardiolipin-enriched raft-like microdomains are essential activating platforms for apoptotic signals on mitochondria. FEBS Lett. 583, 2447-2450
    • (2009) FEBS Lett. , vol.583 , pp. 2447-2450
    • Sorice, M.1    Manganelli, V.2    Matarrese, P.3    Tinari, A.4    Misasi, R.5    Malorni, W.6    Garofalo, T.7
  • 22
    • 79953152683 scopus 로고    scopus 로고
    • Reconstitution of proapoptotic BAK function in liposomes reveals a dual role for mitochondrial lipids in the BAK-driven membrane permeabilization process
    • Landeta, O., Landajuela, A., Gil, D., Taneva, S., Di Primo, C., Sot, B., Valle, M., Frolov, V. A., and Basañez, G. (2011) Reconstitution of proapoptotic BAK function in liposomes reveals a dual role for mitochondrial lipids in the BAK-driven membrane permeabilization process. J. Biol. Chem. 286, 8213-8230
    • (2011) J. Biol. Chem. , vol.286 , pp. 8213-8230
    • Landeta, O.1    Landajuela, A.2    Gil, D.3    Taneva, S.4    Di Primo, C.5    Sot, B.6    Valle, M.7    Frolov, V.A.8    Basañez, G.9
  • 26
    • 0034795258 scopus 로고    scopus 로고
    • Bid, a widely expressed proapoptotic protein of the Bcl-2 family, displays lipid transfer activity
    • DOI 10.1128/MCB.21.21.7268-7276.2001
    • Esposti, M. D., Erler, J. T., Hickman, J. A., and Dive, C. (2001) Bid, a widely expressed proapoptotic protein of the Bcl-2 family, displays lipid transfer activity. Mol. Cell. Biol. 21, 7268-7276 (Pubitemid 32953480)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.21 , pp. 7268-7276
    • Degli, E.M.1    Erler, J.T.2    Hickman, J.A.3    Dive, C.4
  • 28
    • 84862778844 scopus 로고    scopus 로고
    • ATAD3, a vital membrane-bound mitochondrial ATPase involved in tumor progression
    • Li, S., and Rousseau, D. (2012) ATAD3, a vital membrane-bound mitochondrial ATPase involved in tumor progression. J. Bioenerg. Biomembr. 44, 189-197
    • (2012) J. Bioenerg. Biomembr. , vol.44 , pp. 189-197
    • Li, S.1    Rousseau, D.2
  • 29
    • 84860859573 scopus 로고    scopus 로고
    • Role for two conserved intermembrane space proteins, Ups1p and Up2p, in intra-mitochondrial phospholipid trafficking
    • Tamura, Y., Onguka, O., Hobbs, A. E., Jensen, R. E., Iijima, M., Claypool, S. M., and Sesaki, H. (2012) Role for two conserved intermembrane space proteins, Ups1p and Up2p, in intra-mitochondrial phospholipid trafficking. J. Biol. Chem. 287, 15205-15218
    • (2012) J. Biol. Chem. , vol.287 , pp. 15205-15218
    • Tamura, Y.1    Onguka, O.2    Hobbs, A.E.3    Jensen, R.E.4    Iijima, M.5    Claypool, S.M.6    Sesaki, H.7
  • 30
    • 84868596965 scopus 로고    scopus 로고
    • Intramitochondrial transport of phosphatidic acid in yeast by a lipid transfer protein
    • Connerth, M., Tatsuta, T., Haag, M., Klecker, T., Westermann, B., and Langer, T. (2012) Intramitochondrial transport of phosphatidic acid in yeast by a lipid transfer protein. Science 338, 815-818
    • (2012) Science , vol.338 , pp. 815-818
    • Connerth, M.1    Tatsuta, T.2    Haag, M.3    Klecker, T.4    Westermann, B.5    Langer, T.6
  • 31
    • 0142156049 scopus 로고    scopus 로고
    • Phospholipid Scramblase 3 Controls Mitochondrial Structure, Function, and Apoptotic Response
    • Liu, J., Dai, Q., Chen, J., Durrant, D., Freeman, A., Liu, T., Grossman, D., and Lee, R. M. (2003) Phospholipid scramblase 3 controls mitochondrial structure, function, and apoptotic response. Mol. Cancer Res. 1, 892-902 (Pubitemid 37303889)
    • (2003) Molecular Cancer Research , vol.1 , Issue.12 , pp. 892-902
    • Liu, J.1    Dai, Q.2    Chen, J.3    Durrant, D.4    Freeman, A.5    Liu, T.6    Grossman, D.7    Lee, R.M.8
  • 32
    • 77953720612 scopus 로고    scopus 로고
    • Phospholipid scramblase. An update
    • Bevers, E. M., and Williamson, P. L. (2010) Phospholipid scramblase. An update. FEBS Lett. 584, 2724-2730
    • (2010) FEBS Lett. , vol.584 , pp. 2724-2730
    • Bevers, E.M.1    Williamson, P.L.2
  • 33
    • 0347481136 scopus 로고    scopus 로고
    • Transbilayer Lipid Diffusion Promoted by Bax: Implications for Apoptosis
    • DOI 10.1021/bi035348w
    • Epand, R. F., Martinou, J. C., Montessuit, S., and Epand, R. M. (2003) Transbilayer lipid diffusion promoted by Bax. Implications for apoptosis. Biochemistry 42, 14576-14582 (Pubitemid 37532004)
    • (2003) Biochemistry , vol.42 , Issue.49 , pp. 14576-14582
    • Epand, R.F.1    Martinou, J.-C.2    Montessuit, S.3    Epand, R.M.4
  • 34
    • 35549010278 scopus 로고    scopus 로고
    • Reduced creatine-stimulated respiration in doxorubicin challenged mitochondria: Particular sensitivity of the heart
    • DOI 10.1016/j.bbabio.2007.08.006, PII S0005272807001971
    • Tokarska-Schlattner, M., Dolder, M., Gerber, I., Speer, O., Wallimann, T., and Schlattner, U. (2007) Reduced creatine-stimulated respiration in doxorubicin challenged mitochondria. Particular sensitivity of the heart. Biochim. Biophys. Acta 1767, 1276-1284 (Pubitemid 350017745)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.11 , pp. 1276-1284
    • Tokarska-Schlattner, M.1    Dolder, M.2    Gerber, I.3    Speer, O.4    Wallimann, T.5    Schlattner, U.6
  • 35
    • 0017873959 scopus 로고
    • Nucleoside diphosphokinase from human erythrocytes
    • Agarwal, R. P., Robison, B., and Parks, R. E., Jr. (1978) Nucleoside diphosphokinase from human erythrocytes. Methods Enzymol. 51, 376-386
    • (1978) Methods Enzymol. , vol.51 , pp. 376-386
    • Agarwal, R.P.1    Robison, B.2    Parks Jr., R.E.3
  • 36
    • 0025091897 scopus 로고
    • Improved methods to isolate and subfractionate rat liver mitochondria. Lipid composition of the inner and outer membrane
    • DOI 10.1016/0005-2736(90)90036-N
    • Hovius, R., Lambrechts, H., Nicolay, K., and de Kruijff, B. (1990) Improved methods to isolate and subfractionate rat liver mitochondria. Lipid composition of the inner and outer membrane. Biochim. Biophys. Acta. 1021, 217-226 (Pubitemid 20037572)
    • (1990) Biochimica et Biophysica Acta - Biomembranes , vol.1021 , Issue.2 , pp. 217-226
    • Hovius, R.1    Lambrechts, H.2    Nicolay, K.3    De Kruijff, B.4
  • 37
    • 0037020079 scopus 로고    scopus 로고
    • Novel mitochondrial creatine transport activity. Implications for intracellular creatine compartments and bioenergetics
    • Walzel, B., Speer, O., Zanolla, E., Eriksson, O., Bernardi, P., and Wallimann, T. (2002) Novel mitochondrial creatine transport activity. Implications for intracellular creatine compartments and bioenergetics. J. Biol. Chem. 277, 37503-37511
    • (2002) J. Biol. Chem. , vol.277 , pp. 37503-37511
    • Walzel, B.1    Speer, O.2    Zanolla, E.3    Eriksson, O.4    Bernardi, P.5    Wallimann, T.6
  • 38
    • 70449158340 scopus 로고
    • A simple method for the isolation and purification of total lipids from animal tissues
    • Folch, J., Lees, M., and Sloane Stanley, G. H. (1957) A simple method for the isolation and purification of total lipids from animal tissues. J. Biol. Chem. 226, 497-509
    • (1957) J. Biol. Chem. , vol.226 , pp. 497-509
    • Folch, J.1    Lees, M.2    Sloane Stanley, G.H.3
  • 40
    • 84934442060 scopus 로고    scopus 로고
    • Identification of motions in membrane proteins by elastic network models and their experimental validation
    • Isin, B., Tirupula, K. C., Oltvai, Z. N., Klein-Seetharaman, J., and Bahar, I. (2012) Identification of motions in membrane proteins by elastic network models and their experimental validation. Methods Mol. Biol. 914, 285-317
    • (2012) Methods Mol. Biol. , vol.914 , pp. 285-317
    • Isin, B.1    Tirupula, K.C.2    Oltvai, Z.N.3    Klein-Seetharaman, J.4    Bahar, I.5
  • 41
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina. Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
    • Trott, O., and Olson, A. J. (2010) AutoDock Vina. Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J. Comput. Chem. 31, 455-461
    • (2010) J. Comput. Chem. , vol.31 , pp. 455-461
    • Trott, O.1    Olson, A.J.2
  • 42
    • 1842740658 scopus 로고    scopus 로고
    • Cardiolipin and its metabolites move from mitochondria to other cellular membranes during death receptor-mediated apoptosis
    • DOI 10.1038/sj.cdd.4401457
    • Sorice, M., Circella, A., Cristea, I. M., Garofalo, T., Di Renzo, L., Alessandri, C., Valesini, G., and Esposti, M. D. (2004) Cardiolipin and its metabolites move from mitochondria to other cellular membranes during death receptor-mediated apoptosis. Cell Death Differ. 11, 1133-1145 (Pubitemid 39341639)
    • (2004) Cell Death and Differentiation , vol.11 , Issue.10 , pp. 1133-1145
    • Sorice, M.1    Circella, A.2    Cristea, I.M.3    Garofalo, T.4    Di, R.L.5    Alessandri, C.6    Valesini, G.7    Degli, E.M.8
  • 43
    • 0014473526 scopus 로고
    • Kinetic studies of yeast nucleoside diphosphate kinase
    • Garces, E., and Cleland, W. W. (1969) Kinetic studies of yeast nucleoside diphosphate kinase. Biochemistry 8, 633-640
    • (1969) Biochemistry , vol.8 , pp. 633-640
    • Garces, E.1    Cleland, W.W.2
  • 45
    • 0031656932 scopus 로고    scopus 로고
    • Oligomeric state and membrane binding behaviour of creatine kinase isoenzymes: Implications for cellular function and mitochondrial structure
    • Stachowiak, O., Schlattner, U., Dolder, M., and Wallimann, T. (1998) Oligomeric state and membrane binding behaviour of creatine kinase isoenzymes: implications for cellular function and mitochondrial structure. Mol. Cell. Biochem. 184, 141-151 (Pubitemid 28398606)
    • (1998) Molecular and Cellular Biochemistry , vol.184 , Issue.1-2 , pp. 141-151
    • Stachowiak, O.1    Schlattner, U.2    Dolder, M.3    Wallimann, T.4
  • 46
    • 77953526521 scopus 로고    scopus 로고
    • OPA1 disease alleles causing dominant optic atrophy have defects in cardiolipin-stimulated GTP hydrolysis and membrane tubulation
    • Ban, T., Heymann, J. A., Song, Z., Hinshaw, J. E., and Chan, D. C. (2010) OPA1 disease alleles causing dominant optic atrophy have defects in cardiolipin-stimulated GTP hydrolysis and membrane tubulation. Hum. Mol. Genet. 19, 2113-2122
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 2113-2122
    • Ban, T.1    Heymann, J.A.2    Song, Z.3    Hinshaw, J.E.4    Chan, D.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.