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Volumn 107, Issue 12, 2010, Pages 5459-5464

Visualization of JNK activity dynamics with a genetically encoded fluorescent biosensor

Author keywords

Bistable; FRET; Kinase; MAPK; Subcellular

Indexed keywords

ANISOMYCIN; CYAN FLUORESCENT PROTEIN; FLUORESCENT DYE; STRESS ACTIVATED PROTEIN KINASE; TUMOR NECROSIS FACTOR ALPHA; YELLOW FLUORESCENT PROTEIN;

EID: 77950434011     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0909671107     Document Type: Article
Times cited : (81)

References (30)
  • 1
    • 33847754623 scopus 로고    scopus 로고
    • The JNK signal transduction pathway
    • Weston CR, Davis RJ (2007) The JNK signal transduction pathway. Curr Opin Cell Biol 19:142-149.
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 142-149
    • Weston, C.R.1    Davis, R.J.2
  • 2
    • 0037032817 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases
    • Johnson GL, Lapadat R (2002) Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases. Science 298:1911-1912.
    • (2002) Science , vol.298 , pp. 1911-1912
    • Johnson, G.L.1    Lapadat, R.2
  • 3
    • 0032213146 scopus 로고    scopus 로고
    • JNKK1 organizes a MAP kinase module through specific and sequential interactions with upstream and downstream components mediated by its amino- Terminal extension
    • Xia Y, Wu Z, Su B, Murray B, Karin M (1998) JNKK1 organizes a MAP kinase module through specific and sequential interactions with upstream and downstream components mediated by its amino-terminal extension. Genes Dev 12:3369-3381. (Pubitemid 28520985)
    • (1998) Genes and Development , vol.12 , Issue.21 , pp. 3369-3381
    • Xia, Y.1    Wu, Z.2    Su, B.3    Murray, B.4    Karin, M.5
  • 4
    • 0035822634 scopus 로고    scopus 로고
    • Bistability in the JNK cascade
    • Bagowski CP, Ferrell JE, Jr (2001) Bistability in the JNK cascade. Curr Biol 11:1176-1182.
    • (2001) Curr Biol , vol.11 , pp. 1176-1182
    • Bagowski, C.P.1    Ferrell Jr., J.E.2
  • 5
    • 0242515913 scopus 로고    scopus 로고
    • The JNK cascade as a biochemical switch in mammalian cells: Ultrasensitive and all-or-none responses
    • DOI 10.1016/S0960-9822(03)00083-6, PII S0960982203000836
    • Bagowski CP, Besser J, Frey CR, Ferrell JE, Jr (2003) The JNK cascade as a biochemical switch in mammalian cells: ultrasensitive and all-or-none responses. Curr Biol 13:315-320. (Pubitemid 36230022)
    • (2003) Current Biology , vol.13 , Issue.4 , pp. 315-320
    • Bagowski, C.P.1    Besser, J.2    Frey, C.R.3    Ferrell Jr., J.E.4
  • 6
    • 33750345725 scopus 로고    scopus 로고
    • Analyzing protein kinase dynamics in living cells with FRET reporters
    • DOI 10.1016/j.ymeth.2006.06.013, PII S1046202306001046
    • Ni Q, Titov DV, Zhang J (2006) Analyzing protein kinase dynamics in living cells with FRET reporters. Methods 40:279-286. (Pubitemid 44635295)
    • (2006) Methods , vol.40 , Issue.3 , pp. 279-286
    • Ni, Q.1    Titov, D.V.2    Zhang, J.3
  • 7
    • 33845653234 scopus 로고    scopus 로고
    • Uses for JNK: The many and varied substrates of the c-Jun N-terminal kinases
    • Bogoyevitch MA, Kobe B (2006) Uses for JNK: the many and varied substrates of the c-Jun N-terminal kinases. Microbiol Mol Biol Rev 70:1061-1095.
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 1061-1095
    • Bogoyevitch, M.A.1    Kobe, B.2
  • 8
    • 0028329953 scopus 로고
    • JNK1: A protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain
    • DOI 10.1016/0092-8674(94)90380-8
    • Dérijard B, et al. (1994) JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain. Cell 76:1025-1037. (Pubitemid 24106383)
    • (1994) Cell , vol.76 , Issue.6 , pp. 1025-1037
    • Derijard, B.1    Hibi, M.2    Wu, I.-H.3    Barrett, T.4    Su, B.5    Deng, T.6    Karin, M.7    Davis, R.J.8
  • 9
    • 0035850831 scopus 로고    scopus 로고
    • The AP-1 repressor, JDP2, is a bona fide substrate for the c-Jun N-terminal kinase
    • DOI 10.1016/S0014-5793(01)02907-6, PII S0014579301029076
    • Katz S, Heinrich R, Aronheim A (2001) The AP-1 repressor, JDP2, is a bona fide substrate for the c-Jun N-terminal kinase. FEBS Lett 506:196-200. (Pubitemid 32964812)
    • (2001) FEBS Letters , vol.506 , Issue.3 , pp. 196-200
    • Katz, S.1    Heinrich, R.2    Aronheim, A.3
  • 10
    • 4344576752 scopus 로고    scopus 로고
    • The critical features and the mechanism of inhibition of a kinase interaction motif-based peptide inhibitor of JNK
    • DOI 10.1074/jbc.M402181200
    • Barr RK, Boehm I, Attwood PV, Watt PM, Bogoyevitch MA (2004) The critical features and the mechanism of inhibition of a kinase interaction motif-based peptide inhibitor of JNK. J Biol Chem 279:36327-36338. (Pubitemid 39128970)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.35 , pp. 36327-36338
    • Barr, R.K.1    Boehm, I.2    Attwood, P.V.3    Watt, P.M.4    Bogoyevitch, M.A.5
  • 11
    • 0037115778 scopus 로고    scopus 로고
    • Differential targeting of the stress mitogen-activated protein kinases to the c-Jun dimerization protein 2
    • DOI 10.1042/BJ20021127
    • Katz S, Aronheim A (2002) Differential targeting of the stress mitogen-activated protein kinases to the c-Jun dimerization protein 2. Biochem J 368:939-945. (Pubitemid 36042697)
    • (2002) Biochemical Journal , vol.368 , Issue.3 , pp. 939-945
    • Katz, S.1    Aronheim, A.2
  • 12
    • 0033638454 scopus 로고    scopus 로고
    • The molecular basis of FHA domain: Phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms
    • Durocher D, et al. (2000) The molecular basis of FHA domain: phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms. Mol Cell 6:1169-1182.
    • (2000) Mol Cell , vol.6 , pp. 1169-1182
    • Durocher, D.1
  • 13
    • 25644446102 scopus 로고    scopus 로고
    • Insulin disrupts beta-adrenergic signalling to protein kinase a in adipocytes
    • DOI 10.1038/nature04140, PII N04140
    • Zhang J, Hupfeld CJ, Taylor SS, Olefsky JM, Tsien RY (2005) Insulin disrupts beta-adrenergic signalling to protein kinase A in adipocytes. Nature 437:569-573. (Pubitemid 41613556)
    • (2005) Nature , vol.437 , Issue.7058 , pp. 569-573
    • Zhang, J.1    Hupfeld, C.J.2    Taylor, S.S.3    Olefsky, J.M.4    Tsien, R.Y.5
  • 14
    • 33645295543 scopus 로고    scopus 로고
    • Activation of c-Jun N-terminal kinases by ribotoxic stresses
    • Ouyang DY, Wang YY, Zheng YT (2005) Activation of c-Jun N-terminal kinases by ribotoxic stresses. Cell Mol Immunol 2:419-425.
    • (2005) Cell Mol Immunol , vol.2 , pp. 419-425
    • Ouyang, D.Y.1    Wang, Y.Y.2    Zheng, Y.T.3
  • 15
    • 0037178883 scopus 로고    scopus 로고
    • A 15-residue bifunctional element in D-AKAP1 is required for both endoplasmic reticulum and mitochondrial targeting
    • Ma Y, Taylor S (2002) A 15-residue bifunctional element in D-AKAP1 is required for both endoplasmic reticulum and mitochondrial targeting. J Biol Chem 277:27328-27336.
    • (2002) J Biol Chem , vol.277 , pp. 27328-27336
    • Ma, Y.1    Taylor, S.2
  • 16
    • 37349081929 scopus 로고    scopus 로고
    • C-Jun N-terminal kinase regulates mitochondrial bioenergetics by modulating pyruvate dehydrogenase activity in primary cortical neurons
    • DOI 10.1111/j.1471-4159.2007.04957.x
    • Zhou Q, Lam PY, Han D, Cadenas E (2008) c-Jun N-terminal kinase regulates mitochondrial bioenergetics by modulating pyruvate dehydrogenase activity in primary cortical neurons. J Neurochem 104:325-335. (Pubitemid 350293865)
    • (2008) Journal of Neurochemistry , vol.104 , Issue.2 , pp. 325-335
    • Zhou, Q.1    Lam, P.Y.2    Han, D.3    Cadenas, E.4
  • 17
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • Zacharias DA, Violin JD, Newton AC, Tsien RY (2002) Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science 296:913-916.
    • (2002) Science , vol.296 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4
  • 18
    • 0036532226 scopus 로고    scopus 로고
    • Self-perpetuating states in signal transduction: Positive feedback, double-negative feedback and bistability
    • Ferrell JE, Jr (2002) Self-perpetuating states in signal transduction: positive feedback, double-negative feedback and bistability. Curr Opin Cell Biol 14:140-148.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 140-148
    • Ferrell Jr., J.E.1
  • 19
    • 4143110020 scopus 로고    scopus 로고
    • Hysteresis vs. graded responses: The connections make all the difference
    • Ninfa AJ, Mayo AE (2004) Hysteresis vs. graded responses: the connections make all the difference. Sci STKE 2004:pe20.
    • (2004) Sci STKE , vol.2004
    • Ninfa, A.J.1    Mayo, A.E.2
  • 20
    • 49549102185 scopus 로고    scopus 로고
    • Uncovering mechanisms of bistability in biological systems
    • Pomerening JR (2008) Uncovering mechanisms of bistability in biological systems. Curr Opin Biotechnol 19:381-388.
    • (2008) Curr Opin Biotechnol , vol.19 , pp. 381-388
    • Pomerening, J.R.1
  • 21
    • 63049111520 scopus 로고    scopus 로고
    • High content cell screening in a microfluidic device
    • Cheong R, Wang CJ, Levchenko A (2009) High content cell screening in a microfluidic device. Mol Cell Proteomics 8:433-442.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 433-442
    • Cheong, R.1    Wang, C.J.2    Levchenko, A.3
  • 22
    • 33947361161 scopus 로고    scopus 로고
    • Genetically encoded fluorescent indicators to visualize protein phosphorylation by extracellular signal-regulated kinase in single living cells
    • DOI 10.1021/ac062171d
    • Sato M, Kawai Y, Umezawa Y (2007) Genetically encoded fluorescent indicators to visualize protein phosphorylation by extracellular signal-regulated kinase in single living cells. Anal Chem 79:2570-2575. (Pubitemid 46449042)
    • (2007) Analytical Chemistry , vol.79 , Issue.6 , pp. 2570-2575
    • Sato, M.1    Kawai, Y.2    Umezawa, Y.3
  • 23
    • 58049221116 scopus 로고    scopus 로고
    • A genetically encoded fluorescent sensor of ERK activity
    • Harvey CD, et al. (2008) A genetically encoded fluorescent sensor of ERK activity. Proc Natl Acad Sci USA 105:19264-19269.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 19264-19269
    • Harvey, C.D.1
  • 24
    • 16844387124 scopus 로고    scopus 로고
    • Role of JNK activation in apoptosis: A double-edged sword
    • DOI 10.1038/sj.cr.7290262
    • Liu J, Lin A (2005) Role of JNK activation in apoptosis: a double-edged sword. Cell Res 15:36-42. (Pubitemid 41653963)
    • (2005) Cell Research , vol.15 , Issue.1 , pp. 36-42
    • Liu, J.1    Lin, A.2
  • 25
    • 11244280883 scopus 로고    scopus 로고
    • JNK2 translocates to the mitochondria and mediates cytochrome c release in PC12 cells in response to 6-hydroxydopamine
    • DOI 10.1074/jbc.M405858200
    • Eminel S, Klettner A, Roemer L, Herdegen T, Waetzig V (2004) JNK2 translocates to the mitochondria and mediates cytochrome c release in PC12 cells in response to 6-hydroxydopamine. J Biol Chem 279:55385-55392. (Pubitemid 40066538)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.53 , pp. 55385-55392
    • Eminel, S.1    Klettnert, A.2    Roemer, L.3    Herdegen, T.4    Waetzig, V.5
  • 26
    • 0034708832 scopus 로고    scopus 로고
    • The c-Jun NH(2)-terminal kinase promotes insulin resistance during association with insulin receptor substrate-1 and phosphorylation of Ser(307)
    • Aguirre V, Uchida T, Yenush L, Davis R, White MF (2000) The c-Jun NH(2)-terminal kinase promotes insulin resistance during association with insulin receptor substrate-1 and phosphorylation of Ser(307). J Biol Chem 275:9047-9054.
    • (2000) J Biol Chem , vol.275 , pp. 9047-9054
    • Aguirre, V.1    Uchida, T.2    Yenush, L.3    Davis, R.4    White, M.F.5
  • 27
    • 0038495741 scopus 로고    scopus 로고
    • JNK phosphorylates paxillin and regulates cell migration
    • DOI 10.1038/nature01745
    • Huang C, Rajfur Z, Borchers C, Schaller MD, Jacobson K (2003) JNK phosphorylates paxillin and regulates cell migration. Nature 424:219-223. (Pubitemid 36858692)
    • (2003) Nature , vol.424 , Issue.6945 , pp. 219-223
    • Huang, C.1    Rajfur, Z.2    Borchers, C.3    Schaller, M.D.4    Jacobson, K.5
  • 28
    • 0032496358 scopus 로고    scopus 로고
    • The biochemical basis of an all-or-none cell fate switch in Xenopus oocytes
    • Ferrell JE, Jr, Machleder EM (1998) The biochemical basis of an all-or-none cell fate switch in Xenopus oocytes. Science 280:895-898.
    • (1998) Science , vol.280 , pp. 895-898
    • Ferrell Jr., J.E.1    Machleder, E.M.2
  • 29
    • 0345700833 scopus 로고    scopus 로고
    • Building a cell cycle oscillator: Hysteresis and bistability in the activation of Cdc2
    • Pomerening JR, Sontag ED, Ferrell JE, Jr (2003) Building a cell cycle oscillator: hysteresis and bistability in the activation of Cdc2. Nat Cell Biol 5:346-351.
    • (2003) Nat Cell Biol , vol.5 , pp. 346-351
    • Pomerening, J.R.1    Sontag, E.D.2    Ferrell Jr., J.E.3
  • 30
    • 8644266706 scopus 로고    scopus 로고
    • Stimulus-coupled spatial restriction of extracellular signal-regulated kinase 1/2 activity contributes to the specificity of signal-response pathways
    • DOI 10.1128/MCB.24.23.10145-10150.2004
    • Whitehurst A, Cobb MH, White MA (2004) Stimulus-coupled spatial restriction of extracellular signal-regulated kinase 1/2 activity contributes to the specificity of signal-response pathways. Mol Cell Biol 24:10145-10150. (Pubitemid 39507854)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.23 , pp. 10145-10150
    • Whitehurst, A.1    Cobb, M.H.2    White, M.A.3


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