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Volumn 23, Issue 1, 2003, Pages 1-6

Actin-ATP hydrolysis is a major energy drain for neurons

Author keywords

Actin filament treadmilling; Cytoskeleton; Intracellular ATP; Ischemia; Jasplakinolide; Latrunculin

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ADENOSINE TRIPHOSPHATE; CALCIUM ION; CYTOCHALASIN D; JASPAMIDE; LATRUNCULIN A; MONOMER; OUABAIN; SODIUM ION;

EID: 0037220750     PISSN: 02706474     EISSN: None     Source Type: Journal    
DOI: 10.1523/jneurosci.23-01-00002.2003     Document Type: Article
Times cited : (227)

References (39)
  • 3
    • 0034784359 scopus 로고    scopus 로고
    • An energy budget for signaling in the grey matter of the brain
    • Attwell D, Laughlin SB (2001) An energy budget for signaling in the grey matter of the brain. J Cereb Blood Flow Metab 21:1133-1145.
    • (2001) J Cereb Blood Flow Metab , vol.21 , pp. 1133-1145
    • Attwell, D.1    Laughlin, S.B.2
  • 4
    • 0033280237 scopus 로고    scopus 로고
    • Proteins of the ADF/cofilin family: Essential regulators of actin dynamics
    • Bamburg JR (1999) Proteins of the ADF/cofilin family: Essential regulators of actin dynamics. Annu Rev Cell Dev Biol 15:185-230.
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 185-230
    • Bamburg, J.R.1
  • 5
    • 0032494082 scopus 로고    scopus 로고
    • The yeast V159N actin mutant reveals roles for actin dynamics in vivo
    • Belmont LD, Drubin DG (1998) The yeast V159N actin mutant reveals roles for actin dynamics in vivo. J Cell Biol 142:1289-1299.
    • (1998) J Cell Biol , vol.142 , pp. 1289-1299
    • Belmont, L.D.1    Drubin, D.G.2
  • 6
    • 0033019429 scopus 로고    scopus 로고
    • New actin mutants allow further characterization of the nucleotide binding cleft and drug binding sites
    • Belmont LD, Patterson GM, Drubin DG (1999) New actin mutants allow further characterization of the nucleotide binding cleft and drug binding sites. J Cell Sci 112:1325-1336.
    • (1999) J Cell Sci , vol.112 , pp. 1325-1336
    • Belmont, L.D.1    Patterson, G.M.2    Drubin, D.G.3
  • 7
    • 0031884084 scopus 로고    scopus 로고
    • Actin disassembles reversibly during electrically induced recycling of synaptic vesicles in cultured neurons
    • Bernstein BW, DeWit M, Bamburg JR (1998) Actin disassembles reversibly during electrically induced recycling of synaptic vesicles in cultured neurons. Mol Brain Res 53:236-250.
    • (1998) Mol Brain Res , vol.53 , pp. 236-250
    • Bernstein, B.W.1    DeWit, M.2    Bamburg, J.R.3
  • 8
    • 0034681423 scopus 로고    scopus 로고
    • Effects ofjasplakinolide on the kinetics of actin polymerization: An explanation for certain in vivo observations
    • Bubb MR, Spector I, Beyer BB, Fosen KM (2000) Effects ofjasplakinolide on the kinetics of actin polymerization: An explanation for certain in vivo observations. J Biol Chem 275:5163-5170.
    • (2000) J Biol Chem , vol.275 , pp. 5163-5170
    • Bubb, M.R.1    Spector, I.2    Beyer, B.B.3    Fosen, K.M.4
  • 9
    • 0032488917 scopus 로고    scopus 로고
    • Hibernation during hypoxia in cardiomyocytes: Role of mitochondria as the 02 sensor
    • Budinger GR, Duranteau J, Chandel NS, Schumacker PT (1998) Hibernation during hypoxia in cardiomyocytes: Role of mitochondria as the 02 sensor. J Biol Chem 273:3320-3326.
    • (1998) J Biol Chem , vol.273 , pp. 3320-3326
    • Budinger, G.R.1    Duranteau, J.2    Chandel, N.S.3    Schumacker, P.T.4
  • 13
    • 0033533744 scopus 로고    scopus 로고
    • Role of actin-filament disassembly in lamellipodium protrusion in motile cells revealed using the drug jasplakinolide
    • Cramer LP (1999) Role of actin-filament disassembly in lamellipodium protrusion in motile cells revealed using the drug jasplakinolide. Curr Biol 9:1095-1105.
    • (1999) Curr Biol , vol.9 , pp. 1095-1105
    • Cramer, L.P.1
  • 14
    • 0022453434 scopus 로고
    • Nucleotide exchange between cytosolic ATP and F-actin-bound ADP may be a major energy-utilizing process in unstimulated platelets
    • Daniel JL, Molish IR, Robkin L, Holmsen H (1986) Nucleotide exchange between cytosolic ATP and F-actin-bound ADP may be a major energy-utilizing process in unstimulated platelets. Eur J Biochem 156:677-684.
    • (1986) Eur J Biochem , vol.156 , pp. 677-684
    • Daniel, J.L.1    Molish, I.R.2    Robkin, L.3    Holmsen, H.4
  • 15
    • 0032475981 scopus 로고    scopus 로고
    • Synergy between actin depolymerizing factor/cofilin and profilin in increasing actin filament turnover
    • Didry D,Carlier MF,Pantaloni D (1998) Synergy between actin depolymerizing factor/cofilin and profilin in increasing actin filament turnover. J Biol Chem 273:25602-25611.
    • (1998) J Biol Chem , vol.273 , pp. 25602-25611
    • Didry, D.1    Carlier, M.F.2    Pantaloni, D.3
  • 17
    • 0023746711 scopus 로고
    • Two classes of actin microfilaments are associated with the inner cytoskeleton of axons
    • Fath KR, Lasek RJ (1988) Two classes of actin microfilaments are associated with the inner cytoskeleton of axons. J Cell Biol 107:613-621.
    • (1988) J Cell Biol , vol.107 , pp. 613-621
    • Fath, K.R.1    Lasek, R.J.2
  • 18
    • 0032078861 scopus 로고    scopus 로고
    • Rapid actin-based plasticity in dendritic spines
    • Fischer M, Kaech S, Knutti D, Matus A (1998) Rapid actin-based plasticity in dendritic spines. Neuron 20:847-854.
    • (1998) Neuron , vol.20 , pp. 847-854
    • Fischer, M.1    Kaech, S.2    Knutti, D.3    Matus, A.4
  • 19
    • 0024095187 scopus 로고
    • Actions of cytochalasins on the organization of actin filaments and microtubules in a neuronal growth cone
    • Forscher P, Smith SJ (1988) Actions of cytochalasins on the organization of actin filaments and microtubules in a neuronal growth cone. J Cell Biol 107:1505-1516.
    • (1988) J Cell Biol , vol.107 , pp. 1505-1516
    • Forscher, P.1    Smith, S.J.2
  • 20
    • 0028220530 scopus 로고
    • Removal of extracellular sodium prevents anoxia-induced injury in freshly dissociated rat CA1 hippocampal neurons
    • Friedman JE, Haddad GG (1994) Removal of extracellular sodium prevents anoxia-induced injury in freshly dissociated rat CA1 hippocampal neurons. Brain Res 641:57-64.
    • (1994) Brain Res , vol.641 , pp. 57-64
    • Friedman, J.E.1    Haddad, G.G.2
  • 21
    • 0026552005 scopus 로고
    • Postnatal development of electrogenic sodium pump activity in rat hippocampal pyramidal neurons
    • Fukuda A, Prince DA (1992) Postnatal development of electrogenic sodium pump activity in rat hippocampal pyramidal neurons. Brain Res Dev Brain Res 65:101-114.
    • (1992) Brain Res Dev Brain Res , vol.65 , pp. 101-114
    • Fukuda, A.1    Prince, D.A.2
  • 22
    • 0030807917 scopus 로고    scopus 로고
    • The actin-severing protein gelsolin modulates calcium channel and NMDA receptor activities and vulnerability to excitotoxicity in hippocampal neurons
    • Furukawa K, Fu WM, Li Y, Witke W, Kwiatkowski DJ, Mattson MP (1997) The actin-severing protein gelsolin modulates calcium channel and NMDA receptor activities and vulnerability to excitotoxicity in hippocampal neurons. J Neurosci 17:8178-8186.
    • (1997) J Neurosci , vol.17 , pp. 8178-8186
    • Furukawa, K.1    Fu, W.M.2    Li, Y.3    Witke, W.4    Kwiatkowski, D.J.5    Mattson, M.P.6
  • 23
    • 0023007962 scopus 로고
    • Actin polymerization: The mechanism of action of cytochalasin D
    • Goddette DW, Frieden C (1986) Actin polymerization: The mechanism of action of cytochalasin D. J Biol Chem 261:15974-15980.
    • (1986) J Biol Chem , vol.261 , pp. 15974-15980
    • Goddette, D.W.1    Frieden, C.2
  • 24
    • 0021895138 scopus 로고
    • 2+ indicators with greatly improved fluorescence properties
    • 2+ indicators with greatly improved fluorescence properties. J Biol Chem 260:3440-3450.
    • (1985) J Biol Chem , vol.260 , pp. 3440-3450
    • Grynkiewicz, G.1    Poenie, M.2    Tsien, R.Y.3
  • 27
    • 0036147184 scopus 로고    scopus 로고
    • Caffeine eliminates gamma-ray-induced g(2)-phase delay in human tumor cells but not in normal cells
    • Jha MN, Bamburg JR, Bernstein BW, Bedford JS (2002) Caffeine eliminates gamma-ray-induced g(2)-phase delay in human tumor cells but not in normal cells. Radiat Res 157:26-31.
    • (2002) Radiat Res , vol.157 , pp. 26-31
    • Jha, M.N.1    Bamburg, J.R.2    Bernstein, B.W.3    Bedford, J.S.4
  • 29
    • 0018642358 scopus 로고
    • Cation transport and membrane potential properties of primary astroglial cultures from neonatal rat brains
    • Kimelberg HK, Bowman C, Biddlecome S, Bourke RS (1979) Cation transport and membrane potential properties of primary astroglial cultures from neonatal rat brains. Brain Res 177:533-550.
    • (1979) Brain Res , vol.177 , pp. 533-550
    • Kimelberg, H.K.1    Bowman, C.2    Biddlecome, S.3    Bourke, R.S.4
  • 31
    • 0001064450 scopus 로고    scopus 로고
    • Brain energy metabolism
    • Zigmond MJ, Bloom FE, Landis SC, Roberts JL, Squire L, eds. San Diego: Academic
    • Magistretti PJ (1999) Brain energy metabolism. In: Fundamental Neuroscience (Zigmond MJ, Bloom FE, Landis SC, Roberts JL, Squire L, eds), p 389. San Diego: Academic.
    • (1999) Fundamental Neuroscience , pp. 389
    • Magistretti, P.J.1
  • 33
    • 0034282106 scopus 로고    scopus 로고
    • Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function
    • Minamide LS, Striegl AM, Boyle JA, Meberg PJ, Bamburg JR (2000) Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function. Nat Cell Biol 2:628-636.
    • (2000) Nat Cell Biol , vol.2 , pp. 628-636
    • Minamide, L.S.1    Striegl, A.M.2    Boyle, J.A.3    Meberg, P.J.4    Bamburg, J.R.5
  • 34
    • 0033046726 scopus 로고    scopus 로고
    • Divalent cation-, nucleotide-, and polymerization-dependent changes in the conformation of subdomain 2 of actin
    • Moraczewska J, Wawro B, Seguro K, Strzelecka-Golaszewska H (1999) Divalent cation-, nucleotide-, and polymerization-dependent changes in the conformation of subdomain 2 of actin. Biophys J 77:373-385.
    • (1999) Biophys J , vol.77 , pp. 373-385
    • Moraczewska, J.1    Wawro, B.2    Seguro, K.3    Strzelecka-Golaszewska, H.4
  • 35
    • 0033775855 scopus 로고    scopus 로고
    • Latrunculin alters the actin-monomer subunit interface to prevent polymerization
    • Morton WM, Ayscough KR, McLaughlin PJ (2000) Latrunculin alters the actin-monomer subunit interface to prevent polymerization. Nat Cell Biol 2:376-378.
    • (2000) Nat Cell Biol , vol.2 , pp. 376-378
    • Morton, W.M.1    Ayscough, K.R.2    McLaughlin, P.J.3
  • 36
    • 0001256679 scopus 로고    scopus 로고
    • The metabolism of the central nervous system in vivo
    • Field J, Magoun HW, Hall VE, eds. Washington, DC: American Physiological Society
    • Sokoloff L (1996) The metabolism of the central nervous system in vivo. In: Handbook of Physiology-Neurophysiology (Field J, Magoun HW, Hall VE, eds), pp 1843-1864. Washington, DC: American Physiological Society.
    • (1996) Handbook of Physiology-Neurophysiology , pp. 1843-1864
    • Sokoloff, L.1
  • 37
    • 0032829103 scopus 로고    scopus 로고
    • New anti-actin drugs in the study of the organization and function of the actin cytoskeleton
    • Spector I, Braet F, Shochet NR, Bubb MR (1999) New anti-actin drugs in the study of the organization and function of the actin cytoskeleton. Microsc Res Tech 47:18-37.
    • (1999) Microsc Res Tech , vol.47 , pp. 18-37
    • Spector, I.1    Braet, F.2    Shochet, N.R.3    Bubb, M.R.4
  • 38
    • 0035894864 scopus 로고    scopus 로고
    • 2+ ATPase in post-tetanic potentiation at crayfish neuromuscular junctions
    • 2+ ATPase in post-tetanic potentiation at crayfish neuromuscular junctions. J Neurosci 21:9598-9607.
    • (2001) J Neurosci , vol.21 , pp. 9598-9607
    • Zhong, N.1    Beaumont, V.2    Zucker, R.S.3
  • 39
    • 0027293382 scopus 로고
    • Recent quantitative studies of actin filament turnover during cell locomotion
    • Zigmond SH (1993) Recent quantitative studies of actin filament turnover during cell locomotion. Cell Motil Cytoskel 25:309-316.
    • (1993) Cell Motil Cytoskel , vol.25 , pp. 309-316
    • Zigmond, S.H.1


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