메뉴 건너뛰기




Volumn 230, Issue 8, 2015, Pages 1697-1701

MNADK, a long-awaited human mitochondrion-localized NAD kinase

Author keywords

[No Author keywords available]

Indexed keywords

MITOCHONDRIAL NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE KINASE; UNCLASSIFIED DRUG; MITOCHONDRIAL PROTEIN; NADK2 PROTEIN, HUMAN; PHOSPHOTRANSFERASE;

EID: 84928399000     PISSN: 00219541     EISSN: 10974652     Source Type: Journal    
DOI: 10.1002/jcp.24926     Document Type: Review
Times cited : (40)

References (39)
  • 1
    • 77949480387 scopus 로고    scopus 로고
    • The phosphate makes a difference: Cellular functions of NADP
    • Agledal L, Niere M, Ziegler M. 2010. The phosphate makes a difference: Cellular functions of NADP. Redox Rep 15: 2-10.
    • (2010) Redox Rep , vol.15 , pp. 2-10
    • Agledal, L.1    Niere, M.2    Ziegler, M.3
  • 2
    • 13944278132 scopus 로고    scopus 로고
    • Mitochondria, oxidants, and aging
    • Balaban RS, Nemoto S, Finkel T. 2005. Mitochondria, oxidants, and aging. Cell 120: 483-495.
    • (2005) Cell , vol.120 , pp. 483-495
    • Balaban, R.S.1    Nemoto, S.2    Finkel, T.3
  • 4
    • 33747347559 scopus 로고    scopus 로고
    • Synthetic lethal and biochemical analyses of NAD and NADH kinases in Saccharomyces cerevisiae establish separation of cellular functions
    • Bieganowski P, Seidle HF, Wojcik M, Brenner C. 2006. Synthetic lethal and biochemical analyses of NAD and NADH kinases in Saccharomyces cerevisiae establish separation of cellular functions. J Biol Chem 281: 22439-22445.
    • (2006) J Biol Chem , vol.281 , pp. 22439-22445
    • Bieganowski, P.1    Seidle, H.F.2    Wojcik, M.3    Brenner, C.4
  • 5
    • 27144540627 scopus 로고    scopus 로고
    • NADK2, an Arabidopsis chloroplastic NAD kinase, plays a vital role in both chlorophyll synthesis and chloroplast protection
    • Chai MF, Chen QJ, An R, Chen YM, Chen J, Wang XC. 2005. NADK2, an Arabidopsis chloroplastic NAD kinase, plays a vital role in both chlorophyll synthesis and chloroplast protection. Plant Mol Biol 59: 553-564.
    • (2005) Plant Mol Biol , vol.59 , pp. 553-564
    • Chai, M.F.1    Chen, Q.J.2    An, R.3    Chen, Y.M.4    Chen, J.5    Wang, X.C.6
  • 6
    • 0018775962 scopus 로고
    • A candidate for the permeability pathway of the outer mitochondrial membrane
    • Colombini M. 1979. A candidate for the permeability pathway of the outer mitochondrial membrane. Nature 279: 643-645.
    • (1979) Nature , vol.279 , pp. 643-645
    • Colombini, M.1
  • 8
    • 0021759134 scopus 로고
    • A Ca2 + , Calmodulin-dependent NAD kinase from corn is located in the outer mitochondrial membrane
    • Dieter P, Marme D. 1984. A Ca2 +, Calmodulin-dependent NAD kinase from corn is located in the outer mitochondrial membrane. J Biol Chem 259: 184-189.
    • (1984) J Biol Chem , vol.259 , pp. 184-189
    • Dieter, P.1    Marme, D.2
  • 10
    • 0034677947 scopus 로고    scopus 로고
    • NAD(P)H oxidase: Role in cardiovascular biology and disease
    • Griendling KK, Sorescu D, Ushio-Fukai M. 2000. NAD(P)H oxidase: Role in cardiovascular biology and disease. Circ Res 86: 494-501.
    • (2000) Circ Res , vol.86 , pp. 494-501
    • Griendling, K.K.1    Sorescu, D.2    Ushio-Fukai, M.3
  • 11
    • 61549132959 scopus 로고    scopus 로고
    • NAADP: A universal Ca2+ trigger
    • Guse AH, Lee HC. 2008. NAADP: A universal Ca2+ trigger. Sci Signal 1: re10.
    • (2008) Sci Signal , vol.1 , pp. re10
    • Guse, A.H.1    Lee, H.C.2
  • 13
    • 84863763440 scopus 로고    scopus 로고
    • AMPK regulates NADPH homeostasis to promote tumour cell survival during energy stress
    • Jeon SM, Chandel NS, Hay N. 2012. AMPK regulates NADPH homeostasis to promote tumour cell survival during energy stress. Nature 485: 661-665.
    • (2012) Nature , vol.485 , pp. 661-665
    • Jeon, S.M.1    Chandel, N.S.2    Hay, N.3
  • 14
    • 43549127287 scopus 로고    scopus 로고
    • Structure and function of NAD kinase and NADP phosphatase: Key enzymes that regulate the intracellular balance of NAD(H) and NADP(H)
    • Kawai S, Murata K. 2008. Structure and function of NAD kinase and NADP phosphatase: Key enzymes that regulate the intracellular balance of NAD(H) and NADP(H). Biosci Biotechnol Biochem 72: 919-930.
    • (2008) Biosci Biotechnol Biochem , vol.72 , pp. 919-930
    • Kawai, S.1    Murata, K.2
  • 15
    • 0035948228 scopus 로고    scopus 로고
    • Molecular cloning and identification of UTR1 of a yeast Saccharomyces cerevisiae as a gene encoding an NAD kinase
    • Kawai S, Suzuki S, Mori S, Murata K. 2001. Molecular cloning and identification of UTR1 of a yeast Saccharomyces cerevisiae as a gene encoding an NAD kinase. FEMS Microbiol Lett 200: 181-184.
    • (2001) FEMS Microbiol Lett , vol.200 , pp. 181-184
    • Kawai, S.1    Suzuki, S.2    Mori, S.3    Murata, K.4
  • 16
    • 0028906080 scopus 로고
    • Mutants of Saccharomyces cerevisiae sensitive to oxidative and osmotic stress
    • Krems B, Charizanis C, Entian KD. 1995. Mutants of Saccharomyces cerevisiae sensitive to oxidative and osmotic stress. Curr Genet 27: 427-434.
    • (1995) Curr Genet , vol.27 , pp. 427-434
    • Krems, B.1    Charizanis, C.2    Entian, K.D.3
  • 21
    • 0005764576 scopus 로고
    • Light-induced conversion of nicotinamide adenine dinucleotide to nicotinamide adenine dinucleotide phosphate in higher plant leaves
    • Muto S, Miyachi S. 1981. Light-induced conversion of nicotinamide adenine dinucleotide to nicotinamide adenine dinucleotide phosphate in higher plant leaves. Plant Physiol 68: 324-328.
    • (1981) Plant Physiol , vol.68 , pp. 324-328
    • Muto, S.1    Miyachi, S.2
  • 22
    • 84871820491 scopus 로고    scopus 로고
    • Identification and characterization of a human mitochondrial NAD kinase
    • Ohashi K, Kawai S, Murata K. 2012. Identification and characterization of a human mitochondrial NAD kinase. Nat Commun 3:1248.
    • (2012) Nat Commun , vol.3 , pp. 1248
    • Ohashi, K.1    Kawai, S.2    Murata, K.3
  • 23
    • 0037881908 scopus 로고    scopus 로고
    • A novel NADH kinase is the mitochondrial source of NADPH in Saccharomyces cerevisiae
    • Outten CE, Culotta VC. 2003. A novel NADH kinase is the mitochondrial source of NADPH in Saccharomyces cerevisiae. EMBO J 22: 2015-2024.
    • (2003) EMBO J , vol.22 , pp. 2015-2024
    • Outten, C.E.1    Culotta, V.C.2
  • 24
    • 33847711060 scopus 로고    scopus 로고
    • The power to reduce: Pyridine nucleotides-small molecules with a multitude of functions
    • Pollak N, Dolle C, Ziegler M. 2007a. The power to reduce: Pyridine nucleotides-small molecules with a multitude of functions. Biochem J 402: 205-218.
    • (2007) Biochem J , vol.402 , pp. 205-218
    • Pollak, N.1    Dolle, C.2    Ziegler, M.3
  • 25
    • 36348971843 scopus 로고    scopus 로고
    • NAD kinase levels control the NADPH concentration in human cells
    • Pollak N, Niere M, Ziegler M. 2007b. NAD kinase levels control the NADPH concentration in human cells. J Biol Chem 282: 33562-33571.
    • (2007) J Biol Chem , vol.282 , pp. 33562-33571
    • Pollak, N.1    Niere, M.2    Ziegler, M.3
  • 26
    • 0034306267 scopus 로고    scopus 로고
    • Mitochondria, oxygen free radicals, disease and ageing
    • Raha S, Robinson BH. 2000. Mitochondria, oxygen free radicals, disease and ageing. Trends Biochem Sci 25: 502-508.
    • (2000) Trends Biochem Sci , vol.25 , pp. 502-508
    • Raha, S.1    Robinson, B.H.2
  • 28
    • 22144434877 scopus 로고    scopus 로고
    • Identification of ATP-NADH kinase isozymes and their contribution to supply of NADP(H) in Saccharomyces cerevisiae
    • Shi F, Kawai S, Mori S, Kono E, Murata K. 2005. Identification of ATP-NADH kinase isozymes and their contribution to supply of NADP(H) in Saccharomyces cerevisiae. FEBS J 272: 3337-3349.
    • (2005) FEBS J , vol.272 , pp. 3337-3349
    • Shi, F.1    Kawai, S.2    Mori, S.3    Kono, E.4    Murata, K.5
  • 29
    • 0013027638 scopus 로고
    • Calmodulin-dependent and independent NAD kinase activities from cytoplasmic and AT fractions of spinach (Spinacia oleracea L.)
    • Simon P, Dieter P, Bonzon M, Greppin H, Marme D. 1982. Calmodulin-dependent and independent NAD kinase activities from cytoplasmic and AT fractions of spinach (Spinacia oleracea L.). Plant Cell Rep 1: 119-122.
    • (1982) Plant Cell Rep , vol.1 , pp. 119-122
    • Simon, P.1    Dieter, P.2    Bonzon, M.3    Greppin, H.4    Marme, D.5
  • 31
    • 0043234233 scopus 로고    scopus 로고
    • POS5 gene of Saccharomyces cerevisiae encodes a mitochondrial NADH kinase required for stability of mitochondrial DNA
    • Strand MK, Stuart GR, Longley MJ, Graziewicz MA, Dominick OC, Copeland WC. 2003. POS5 gene of Saccharomyces cerevisiae encodes a mitochondrial NADH kinase required for stability of mitochondrial DNA. Eukaryot Cell 2: 809-820.
    • (2003) Eukaryot Cell , vol.2 , pp. 809-820
    • Strand, M.K.1    Stuart, G.R.2    Longley, M.J.3    Graziewicz, M.A.4    Dominick, O.C.5    Copeland, W.C.6
  • 32
    • 33644513561 scopus 로고    scopus 로고
    • Identification of the mitochondrial NAD+ transporter in Saccharomyces cerevisiae
    • Todisco S, Agrimi G, Castegna A, Palmieri F. 2006. Identification of the mitochondrial NAD+ transporter in Saccharomyces cerevisiae. J Biol Chem 281: 1524-1531.
    • (2006) J Biol Chem , vol.281 , pp. 1524-1531
    • Todisco, S.1    Agrimi, G.2    Castegna, A.3    Palmieri, F.4
  • 33
    • 12744280982 scopus 로고    scopus 로고
    • Identification, molecular cloning and functional characterization of a novel NADH kinase from Arabidopsis thaliana (thale cress)
    • Turner WL, Waller JC, Snedden WA. 2005. Identification, molecular cloning and functional characterization of a novel NADH kinase from Arabidopsis thaliana (thale cress). Biochem J 385: 217-223.
    • (2005) Biochem J , vol.385 , pp. 217-223
    • Turner, W.L.1    Waller, J.C.2    Snedden, W.A.3
  • 34
    • 3543001681 scopus 로고    scopus 로고
    • Cloning and characterization of two NAD kinases from Arabidopsis. identification of a calmodulin binding isoform
    • Turner WL, Waller JC, Vanderbeld B, Snedden WA. 2004. Cloning and characterization of two NAD kinases from Arabidopsis. identification of a calmodulin binding isoform. Plant Physiol 135: 1243-1255.
    • (2004) Plant Physiol , vol.135 , pp. 1243-1255
    • Turner, W.L.1    Waller, J.C.2    Vanderbeld, B.3    Snedden, W.A.4
  • 36
    • 77949774450 scopus 로고    scopus 로고
    • Subcellular and tissue localization of NAD kinases from Arabidopsis: Compartmentalization of de novo NADP biosynthesis
    • Waller JC, Dhanoa PK, Schumann U, Mullen RT, Snedden WA. 2010. Subcellular and tissue localization of NAD kinases from Arabidopsis: Compartmentalization of de novo NADP biosynthesis. Planta 231: 305-317.
    • (2010) Planta , vol.231 , pp. 305-317
    • Waller, J.C.1    Dhanoa, P.K.2    Schumann, U.3    Mullen, R.T.4    Snedden, W.A.5
  • 37
    • 0021987751 scopus 로고
    • Calmodulin-dependent NAD kinase of human neutrophils
    • Williams MB, Jones HP. 1985. Calmodulin-dependent NAD kinase of human neutrophils. Arch Biochem Biophys 237: 80-87.
    • (1985) Arch Biochem Biophys , vol.237 , pp. 80-87
    • Williams, M.B.1    Jones, H.P.2
  • 39
    • 84965031012 scopus 로고    scopus 로고
    • MNADK, a novel liver-enriched mitochondrion-localized NAD kinase
    • Zhang R. 2013. MNADK, a novel liver-enriched mitochondrion-localized NAD kinase. Biol Open 2: 432-438.
    • (2013) Biol Open , vol.2 , pp. 432-438
    • Zhang, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.