메뉴 건너뛰기




Volumn 75, Issue 3, 2013, Pages 184-189

Protein phosphatase 2A dephosphorylates SNAP-25 through two distinct mechanisms in mouse brain synaptosomes

Author keywords

Calcium; Exocytosis; Phosphatase; SNARE protein; Synaptosome

Indexed keywords

4 AMINO 7 TERT BUTYL 5 (4 METHYLPHENYL)PYRAZOLO[3,4 D]PYRIMIDINE; CALYCULIN A; CYCLOSPORIN A; IONOMYCIN; OKADAIC ACID; PHORBOL DIBUTYRATE; PHOSPHOPROTEIN PHOSPHATASE 2A; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; TAUTOMYCIN;

EID: 84875962452     PISSN: 01680102     EISSN: 18728111     Source Type: Journal    
DOI: 10.1016/j.neures.2013.01.002     Document Type: Article
Times cited : (7)

References (45)
  • 2
    • 80054834577 scopus 로고    scopus 로고
    • Protein kinase C-dependent dephosphorylation of tyrosine hydroxylase requires the B56δ heterotrimeric form of protein phosphatase 2A
    • Ahn J.H., Kim Y., Kim H.S., Greengard P., Nairn A.C. Protein kinase C-dependent dephosphorylation of tyrosine hydroxylase requires the B56δ heterotrimeric form of protein phosphatase 2A. PLoS ONE 2011, 6:e26292.
    • (2011) PLoS ONE , vol.6
    • Ahn, J.H.1    Kim, Y.2    Kim, H.S.3    Greengard, P.4    Nairn, A.C.5
  • 4
    • 0038579784 scopus 로고    scopus 로고
    • Two modes of exocytosis from synaptosomes are differentially regulated by protein phosphatase types 2A and 2B
    • Baldwin M.L., Rostas J.A., Sim A.T. Two modes of exocytosis from synaptosomes are differentially regulated by protein phosphatase types 2A and 2B. J. Neurochem. 2003, 85:1190-1199.
    • (2003) J. Neurochem. , vol.85 , pp. 1190-1199
    • Baldwin, M.L.1    Rostas, J.A.2    Sim, A.T.3
  • 5
    • 0030695315 scopus 로고    scopus 로고
    • Amphiphysin I is associated with coated endocytic intermediates and undergoes stimulation-dependent dephosphorylation in nerve terminals
    • Bauerfeind R., Takei K., De Camilli P. Amphiphysin I is associated with coated endocytic intermediates and undergoes stimulation-dependent dephosphorylation in nerve terminals. J. Biol. Chem. 1997, 272:30984-30992.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30984-30992
    • Bauerfeind, R.1    Takei, K.2    De Camilli, P.3
  • 6
    • 27944476273 scopus 로고    scopus 로고
    • A role for protein phosphatases 1, 2A, and 2B in cerebellar long-term potentiation
    • Belmeguenai A., Hansel C. A role for protein phosphatases 1, 2A, and 2B in cerebellar long-term potentiation. J. Neurosci. 2005, 25:10768-10772.
    • (2005) J. Neurosci. , vol.25 , pp. 10768-10772
    • Belmeguenai, A.1    Hansel, C.2
  • 7
    • 0031027044 scopus 로고    scopus 로고
    • GAP-43: an intrinsic determinant of neuronal development and plasticity
    • Benowitz L.I., Routtenberg A. GAP-43: an intrinsic determinant of neuronal development and plasticity. Trends Neurosci. 1997, 20:84-91.
    • (1997) Trends Neurosci. , vol.20 , pp. 84-91
    • Benowitz, L.I.1    Routtenberg, A.2
  • 8
    • 41749114790 scopus 로고    scopus 로고
    • Aerine threonine phosphorylation
    • Academic Press, Amsterdam, G.J. Siegel, R.W. Albers, S.T. Brady, D.L. Price (Eds.)
    • Bibb J.A., Nestler E.J. Aerine threonine phosphorylation. Basic Neurochemistry. Molecular, Cellular and Medical Aspects 2006, Academic Press, Amsterdam, pp. 391. G.J. Siegel, R.W. Albers, S.T. Brady, D.L. Price (Eds.).
    • (2006) Basic Neurochemistry. Molecular, Cellular and Medical Aspects , pp. 391
    • Bibb, J.A.1    Nestler, E.J.2
  • 9
    • 33644770187 scopus 로고    scopus 로고
    • Structure and function of SNARE and SNARE-interacting proteins
    • Brunger A.T. Structure and function of SNARE and SNARE-interacting proteins. Q. Rev. Biophys. 2005, 38:1-47.
    • (2005) Q. Rev. Biophys. , vol.38 , pp. 1-47
    • Brunger, A.T.1
  • 10
    • 0028940325 scopus 로고
    • Identification of soluble protein phosphatases that dephosphorylate voltage-sensitive sodium channels in rat brain
    • Chen T.C., Law B., Kondratyuk T., Rossie S. Identification of soluble protein phosphatases that dephosphorylate voltage-sensitive sodium channels in rat brain. J. Biol. Chem. 1995, 270:7750-7756.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7750-7756
    • Chen, T.C.1    Law, B.2    Kondratyuk, T.3    Rossie, S.4
  • 11
    • 0034078320 scopus 로고    scopus 로고
    • FK506, an immunosuppressant targeting calcineurin function
    • Dumont F.J. FK506, an immunosuppressant targeting calcineurin function. Curr. Med. Chem. 2000, 7:731-748.
    • (2000) Curr. Med. Chem. , vol.7 , pp. 731-748
    • Dumont, F.J.1
  • 12
    • 0030924806 scopus 로고    scopus 로고
    • Differential inhibition and posttranslational modification of protein phosphatase 1 and 2A in MCF7 cells treated with calyculin-A, okadaic acid, and tautomycin
    • Favre B., Turowski P., Hemmings B.A. Differential inhibition and posttranslational modification of protein phosphatase 1 and 2A in MCF7 cells treated with calyculin-A, okadaic acid, and tautomycin. J. Biol. Chem. 1997, 272:13856-13863.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13856-13863
    • Favre, B.1    Turowski, P.2    Hemmings, B.A.3
  • 13
    • 3342924184 scopus 로고    scopus 로고
    • Regulation of choline transporter surface expression and phosphorylation by protein kinase C and protein phosphatase 1/2A
    • Gates J., Ferguson S.M., Blakely R.D., Apparsundaram S. Regulation of choline transporter surface expression and phosphorylation by protein kinase C and protein phosphatase 1/2A. J. Pharmacol. Exp. Ther. 2004, 310:536-545.
    • (2004) J. Pharmacol. Exp. Ther. , vol.310 , pp. 536-545
    • Gates, J.1    Ferguson, S.M.2    Blakely, R.D.3    Apparsundaram, S.4
  • 14
    • 0033031477 scopus 로고    scopus 로고
    • Activity-dependent phosphorylation of SNAP-25 in hippocampal organotypic cultures
    • Genoud S., Pralong W., Riederer B.M., Eder L., Catsicas S., Muller D. Activity-dependent phosphorylation of SNAP-25 in hippocampal organotypic cultures. J. Neurochem. 1999, 72:1699-1706.
    • (1999) J. Neurochem. , vol.72 , pp. 1699-1706
    • Genoud, S.1    Pralong, W.2    Riederer, B.M.3    Eder, L.4    Catsicas, S.5    Muller, D.6
  • 15
    • 0030176052 scopus 로고    scopus 로고
    • Protein kinase C enhances exocytosis from chromaffin cells by increasing the size of the readily releasable pool of secretory granules
    • Gillis K.D., Mößner R., Neher E. Protein kinase C enhances exocytosis from chromaffin cells by increasing the size of the readily releasable pool of secretory granules. Neuron 1996, 16:1209-1220.
    • (1996) Neuron , vol.16 , pp. 1209-1220
    • Gillis, K.D.1    Mößner, R.2    Neher, E.3
  • 16
    • 33744800245 scopus 로고    scopus 로고
    • Modulation of Kv2.1 channel gating and TEA sensitivity by distinct domains of SNAP-25
    • He Y., Kang Y., Leung Y.M., Xia F., Gao X., Xie H., Gaisano H.Y., Tsushima R.G. Modulation of Kv2.1 channel gating and TEA sensitivity by distinct domains of SNAP-25. Biochem. J. 2006, 396:363-369.
    • (2006) Biochem. J. , vol.396 , pp. 363-369
    • He, Y.1    Kang, Y.2    Leung, Y.M.3    Xia, F.4    Gao, X.5    Xie, H.6    Gaisano, H.Y.7    Tsushima, R.G.8
  • 17
    • 38149118182 scopus 로고    scopus 로고
    • Botulinum neurotoxin A and neurotoxin E cleavage products of synaptosome-associated protein of 25 kd exhibit distinct actions on pancreatic islet beta-cell Kv2.1 channel gating
    • He Y., Elias C.L., Huang Y.C., Gao X., Leung Y.M., Kang Y., Xie H., Chaddock J.A., Tsushima R.G., Gaisano H.Y. Botulinum neurotoxin A and neurotoxin E cleavage products of synaptosome-associated protein of 25 kd exhibit distinct actions on pancreatic islet beta-cell Kv2.1 channel gating. Pancreas 2008, 36:10-17.
    • (2008) Pancreas , vol.36 , pp. 10-17
    • He, Y.1    Elias, C.L.2    Huang, Y.C.3    Gao, X.4    Leung, Y.M.5    Kang, Y.6    Xie, H.7    Chaddock, J.A.8    Tsushima, R.G.9    Gaisano, H.Y.10
  • 18
    • 23844556932 scopus 로고    scopus 로고
    • SNAREs and traffic
    • Hong W. SNAREs and traffic. Biochim. Biophys. Acta 2005, 1744:493-517.
    • (2005) Biochim. Biophys. Acta , vol.1744 , pp. 493-517
    • Hong, W.1
  • 19
    • 0033809439 scopus 로고    scopus 로고
    • Two distinct mechanisms underlie the stimulation of neurotransmitter release by phorbol esters in clonal rat pheochromocytoma PC12 cells
    • Iwasaki S., Kataoka M., Sekiguchi M., Shimazaki Y., Sato K., Takahashi M. Two distinct mechanisms underlie the stimulation of neurotransmitter release by phorbol esters in clonal rat pheochromocytoma PC12 cells. J. Biochem. 2000, 128:407-414.
    • (2000) J. Biochem. , vol.128 , pp. 407-414
    • Iwasaki, S.1    Kataoka, M.2    Sekiguchi, M.3    Shimazaki, Y.4    Sato, K.5    Takahashi, M.6
  • 20
    • 0037459076 scopus 로고    scopus 로고
    • Membrane fusion
    • Jahn R., Lang T., Sudhof T.C. Membrane fusion. Cell 2003, 112:519-533.
    • (2003) Cell , vol.112 , pp. 519-533
    • Jahn, R.1    Lang, T.2    Sudhof, T.C.3
  • 22
    • 0035470838 scopus 로고    scopus 로고
    • 2+ channels, cytoplasmic messengers and proteins of the synaptic vesicle release complex
    • 2+ channels, cytoplasmic messengers and proteins of the synaptic vesicle release complex. Trends Pharmacol. Sci. 2001, 22:519-525.
    • (2001) Trends Pharmacol. Sci. , vol.22 , pp. 519-525
    • Jarvis, S.E.1    Zamponi, G.W.2
  • 27
    • 0032543766 scopus 로고    scopus 로고
    • Calcium triggers calcineurin-dependent synaptic vesicle recycling in mammalian nerve terminals
    • Marks B., McMahon H.T. Calcium triggers calcineurin-dependent synaptic vesicle recycling in mammalian nerve terminals. Curr. Biol. 1998, 8:740-749.
    • (1998) Curr. Biol. , vol.8 , pp. 740-749
    • Marks, B.1    McMahon, H.T.2
  • 30
    • 0027934706 scopus 로고
    • Calcineurin-mediated protein dephosphorylation in brain nerve terminals regulates the release of glutamate
    • Nichols R.A., Suplick G.R., Brown J.M. Calcineurin-mediated protein dephosphorylation in brain nerve terminals regulates the release of glutamate. J. Biol. Chem. 1994, 269:23817-23823.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23817-23823
    • Nichols, R.A.1    Suplick, G.R.2    Brown, J.M.3
  • 31
    • 0028966170 scopus 로고
    • Expression and complex formation of soluble N-ethyl-maleimide-sensitive factor attachment protein (SNAP) receptors in clonal rat endocrine cells
    • Oho C., Seino S., Takahashi M. Expression and complex formation of soluble N-ethyl-maleimide-sensitive factor attachment protein (SNAP) receptors in clonal rat endocrine cells. Neurosci. Lett. 1995, 186:208-210.
    • (1995) Neurosci. Lett. , vol.186 , pp. 208-210
    • Oho, C.1    Seino, S.2    Takahashi, M.3
  • 37
    • 0036459950 scopus 로고    scopus 로고
    • Protein kinase C-mediated translocation of secretory vesicles to plasma membrane and enhancement of neurotransmitter release from PC12 cells
    • Shoji-Kasai Y., Itakura M., Kataoka M., Yamamori S., Takahashi M. Protein kinase C-mediated translocation of secretory vesicles to plasma membrane and enhancement of neurotransmitter release from PC12 cells. Eur. J. Neurosci. 2002, 15:1390-1394.
    • (2002) Eur. J. Neurosci. , vol.15 , pp. 1390-1394
    • Shoji-Kasai, Y.1    Itakura, M.2    Kataoka, M.3    Yamamori, S.4    Takahashi, M.5
  • 39
  • 40
    • 0036024250 scopus 로고    scopus 로고
    • Negative regulation of exocytosis at the nerve terminal
    • Takahashi M., Ohnishi H. Negative regulation of exocytosis at the nerve terminal. Mol. Psychiatry 2002, 7:536-537.
    • (2002) Mol. Psychiatry , vol.7 , pp. 536-537
    • Takahashi, M.1    Ohnishi, H.2
  • 41
    • 0141955265 scopus 로고    scopus 로고
    • New aspects of neurotransmitter release and exocytosis: regulation of neurotransmitter release by phosphorylation
    • Takahashi M., Itakura M., Kataoka M. New aspects of neurotransmitter release and exocytosis: regulation of neurotransmitter release by phosphorylation. J. Pharmachol. Sci. 2003, 93:41-45.
    • (2003) J. Pharmachol. Sci. , vol.93 , pp. 41-45
    • Takahashi, M.1    Itakura, M.2    Kataoka, M.3
  • 42
    • 0033215370 scopus 로고    scopus 로고
    • Protein phosphorylation and the regulation of synaptic membrane traffic
    • Turner K.M., Burgoyne R.D., Morgan A. Protein phosphorylation and the regulation of synaptic membrane traffic. Trends Neurosci. 1999, 22:459-464.
    • (1999) Trends Neurosci. , vol.22 , pp. 459-464
    • Turner, K.M.1    Burgoyne, R.D.2    Morgan, A.3
  • 45
    • 48249120761 scopus 로고    scopus 로고
    • The basal level of intracellular calcium gates the activation of phosphoinositide 3-kinase - Akt signaling by brain-derived neurotrophic factor in cortical neurons
    • Zheng F., Soellner D., Nunez J., Wang H. The basal level of intracellular calcium gates the activation of phosphoinositide 3-kinase - Akt signaling by brain-derived neurotrophic factor in cortical neurons. J. Neurochem. 2008, 106:1259-1274.
    • (2008) J. Neurochem. , vol.106 , pp. 1259-1274
    • Zheng, F.1    Soellner, D.2    Nunez, J.3    Wang, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.