메뉴 건너뛰기




Volumn 14, Issue 7, 2017, Pages 720-728

Genetically encoded fluorescent sensors reveal dynamic regulation of NADPH metabolism

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOSE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PHOTOPROTEIN; PROTEIN BINDING;

EID: 85027497733     PISSN: 15487091     EISSN: 15487105     Source Type: Journal    
DOI: 10.1038/nmeth.4306     Document Type: Article
Times cited : (233)

References (48)
  • 1
    • 84889575198 scopus 로고    scopus 로고
    • Modulation of oxidative stress as an anticancer strategy
    • Gorrini, C., Harris, I. S., & Mak, T. W. Modulation of oxidative stress as an anticancer strategy. Nat. Rev. Drug Discov. 12, 931-947 (2013
    • (2013) Nat. Rev. Drug Discov , vol.12 , pp. 931-947
    • Gorrini, C.1    Harris, I.S.2    Mak, T.W.3
  • 2
    • 84869009687 scopus 로고    scopus 로고
    • How cancer metabolism is tuned for proliferation and vulnerable to disruption
    • Schulze, A., & Harris, A. L. How cancer metabolism is tuned for proliferation and vulnerable to disruption. Nature 491, 364-373 (2012
    • (2012) Nature , vol.491 , pp. 364-373
    • Schulze, A.1    Harris, A.L.2
  • 3
    • 0036883907 scopus 로고    scopus 로고
    • Blocking NO syn thesis: How, where and why?
    • Vallance, P., & Leiper, J. Blocking NO synthesis: how, where and why? Nat. Rev. Drug Discov. 1, 939-950 (2002
    • (2002) Nat. Rev. Drug Discov , vol.1 , pp. 939-950
    • Vallance, P.1    Leiper, J.2
  • 4
    • 67650071137 scopus 로고    scopus 로고
    • Targeting cancer cells by ROS-mediated mechanisms: A radical therapeutic approach?
    • Trachootham, D., Alexandre, J., & Huang, P. Targeting cancer cells by ROS-mediated mechanisms: a radical therapeutic approach? Nat. Rev. Drug Discov. 8, 579-591 (2009
    • (2009) Nat. Rev. Drug Discov , vol.8 , pp. 579-591
    • Trachootham, D.1    Alexandre, J.2    Huang, P.3
  • 5
    • 36348971843 scopus 로고    scopus 로고
    • NAD kinase levels control the NADPH concentration in human cells
    • Pollak, N., Niere, M., & Ziegler, M. NAD kinase levels control the NADPH concentration in human cells. J. Biol. Chem. 282, 33562-33571 (2007
    • (2007) J. Biol. Chem , vol.282 , pp. 33562-33571
    • Pollak, N.1    Niere, M.2    Ziegler, M.3
  • 6
    • 84961156995 scopus 로고    scopus 로고
    • G6PD protects from oxidative damage and improves healthspan in mice
    • Nóbrega-Pereira, S., et al. G6PD protects from oxidative damage and improves healthspan in mice. Nat. Commun. 7, 10894 (2016
    • (2016) Nat. Commun , vol.7 , pp. 10894
    • Nóbrega-Pereira, S.1
  • 7
    • 0029097424 scopus 로고
    • Feasibility of a mitochondrial pyruvate malate shuttle in pancreatic islets Further implication of cytosolic NADPH in insulin secretion
    • MacDonald, M. J. Feasibility of a mitochondrial pyruvate malate shuttle in pancreatic islets. Further implication of cytosolic NADPH in insulin secretion. J. Biol. Chem. 270, 20051-20058 (1995
    • (1995) J. Biol. Chem , vol.270 , pp. 20051-20058
    • MacDonald, M.J.1
  • 8
    • 84901756757 scopus 로고    scopus 로고
    • Separating NADH and NADPH fluorescence in live cells and tissues using FLIM
    • Blacker, T. S., et al. Separating NADH and NADPH fluorescence in live cells and tissues using FLIM. Nat. Commun. 5, 3936 (2014
    • (2014) Nat. Commun , vol.5 , pp. 3936
    • Blacker, T.S.1
  • 9
    • 80053898694 scopus 로고    scopus 로고
    • Genetically encoded fluorescent sensors for intracellular NADH detection
    • Zhao, Y., et al. Genetically encoded fluorescent sensors for intracellular NADH detection. Cell Metab. 14, 555-566 (2011
    • (2011) Cell Metab , vol.14 , pp. 555-566
    • Zhao, Y.1
  • 10
    • 84983551800 scopus 로고    scopus 로고
    • SoNar, a highly responsive NAD+/NADH sensor, allows high-Throughput metabolic screening of anti-Tumor agents
    • Zhao, Y., et al. SoNar, a highly responsive NAD+/NADH sensor, allows high-Throughput metabolic screening of anti-Tumor agents. Cell Metab. 21, 777-789 (2015
    • (2015) Cell Metab , vol.21 , pp. 777-789
    • Zhao, Y.1
  • 11
    • 84890450161 scopus 로고    scopus 로고
    • Genetically encoded fluorescent indicator for imaging NAD(+)/NADH ratio changes in different cellular compartments
    • Bilan, D. S., et al. Genetically encoded fluorescent indicator for imaging NAD(+)/NADH ratio changes in different cellular compartments. Biochim. Biophys. Acta 1840, 951-957 (2014
    • (2014) Biochim. Biophys. Acta , vol.1840 , pp. 951-957
    • Bilan, D.S.1
  • 12
    • 80053902441 scopus 로고    scopus 로고
    • Imaging cytosolic NADH-NAD(+) redox state with a genetically encoded fluorescent biosensor
    • Hung, Y. P., Albeck, J. G., Tantama, M., & Yellen, G. Imaging cytosolic NADH-NAD(+) redox state with a genetically encoded fluorescent biosensor. Cell Metab. 14, 545-554 (2011
    • (2011) Cell Metab , vol.14 , pp. 545-554
    • Hung, Y.P.1    Albeck, J.G.2    Tantama, M.3    Yellen, G.4
  • 13
    • 84975132387 scopus 로고    scopus 로고
    • Biosensor reveals multiple sources for mitochondrial NAD+
    • Cambronne, X. A., et al. Biosensor reveals multiple sources for mitochondrial NAD+. Science 352, 1474-1477 (2016
    • (2016) Science , vol.352 , pp. 1474-1477
    • Cambronne, X.A.1
  • 14
    • 84958280443 scopus 로고    scopus 로고
    • Apollo-NADP+: A spectrally tunable family of genetically encoded sensors for NADP+
    • Cameron, W. D., et al. Apollo-NADP+: a spectrally tunable family of genetically encoded sensors for NADP+. Nat. Methods 13, 352-358 (2016
    • (2016) Nat. Methods , vol.13 , pp. 352-358
    • Cameron, W.D.1
  • 15
    • 84979943712 scopus 로고    scopus 로고
    • In vivo monitoring of cellular energy metabolism using SoNar, a highly responsive sensor for NAD+/NADH redox state
    • Zhao, Y., et al. In vivo monitoring of cellular energy metabolism using SoNar, a highly responsive sensor for NAD+/NADH redox state. Nat. Protoc. 11, 1345-1359 (2016
    • (2016) Nat. Protoc , vol.11 , pp. 1345-1359
    • Zhao, Y.1
  • 16
    • 84973457842 scopus 로고    scopus 로고
    • Real-Time and high-Throughput analysis of mitochondrial metabolic states in living cells using genetically encoded NAD+/NADH sensors
    • Zhao, Y., & Yang, Y. Real-Time and high-Throughput analysis of mitochondrial metabolic states in living cells using genetically encoded NAD+/NADH sensors. Free Radic. Biol. Med. 100, 43-52 (2016
    • (2016) Free Radic. Biol. Med , vol.100 , pp. 43-52
    • Zhao, Y.1    Yang, Y.2
  • 17
    • 33748271948 scopus 로고    scopus 로고
    • Comparison of protein active site structures for functional annotation of proteins and drug design
    • Powers, R., et al. Comparison of protein active site structures for functional annotation of proteins and drug design. Proteins 65, 124-135 (2006
    • (2006) Proteins , vol.65 , pp. 124-135
    • Powers, R.1
  • 18
    • 33947323287 scopus 로고    scopus 로고
    • Structure of archaeal glyoxylate reductase from Pyrococcus horikoshii OT3 complexed with nicotinamide adenine dinucleotide phosphate
    • Yoshikawa, S., et al. Structure of archaeal glyoxylate reductase from Pyrococcus horikoshii OT3 complexed with nicotinamide adenine dinucleotide phosphate. Acta Crystallogr. D Biol. Crystallogr. 63, 357-365 (2007
    • (2007) Acta Crystallogr. D Biol. Crystallogr , vol.63 , pp. 357-365
    • Yoshikawa, S.1
  • 19
    • 0035853040 scopus 로고    scopus 로고
    • Circularly permuted green fluorescent proteins engineered to sense Ca2+
    • Nagai, T., Sawano, A., Park, E. S., & Miyawaki, A. Circularly permuted green fluorescent proteins engineered to sense Ca2+. Proc. Natl. Acad. Sci. USA 98, 3197-3202 (2001
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3197-3202
    • Nagai, T.1    Sawano, A.2    Park, E.S.3    Miyawaki, A.4
  • 20
    • 0023117765 scopus 로고
    • Cytosolic ratios of free [nadph]/[nadp+] and [nadh]/[nad+] in mouse pancreatic islets, and nutrient-induced insulin secretion
    • Hedeskov, C. J., Capito, K., & Thams, P. Cytosolic ratios of free [NADPH]/[NADP+] and [NADH]/[NAD+] in mouse pancreatic islets, and nutrient-induced insulin secretion. Biochem. J. 241, 161-167 (1987
    • (1987) Biochem. J , vol.241 , pp. 161-167
    • Hedeskov, C.J.1    Capito, K.2    Thams, P.3
  • 21
    • 0014621744 scopus 로고
    • The redox state of free nicotinamide-Adenine dinucleotide phosphate in the cytoplasm of rat liver
    • Veech, R. L., Eggleston, L. V., & Krebs, H. A. The redox state of free nicotinamide-Adenine dinucleotide phosphate in the cytoplasm of rat liver. Biochem. J. 115, 609-619 (1969
    • (1969) Biochem. J , vol.115 , pp. 609-619
    • Veech, R.L.1    Eggleston, L.V.2    Krebs, H.A.3
  • 22
    • 84871820491 scopus 로고    scopus 로고
    • Identification and characterization of a human mitochondrial NAD kinase
    • Ohashi, K., Kawai, S., & Murata, K. Identification and characterization of a human mitochondrial NAD kinase. Nat. Commun. 3, 1248 (2012
    • (2012) Nat. Commun , vol.3 , pp. 1248
    • Ohashi, K.1    Kawai, S.2    Murata, K.3
  • 23
    • 84888873103 scopus 로고    scopus 로고
    • Imaging energy status in live cells with a fluorescent biosensor of the intracellular ATP-To-ADP ratio
    • Tantama, M., Martínez-François, J. R., Mongeon, R., & Yellen, G. Imaging energy status in live cells with a fluorescent biosensor of the intracellular ATP-To-ADP ratio. Nat. Commun. 4, 2550 (2013
    • (2013) Nat. Commun , vol.4 , pp. 2550
    • Tantama, M.1    Martínez-François, J.R.2    Mongeon, R.3    Yellen, G.4
  • 24
    • 0031024858 scopus 로고    scopus 로고
    • Differences in nitric oxide synthase activity in a macrophage-like cell line, RAW264.7 cells, treated with lipopolysaccharide (LPS) in the presence or absence of interferon-? (IFN-?): Possible heterogeneity of iNOS activity
    • Noda, T., & Amano, F. Differences in nitric oxide synthase activity in a macrophage-like cell line, RAW264.7 cells, treated with lipopolysaccharide (LPS) in the presence or absence of interferon-? (IFN-?): possible heterogeneity of iNOS activity. J. Biochem. 121, 38-46 (1997
    • (1997) J. Biochem , vol.121 , pp. 38-46
    • Noda, T.1    Amano, F.2
  • 25
    • 40949111343 scopus 로고    scopus 로고
    • GLUT1 and GLUT9 as major contributors to glucose influx in HepG2 cells identified by a high sensitivity intramolecular FRET glucose sensor
    • Takanaga, H., Chaudhuri, B., & Frommer, W. B. GLUT1 and GLUT9 as major contributors to glucose influx in HepG2 cells identified by a high sensitivity intramolecular FRET glucose sensor. Biochim. Biophys. Acta 1778, 1091-1099 (2008
    • (2008) Biochim. Biophys. Acta , vol.778 , pp. 1091-1099
    • Takanaga, H.1    Chaudhuri, B.2    Frommer, W.B.3
  • 26
    • 2542455473 scopus 로고    scopus 로고
    • Imaging dynamic redox changes in mammalian cells with green fluorescent protein indicators
    • Dooley, C. T., et al. Imaging dynamic redox changes in mammalian cells with green fluorescent protein indicators. J. Biol. Chem. 279, 22284-22293 (2004
    • (2004) J. Biol. Chem , vol.279 , pp. 22284-22293
    • Dooley, C.T.1
  • 27
    • 0028834278 scopus 로고
    • Targeted disruption of the housekeeping gene encoding glucose 6-phosphate dehydrogenase (G6PD): G6PD is dispensable for pentose synthesis but essential for defense against oxidative stress
    • Pandolfi, P. P., et al. Targeted disruption of the housekeeping gene encoding glucose 6-phosphate dehydrogenase (G6PD): G6PD is dispensable for pentose synthesis but essential for defense against oxidative stress. EMBO J. 14, 5209-5215 (1995
    • (1995) EMBO J , vol.14 , pp. 5209-5215
    • Pandolfi, P.P.1
  • 28
    • 0034654509 scopus 로고    scopus 로고
    • Human glucose-6-phosphate dehydrogenase: The crystal structure reveals a structural NADP+ molecule and provides insights into enzyme deficiency
    • Au, S. W., Gover, S., Lam, V. M., & Adams, M. J. Human glucose-6-phosphate dehydrogenase: the crystal structure reveals a structural NADP+ molecule and provides insights into enzyme deficiency. Structure 8, 293-303 (2000
    • (2000) Structure , vol.8 , pp. 293-303
    • Au, S.W.1    Gover, S.2    Lam, V.M.3    Adams, M.J.4
  • 29
    • 23044437445 scopus 로고    scopus 로고
    • Ca2+/calmodulin-dependent protein kinase kinase-β acts upstream of AMP-Activated protein kinase in mammalian cells
    • Woods, A., et al. Ca2+/calmodulin-dependent protein kinase kinase-β acts upstream of AMP-Activated protein kinase in mammalian cells. Cell Metab. 2, 21-33 (2005
    • (2005) Cell Metab , vol.2 , pp. 21-33
    • Woods, A.1
  • 30
    • 79953732149 scopus 로고    scopus 로고
    • A fluorescent reporter of AMPK activity and cellular energy stress
    • Tsou, P., Zheng, B., Hsu, C. H., Sasaki, A. T., & Cantley, L. C A fluorescent reporter of AMPK activity and cellular energy stress. Cell Metab. 13, 476-486 (2011
    • (2011) Cell Metab , vol.13 , pp. 476-486
    • Tsou, P.1    Zheng, B.2    Hsu, C.H.3    Sasaki, A.T.4    Cantley, L.C.5
  • 31
    • 79959338922 scopus 로고    scopus 로고
    • AMPK is a direct adenylate charge-regulated protein kinase
    • Oakhill, J. S., et al. AMPK is a direct adenylate charge-regulated protein kinase. Science 332, 1433-1435 (2011
    • (2011) Science , vol.332 , pp. 1433-1435
    • Oakhill, J.S.1
  • 32
    • 84923381507 scopus 로고    scopus 로고
    • Red fluorescent genetically encoded indicator for intracellular hydrogen peroxide
    • Ermakova, Y. G., et al. Red fluorescent genetically encoded indicator for intracellular hydrogen peroxide. Nat. Commun. 5, 5222 (2014
    • (2014) Nat. Commun , vol.5 , pp. 5222
    • Ermakova, Y.G.1
  • 33
    • 67649255876 scopus 로고    scopus 로고
    • A tissue-scale gradient of hydrogen peroxide mediates rapid wound detection in zebrafish
    • Niethammer, P., Grabher, C., Look, A. T., & Mitchison, T. J A tissue-scale gradient of hydrogen peroxide mediates rapid wound detection in zebrafish. Nature 459, 996-999 (2009
    • (2009) Nature , vol.459 , pp. 996-999
    • Niethammer, P.1    Grabher, C.2    Look, A.T.3    Mitchison, T.J.4
  • 34
    • 33645283923 scopus 로고    scopus 로고
    • Genetically encoded fluorescent indicator for intracellular hydrogen peroxide
    • Belousov, V. V., et al. Genetically encoded fluorescent indicator for intracellular hydrogen peroxide. Nat. Methods 3, 281-286 (2006
    • (2006) Nat. Methods , vol.3 , pp. 281-286
    • Belousov, V.V.1
  • 35
    • 59349118696 scopus 로고    scopus 로고
    • A genetically encoded fluorescent reporter of ATP: ADP ratio
    • Berg, J., Hung, Y. P., & Yellen, G A genetically encoded fluorescent reporter of ATP: ADP ratio. Nat. Methods 6, 161-166 (2009
    • (2009) Nat. Methods , vol.6 , pp. 161-166
    • Berg, J.1    Hung, Y.P.2    Yellen, G.3
  • 36
    • 84889043177 scopus 로고    scopus 로고
    • Method for accurate determination of dissociation constants of optical ratiometric systems: Chemical probes, genetically encoded sensors, and interacting molecules
    • Pomorski, A., Kochan'czyk, T., Miłoch, A., & Kreozel, A. Method for accurate determination of dissociation constants of optical ratiometric systems: chemical probes, genetically encoded sensors, and interacting molecules. Anal. Chem. 85, 11479-11486 (2013
    • (2013) Anal. Chem , vol.85 , pp. 11479-11486
    • Pomorski, A.1    Kochanczyk, T.2    Miłoch, A.3    Kreozel, A.4
  • 37
    • 84955326448 scopus 로고    scopus 로고
    • The emerging hallmarks of cancer metabolism
    • Pavlova, N. N., & Thompson, C. B. The emerging hallmarks of cancer metabolism. Cell Metab. 23, 27-47 (2016
    • (2016) Cell Metab , vol.23 , pp. 27-47
    • Pavlova, N.N.1    Thompson, C.B.2
  • 38
    • 84863763440 scopus 로고    scopus 로고
    • AMPK regulates NADPH homeostasis to promote tumour cell survival during energy stress
    • Jeon, S. M., Chandel, N. S., & Hay, N. AMPK regulates NADPH homeostasis to promote tumour cell survival during energy stress. Nature 485, 661-665 (2012
    • (2012) Nature , vol.485 , pp. 661-665
    • Jeon, S.M.1    Chandel, N.S.2    Hay, N.3
  • 39
    • 33744514139 scopus 로고    scopus 로고
    • Identification and characterization of a small molecule AMPK activator that treats key components of type 2 diabetes and the metabolic syndrome
    • Cool, B., et al. Identification and characterization of a small molecule AMPK activator that treats key components of type 2 diabetes and the metabolic syndrome. Cell Metab. 3, 403-416 (2006
    • (2006) Cell Metab , vol.3 , pp. 403-416
    • Cool, B.1
  • 40
    • 84964600616 scopus 로고    scopus 로고
    • Chronic activation of ?2 AMPK induces obesity and reduces β cell function
    • Yavari, A., et al. Chronic activation of ?2 AMPK induces obesity and reduces β cell function. Cell Metab. 23, 821-836 (2016
    • (2016) Cell Metab , vol.23 , pp. 821-836
    • Yavari, A.1
  • 41
    • 84904038165 scopus 로고    scopus 로고
    • AMPK at the nexus of energetics and aging
    • Burkewitz, K., Zhang, Y., & Mair, W. B. AMPK at the nexus of energetics and aging. Cell Metab. 20, 10-25 (2014
    • (2014) Cell Metab , vol.20 , pp. 10-25
    • Burkewitz, K.1    Zhang, Y.2    Mair, W.B.3
  • 42
    • 67749111502 scopus 로고    scopus 로고
    • The LKB1-AMPK pathway: Metabolism and growth control in tumour suppression
    • Shackelford, D. B., & Shaw, R. J. The LKB1-AMPK pathway: metabolism and growth control in tumour suppression. Nat. Rev. Cancer 9, 563-575 (2009
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 563-575
    • Shackelford, D.B.1    Shaw, R.J.2
  • 43
    • 0025865772 scopus 로고
    • Repression of the E coli recA gene requires at least two LexA protein monomers
    • Thliveris, A. T., Little, J. W., & Mount, D. W. Repression of the E. coli recA gene requires at least two LexA protein monomers. Biochimie 73, 449-456 (1991
    • (1991) Biochimie , vol.73 , pp. 449-456
    • Thliveris, A.T.1    Little, J.W.2    Mount, D.W.3
  • 44
    • 80053371503 scopus 로고    scopus 로고
    • An expanded palette of genetically encoded Ca2+ indicators
    • Zhao, Y., et al. An expanded palette of genetically encoded Ca2+ indicators. Science 333, 1888-1891 (2011
    • (2011) Science , vol.333 , pp. 1888-1891
    • Zhao, Y.1
  • 45
    • 0032499784 scopus 로고    scopus 로고
    • Measurement of cytosolic, mitochondrial, and Golgi pH in single living cells with green fluorescent proteins
    • Llopis, J., McCaffery, J. M., Miyawaki, A., Farquhar, M. G., & Tsien, R. Y. Measurement of cytosolic, mitochondrial, and Golgi pH in single living cells with green fluorescent proteins. Proc. Natl. Acad. Sci. USA 95, 6803-6808 (1998
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6803-6808
    • Llopis, J.1    McCaffery, J.M.2    Miyawaki, A.3    Farquhar, M.G.4    Tsien, R.Y.5
  • 46
    • 0032562785 scopus 로고    scopus 로고
    • Importance of glucose-6-phosphate dehydrogenase activity for cell growth
    • Tian, W. N., et al. Importance of glucose-6-phosphate dehydrogenase activity for cell growth. J. Biol. Chem. 273, 10609-10617 (1998
    • (1998) J. Biol. Chem , vol.273 , pp. 10609-10617
    • Tian, W.N.1
  • 47
    • 0037881908 scopus 로고    scopus 로고
    • A novel NADH kinase is the mitochondrial source of NADPH in Saccharomyces cerevisiae
    • Outten, C. E., & Culotta, V. C A novel NADH kinase is the mitochondrial source of NADPH in Saccharomyces cerevisiae. EMBO J. 22, 2015-2024 (2003
    • (2003) EMBO J , vol.22 , pp. 2015-2024
    • Outten, C.E.1    Culotta, V.C.2
  • 48
    • 0028081399 scopus 로고
    • Single extraction method for the spectrophotometric quantification of oxidized and reduced pyridine nucleotides in erythrocytes
    • Wagner, T. C., & Scott, M. D. Single extraction method for the spectrophotometric quantification of oxidized and reduced pyridine nucleotides in erythrocytes. Anal. Biochem. 222, 417-426 (1994
    • (1994) Anal. Biochem , vol.222 , pp. 417-426
    • Wagner, T.C.1    Scott, M.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.