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Volumn 154, Issue 1-3, 2014, Pages 36-41

Alterations of the myristoylated, alanine-rich C kinase substrate (MARCKS) in prefrontal cortex in schizophrenia

Author keywords

Cytoskeleton; Dendritic dynamics; Myristoylation; Neurotransmission; Synaptic plasticity

Indexed keywords

MARCKS PROTEIN; PEPTIDES AND PROTEINS; PROTEIN N MYRISTOYLTRANSFERASE; PROTEIN NIP71; UNCLASSIFIED DRUG; HALOPERIDOL; HALOPERIDOL DECANOATE; MEMBRANE PROTEIN; MYRISTOYLATED ALANINE-RICH C KINASE SUBSTRATE; N-MYRISTOYLTRANSFERASE INHIBITOR PROTEIN 71, HUMAN; NEUROLEPTIC AGENT; SIGNAL PEPTIDE; TUMOR PROTEIN;

EID: 84897029323     PISSN: 09209964     EISSN: 15732509     Source Type: Journal    
DOI: 10.1016/j.schres.2014.02.003     Document Type: Article
Times cited : (19)

References (73)
  • 1
    • 0026472164 scopus 로고
    • The MARCKS brothers: a family of protein kinase C substrates
    • Aderem A. The MARCKS brothers: a family of protein kinase C substrates. Cell 1992, 71(5):713-716.
    • (1992) Cell , vol.71 , Issue.5 , pp. 713-716
    • Aderem, A.1
  • 2
    • 77956493486 scopus 로고    scopus 로고
    • The dynamics of excitatory synapse formation on dendritic spines
    • Amaral M.D., Pozzo-Miller L. The dynamics of excitatory synapse formation on dendritic spines. Cellscience 2009, 5(4):19-25.
    • (2009) Cellscience , vol.5 , Issue.4 , pp. 19-25
    • Amaral, M.D.1    Pozzo-Miller, L.2
  • 3
    • 84879970825 scopus 로고    scopus 로고
    • Presynaptic neurexin-3 alternative splicing trans-synaptically controls postsynaptic AMPA receptor trafficking
    • Aoto J., Martinelli D.C., Malenka R.C., Tabuchi K., Sudhof T.C. Presynaptic neurexin-3 alternative splicing trans-synaptically controls postsynaptic AMPA receptor trafficking. Cell 2013, 154(1):75-88.
    • (2013) Cell , vol.154 , Issue.1 , pp. 75-88
    • Aoto, J.1    Martinelli, D.C.2    Malenka, R.C.3    Tabuchi, K.4    Sudhof, T.C.5
  • 4
    • 0037083896 scopus 로고    scopus 로고
    • Cross-talk unfolded: MARCKS proteins
    • Arbuzova A., Schmitz A.A., Vergeres G. Cross-talk unfolded: MARCKS proteins. Biochem. J. 2002, 362(Pt 1):1-12.
    • (2002) Biochem. J. , vol.362 , Issue.PART 1 , pp. 1-12
    • Arbuzova, A.1    Schmitz, A.A.2    Vergeres, G.3
  • 5
    • 0030869425 scopus 로고    scopus 로고
    • Kinetics of interaction of the myristoylated alanine-rich C kinase substrate, membranes, and calmodulin
    • Arbuzova A., Wang J., Murray D., Jacob J., Cafiso D.S., McLaughlin S. Kinetics of interaction of the myristoylated alanine-rich C kinase substrate, membranes, and calmodulin. J. Biol. Chem. 1997, 272(43):27167-27177.
    • (1997) J. Biol. Chem. , vol.272 , Issue.43 , pp. 27167-27177
    • Arbuzova, A.1    Wang, J.2    Murray, D.3    Jacob, J.4    Cafiso, D.S.5    McLaughlin, S.6
  • 6
    • 84867125875 scopus 로고    scopus 로고
    • Neuromodulation of thought: flexibilities and vulnerabilities in prefrontal cortical network synapses
    • Arnsten A.F., Wang M.J., Paspalas C.D. Neuromodulation of thought: flexibilities and vulnerabilities in prefrontal cortical network synapses. Neuron 2012, 76(1):223-239.
    • (2012) Neuron , vol.76 , Issue.1 , pp. 223-239
    • Arnsten, A.F.1    Wang, M.J.2    Paspalas, C.D.3
  • 8
    • 25644436461 scopus 로고    scopus 로고
    • Essential role for the PKC target MARCKS in maintaining dendritic spine morphology
    • Calabrese B., Halpain S. Essential role for the PKC target MARCKS in maintaining dendritic spine morphology. Neuron 2005, 48(1):77-90.
    • (2005) Neuron , vol.48 , Issue.1 , pp. 77-90
    • Calabrese, B.1    Halpain, S.2
  • 10
    • 84875200034 scopus 로고    scopus 로고
    • Remodeling chromatin and synapses in depression
    • Duman R.S. Remodeling chromatin and synapses in depression. Nat. Med. 2013, 19(3):267.
    • (2013) Nat. Med. , vol.19 , Issue.3 , pp. 267
    • Duman, R.S.1
  • 11
    • 65349191920 scopus 로고    scopus 로고
    • The neurodevelopmental hypothesis of schizophrenia, revisited
    • Fatemi S.H., Folsom T.D. The neurodevelopmental hypothesis of schizophrenia, revisited. Schizophr. Bull. 2009, 35(3):528-548.
    • (2009) Schizophr. Bull. , vol.35 , Issue.3 , pp. 528-548
    • Fatemi, S.H.1    Folsom, T.D.2
  • 13
    • 77956466815 scopus 로고    scopus 로고
    • When cortical development goes wrong: schizophrenia as a neurodevelopmental disease of microcircuits
    • Garey L. When cortical development goes wrong: schizophrenia as a neurodevelopmental disease of microcircuits. J. Anat. 2010, 217(4):324-333.
    • (2010) J. Anat. , vol.217 , Issue.4 , pp. 324-333
    • Garey, L.1
  • 14
    • 36049013008 scopus 로고    scopus 로고
    • Polysialic acid-neural cell adhesion molecule in brain plasticity: from synapses to integration of new neurons
    • Gascon E., Vutskits L., Kiss J.Z. Polysialic acid-neural cell adhesion molecule in brain plasticity: from synapses to integration of new neurons. Brain Res. Rev. 2007, 56(1):101-118.
    • (2007) Brain Res. Rev. , vol.56 , Issue.1 , pp. 101-118
    • Gascon, E.1    Vutskits, L.2    Kiss, J.Z.3
  • 15
    • 84868304259 scopus 로고    scopus 로고
    • Alterations in the expression of PSA-NCAM and synaptic proteins in the dorsolateral prefrontal cortex of psychiatric disorder patients
    • Gilabert-Juan J., Varea E., Guirado R., Blasco-Ibanez J.M., Crespo C., Nacher J. Alterations in the expression of PSA-NCAM and synaptic proteins in the dorsolateral prefrontal cortex of psychiatric disorder patients. Neurosci. Lett. 2012, 530(1):97-102.
    • (2012) Neurosci. Lett. , vol.530 , Issue.1 , pp. 97-102
    • Gilabert-Juan, J.1    Varea, E.2    Guirado, R.3    Blasco-Ibanez, J.M.4    Crespo, C.5    Nacher, J.6
  • 17
    • 84884288041 scopus 로고    scopus 로고
    • Dendritic spine pathology in schizophrenia
    • Glausier J.R., Lewis D.A. Dendritic spine pathology in schizophrenia. Neuroscience 2013, 251:90-107.
    • (2013) Neuroscience , vol.251 , pp. 90-107
    • Glausier, J.R.1    Lewis, D.A.2
  • 19
    • 5344224076 scopus 로고    scopus 로고
    • Cathepsin B-like proteolysis and MARCKS degradation in sub-lethal NMDA-induced collapse of dendritic spines
    • Graber S., Maiti S., Halpain S. Cathepsin B-like proteolysis and MARCKS degradation in sub-lethal NMDA-induced collapse of dendritic spines. Neuropharmacology 2004, 47(5):706-713.
    • (2004) Neuropharmacology , vol.47 , Issue.5 , pp. 706-713
    • Graber, S.1    Maiti, S.2    Halpain, S.3
  • 21
    • 18844385201 scopus 로고    scopus 로고
    • Increased N-acetylaspartate in rat striatum following long-term administration of haloperidol
    • Harte M.K., Bachus S.B., Reynolds G.P. Increased N-acetylaspartate in rat striatum following long-term administration of haloperidol. Schizophr. Res. 2005, 75(2-3):303-308.
    • (2005) Schizophr. Res. , vol.75 , Issue.2-3 , pp. 303-308
    • Harte, M.K.1    Bachus, S.B.2    Reynolds, G.P.3
  • 22
    • 0026513601 scopus 로고
    • MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium-calmodulin
    • Hartwig J.H., Thelen M., Rosen A., Janmey P.A., Nairn A.C., Aderem A. MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium-calmodulin. Nature 1992, 356(6370):618-622.
    • (1992) Nature , vol.356 , Issue.6370 , pp. 618-622
    • Hartwig, J.H.1    Thelen, M.2    Rosen, A.3    Janmey, P.A.4    Nairn, A.C.5    Aderem, A.6
  • 24
    • 0032124808 scopus 로고    scopus 로고
    • Visual imprinting and the neural mechanisms of recognition memory
    • Horn G. Visual imprinting and the neural mechanisms of recognition memory. Trends Neurosci. 1998, 21(7):300-305.
    • (1998) Trends Neurosci. , vol.21 , Issue.7 , pp. 300-305
    • Horn, G.1
  • 26
    • 84886951417 scopus 로고    scopus 로고
    • Age-dependent regulation of synaptic connections by dopamine D2 receptors
    • Jia J.M., Zhao J., Hu Z., Lindberg D., Li Z. Age-dependent regulation of synaptic connections by dopamine D2 receptors. Nat. Neurosci. 2013, 16(11):1627-1636.
    • (2013) Nat. Neurosci. , vol.16 , Issue.11 , pp. 1627-1636
    • Jia, J.M.1    Zhao, J.2    Hu, Z.3    Lindberg, D.4    Li, Z.5
  • 27
    • 0022539842 scopus 로고
    • Effects of intermittent and continuous haloperidol administration on the dopaminergic system in the rat brain
    • Kashihara K., Sato M., Fujiwara Y., Harada T., Ogawa T., Otsuki S. Effects of intermittent and continuous haloperidol administration on the dopaminergic system in the rat brain. Biol. Psychiatry 1986, 21(7):650-656.
    • (1986) Biol. Psychiatry , vol.21 , Issue.7 , pp. 650-656
    • Kashihara, K.1    Sato, M.2    Fujiwara, Y.3    Harada, T.4    Ogawa, T.5    Otsuki, S.6
  • 30
    • 11144256944 scopus 로고    scopus 로고
    • Modulation of neurotransmitter release by the second messenger-activated protein kinases: implications for presynaptic plasticity
    • Leenders A.G., Sheng Z.H. Modulation of neurotransmitter release by the second messenger-activated protein kinases: implications for presynaptic plasticity. Pharmacol. Ther. 2005, 105(1):69-84.
    • (2005) Pharmacol. Ther. , vol.105 , Issue.1 , pp. 69-84
    • Leenders, A.G.1    Sheng, Z.H.2
  • 31
    • 0030454553 scopus 로고    scopus 로고
    • Myristoylated alanine-rich C kinase substrate (MARCKS): a molecular target for the therapeutic action of mood stabilizers in the brain?
    • (discussion 32-23)
    • Lenox R.H., McNamara R.K., Watterson J.M., Watson D.G. Myristoylated alanine-rich C kinase substrate (MARCKS): a molecular target for the therapeutic action of mood stabilizers in the brain?. J. Clin. Psychiatry 1996, 57(Suppl. 13):23-31. (discussion 32-23).
    • (1996) J. Clin. Psychiatry , vol.57 , Issue.SUPPL. 13 , pp. 23-31
    • Lenox, R.H.1    McNamara, R.K.2    Watterson, J.M.3    Watson, D.G.4
  • 32
    • 58149300222 scopus 로고    scopus 로고
    • Actin filament assembly by myristoylated alanine-rich C kinase substrate-phosphatidylinositol-4,5-diphosphate signaling is critical for dendrite branching
    • Li H., Chen G., Zhou B., Duan S. Actin filament assembly by myristoylated alanine-rich C kinase substrate-phosphatidylinositol-4,5-diphosphate signaling is critical for dendrite branching. Mol. Biol. Cell 2008, 19(11):4804-4813.
    • (2008) Mol. Biol. Cell , vol.19 , Issue.11 , pp. 4804-4813
    • Li, H.1    Chen, G.2    Zhou, B.3    Duan, S.4
  • 33
    • 25644435751 scopus 로고    scopus 로고
    • MARCKS for maintenance in dendritic spines
    • Matus A. MARCKS for maintenance in dendritic spines. Neuron 2005, 48(1):4-5.
    • (2005) Neuron , vol.48 , Issue.1 , pp. 4-5
    • Matus, A.1
  • 34
    • 0029058605 scopus 로고
    • The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions
    • McLaughlin S., Aderem A. The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions. Trends Biochem. Sci. 1995, 20(7):272-276.
    • (1995) Trends Biochem. Sci. , vol.20 , Issue.7 , pp. 272-276
    • McLaughlin, S.1    Aderem, A.2
  • 36
    • 23844529482 scopus 로고    scopus 로고
    • Effect of myristoylated alanine-rich C kinase substrate (MARCKS) overexpression on hippocampus-dependent learning and hippocampal synaptic plasticity in MARCKS transgenic mice
    • McNamara R.K., Hussain R.J., Simon E.J., Stumpo D.J., Blackshear P.J., Abel T., Lenox R.H. Effect of myristoylated alanine-rich C kinase substrate (MARCKS) overexpression on hippocampus-dependent learning and hippocampal synaptic plasticity in MARCKS transgenic mice. Hippocampus 2005, 15(5):675-683.
    • (2005) Hippocampus , vol.15 , Issue.5 , pp. 675-683
    • McNamara, R.K.1    Hussain, R.J.2    Simon, E.J.3    Stumpo, D.J.4    Blackshear, P.J.5    Abel, T.6    Lenox, R.H.7
  • 37
    • 0031055532 scopus 로고    scopus 로고
    • Comparative distribution of myristoylated alanine-rich C kinase substrate (MARCKS) and F1/GAP-43 gene expression in the adult rat brain
    • McNamara R.K., Lenox R.H. Comparative distribution of myristoylated alanine-rich C kinase substrate (MARCKS) and F1/GAP-43 gene expression in the adult rat brain. J. Comp. Neurol. 1997, 379(1):48-71.
    • (1997) J. Comp. Neurol. , vol.379 , Issue.1 , pp. 48-71
    • McNamara, R.K.1    Lenox, R.H.2
  • 38
    • 35448979574 scopus 로고    scopus 로고
    • The role of electrostatic and nonpolar interactions in the association of peripheral proteins with membranes
    • Murray D., Arbuzova A., Honig B., McLaughlin S. The role of electrostatic and nonpolar interactions in the association of peripheral proteins with membranes. Curr. Top. Membr. 2002, 52:277-307.
    • (2002) Curr. Top. Membr. , vol.52 , pp. 277-307
    • Murray, D.1    Arbuzova, A.2    Honig, B.3    McLaughlin, S.4
  • 39
    • 0031571632 scopus 로고    scopus 로고
    • Electrostatic interaction of myristoylated proteins with membranes: simple physics, complicated biology
    • Murray D., Ben-Tal N., Honig B., McLaughlin S. Electrostatic interaction of myristoylated proteins with membranes: simple physics, complicated biology. Structure 1997, 5(8):985-989.
    • (1997) Structure , vol.5 , Issue.8 , pp. 985-989
    • Murray, D.1    Ben-Tal, N.2    Honig, B.3    McLaughlin, S.4
  • 42
    • 0025423954 scopus 로고
    • Localization of the MARCKS (87kDa) protein, a major specific substrate for protein kinase C, in rat brain
    • Ouimet C.C., Wang J.K., Walaas S.I., Albert K.A., Greengard P. Localization of the MARCKS (87kDa) protein, a major specific substrate for protein kinase C, in rat brain. J. Neurosci. 1990, 10(5):1683-1698.
    • (1990) J. Neurosci. , vol.10 , Issue.5 , pp. 1683-1698
    • Ouimet, C.C.1    Wang, J.K.2    Walaas, S.I.3    Albert, K.A.4    Greengard, P.5
  • 43
    • 0038721947 scopus 로고    scopus 로고
    • Altered expression and phosphorylation of myristoylated alanine-rich C kinase substrate (MARCKS) in postmortem brain of suicide victims with or without depression
    • Pandey G.N., Dwivedi Y., Ren X., Rizavi H.S., Roberts R.C., Conley R.R., Tamminga C. Altered expression and phosphorylation of myristoylated alanine-rich C kinase substrate (MARCKS) in postmortem brain of suicide victims with or without depression. J. Psychiatr. Res. 2003, 37(5):421-432.
    • (2003) J. Psychiatr. Res. , vol.37 , Issue.5 , pp. 421-432
    • Pandey, G.N.1    Dwivedi, Y.2    Ren, X.3    Rizavi, H.S.4    Roberts, R.C.5    Conley, R.R.6    Tamminga, C.7
  • 44
    • 0036148617 scopus 로고    scopus 로고
    • Protein kinase C and phospholipase C activity and expression of their specific isozymes is decreased and expression of MARCKS is increased in platelets of bipolar but not in unipolar patients
    • Pandey G.N., Dwivedi Y., SridharaRao J., Ren X., Janicak P.G., Sharma R. Protein kinase C and phospholipase C activity and expression of their specific isozymes is decreased and expression of MARCKS is increased in platelets of bipolar but not in unipolar patients. Neuropsychopharmacology 2002, 26(2):216-228.
    • (2002) Neuropsychopharmacology , vol.26 , Issue.2 , pp. 216-228
    • Pandey, G.N.1    Dwivedi, Y.2    SridharaRao, J.3    Ren, X.4    Janicak, P.G.5    Sharma, R.6
  • 45
    • 84855340012 scopus 로고    scopus 로고
    • Dysbindin-1 modulates prefrontal cortical activity and schizophrenia-like behaviors via dopamine/D2 pathways
    • Papaleo F., Yang F., Garcia S., Chen J., Lu B., Crawley J.N., Weinberger D.R. Dysbindin-1 modulates prefrontal cortical activity and schizophrenia-like behaviors via dopamine/D2 pathways. Mol. Psychiatry 2012, 17(1):85-98.
    • (2012) Mol. Psychiatry , vol.17 , Issue.1 , pp. 85-98
    • Papaleo, F.1    Yang, F.2    Garcia, S.3    Chen, J.4    Lu, B.5    Crawley, J.N.6    Weinberger, D.R.7
  • 48
    • 0033838076 scopus 로고    scopus 로고
    • Protein kinase C alpha-dependent phosphorylation of Golgi proteins
    • Radau B., Otto A., Muller E.C., Westermann P. Protein kinase C alpha-dependent phosphorylation of Golgi proteins. Electrophoresis 2000, 21(13):2684-2687.
    • (2000) Electrophoresis , vol.21 , Issue.13 , pp. 2684-2687
    • Radau, B.1    Otto, A.2    Muller, E.C.3    Westermann, P.4
  • 49
    • 0032692358 scopus 로고    scopus 로고
    • Differential changes in the phosphorylation of the protein kinase C substrates myristoylated alanine-rich C kinase substrate and growth-associated protein-43/B-50 following Schaffer collateral long-term potentiation and long-term depression
    • Ramakers G.M., McNamara R.K., Lenox R.H., De Graan P.N. Differential changes in the phosphorylation of the protein kinase C substrates myristoylated alanine-rich C kinase substrate and growth-associated protein-43/B-50 following Schaffer collateral long-term potentiation and long-term depression. J. Neurochem. 1999, 73(5):2175-2183.
    • (1999) J. Neurochem. , vol.73 , Issue.5 , pp. 2175-2183
    • Ramakers, G.M.1    McNamara, R.K.2    Lenox, R.H.3    De Graan, P.N.4
  • 50
    • 0345102483 scopus 로고    scopus 로고
    • Nonelectrostatic contributions to the binding of MARCKS-related protein to lipid bilayers
    • Ramsden J.J., Vergeres G. Nonelectrostatic contributions to the binding of MARCKS-related protein to lipid bilayers. Arch. Biochem. Biophys. 1999, 371(2):241-245.
    • (1999) Arch. Biochem. Biophys. , vol.371 , Issue.2 , pp. 241-245
    • Ramsden, J.J.1    Vergeres, G.2
  • 51
    • 0035965243 scopus 로고    scopus 로고
    • Chromaffin cell F-actin disassembly and potentiation of catecholamine release in response to protein kinase C activation by phorbol esters is mediated through myristoylated alanine-rich C kinase substrate phosphorylation
    • Rose S.D., Lejen T., Zhang L., Trifaro J.M. Chromaffin cell F-actin disassembly and potentiation of catecholamine release in response to protein kinase C activation by phorbol esters is mediated through myristoylated alanine-rich C kinase substrate phosphorylation. J. Biol. Chem. 2001, 276(39):36757-36763.
    • (2001) J. Biol. Chem. , vol.276 , Issue.39 , pp. 36757-36763
    • Rose, S.D.1    Lejen, T.2    Zhang, L.3    Trifaro, J.M.4
  • 52
    • 84860211462 scopus 로고    scopus 로고
    • Abnormalities of the Duo/Ras-related C3 botulinum toxin substrate 1/p21-activated kinase 1 pathway drive myosin light chain phosphorylation in frontal cortex in schizophrenia
    • Rubio M.D., Haroutunian V., Meador-Woodruff J.H. Abnormalities of the Duo/Ras-related C3 botulinum toxin substrate 1/p21-activated kinase 1 pathway drive myosin light chain phosphorylation in frontal cortex in schizophrenia. Biol. Psychiatry 2012, 71(10):906-914.
    • (2012) Biol. Psychiatry , vol.71 , Issue.10 , pp. 906-914
    • Rubio, M.D.1    Haroutunian, V.2    Meador-Woodruff, J.H.3
  • 53
    • 37349120002 scopus 로고    scopus 로고
    • Polysialic acid in the plasticity of the developing and adult vertebrate nervous system
    • Rutishauser U. Polysialic acid in the plasticity of the developing and adult vertebrate nervous system. Nat. Rev. Neurosci. 2008, 9(1):26-35.
    • (2008) Nat. Rev. Neurosci. , vol.9 , Issue.1 , pp. 26-35
    • Rutishauser, U.1
  • 54
    • 84875962461 scopus 로고    scopus 로고
    • Potential molecular mechanisms for decreased synaptic glutamate release in dysbindin-1 mutant mice
    • Saggu S., Cannon T.D., Jentsch J.D., Lavin A. Potential molecular mechanisms for decreased synaptic glutamate release in dysbindin-1 mutant mice. Schizophr. Res. 2013, 146(1-3):254-263.
    • (2013) Schizophr. Res. , vol.146 , Issue.1-3 , pp. 254-263
    • Saggu, S.1    Cannon, T.D.2    Jentsch, J.D.3    Lavin, A.4
  • 55
    • 0141989959 scopus 로고    scopus 로고
    • New aspects of neurotransmitter release and exocytosis: Rho-kinase-dependent myristoylated alanine-rich C-kinase substrate phosphorylation and regulation of neurofilament structure in neuronal cells
    • Sasaki Y. New aspects of neurotransmitter release and exocytosis: Rho-kinase-dependent myristoylated alanine-rich C-kinase substrate phosphorylation and regulation of neurofilament structure in neuronal cells. J. Pharmacol. Sci. 2003, 93(1):35-40.
    • (2003) J. Pharmacol. Sci. , vol.93 , Issue.1 , pp. 35-40
    • Sasaki, Y.1
  • 56
    • 84857916012 scopus 로고    scopus 로고
    • PSA-NCAM: synaptic functions mediated by its interactions with proteoglycans and glutamate receptors
    • Senkov O., Tikhobrazova O., Dityatev A. PSA-NCAM: synaptic functions mediated by its interactions with proteoglycans and glutamate receptors. Int. J. Biochem. Cell Biol. 2012, 44(4):591-595.
    • (2012) Int. J. Biochem. Cell Biol. , vol.44 , Issue.4 , pp. 591-595
    • Senkov, O.1    Tikhobrazova, O.2    Dityatev, A.3
  • 57
    • 0029780527 scopus 로고    scopus 로고
    • Molecular determinants of the myristoyl-electrostatic switch of MARCKS
    • Seykora J.T., Myat M.M., Allen L.A., Ravetch J.V., Aderem A. Molecular determinants of the myristoyl-electrostatic switch of MARCKS. J. Biol. Chem. 1996, 271(31):18797-18802.
    • (1996) J. Biol. Chem. , vol.271 , Issue.31 , pp. 18797-18802
    • Seykora, J.T.1    Myat, M.M.2    Allen, L.A.3    Ravetch, J.V.4    Aderem, A.5
  • 58
    • 0027509672 scopus 로고
    • Learning selectively increases protein kinase C substrate phosphorylation in specific regions of the chick brain
    • Sheu F.S., McCabe B.J., Horn G., Routtenberg A. Learning selectively increases protein kinase C substrate phosphorylation in specific regions of the chick brain. Proc. Natl. Acad. Sci. U. S. A. 1993, 90(7):2705-2709.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , Issue.7 , pp. 2705-2709
    • Sheu, F.S.1    McCabe, B.J.2    Horn, G.3    Routtenberg, A.4
  • 59
    • 0035943628 scopus 로고    scopus 로고
    • Overexpression of the myristoylated alanine-rich C-kinase substrate inhibits cell adhesion to extracellular matrix components
    • Spizz G., Blackshear P.J. Overexpression of the myristoylated alanine-rich C-kinase substrate inhibits cell adhesion to extracellular matrix components. J. Biol. Chem. 2001, 276(34):32264-32273.
    • (2001) J. Biol. Chem. , vol.276 , Issue.34 , pp. 32264-32273
    • Spizz, G.1    Blackshear, P.J.2
  • 61
  • 63
    • 15444365811 scopus 로고    scopus 로고
    • MARCKS is a natively unfolded protein with an inaccessible actin-binding site: evidence for long-range intramolecular interactions
    • Tapp H., Al-Naggar I.M., Yarmola E.G., Harrison A., Shaw G., Edison A.S., Bubb M.R. MARCKS is a natively unfolded protein with an inaccessible actin-binding site: evidence for long-range intramolecular interactions. J. Biol. Chem. 2005, 280(11):9946-9956.
    • (2005) J. Biol. Chem. , vol.280 , Issue.11 , pp. 9946-9956
    • Tapp, H.1    Al-Naggar, I.M.2    Yarmola, E.G.3    Harrison, A.4    Shaw, G.5    Edison, A.S.6    Bubb, M.R.7
  • 64
    • 84874786646 scopus 로고    scopus 로고
    • Functional role of the interaction between polysialic acid and myristoylated alanine-rich C kinase substrate at the plasma membrane
    • Theis T., Mishra B., von der Ohe M., Loers G., Prondzynski M., Pless O., Blackshear P.J., Schachner M., Kleene R. Functional role of the interaction between polysialic acid and myristoylated alanine-rich C kinase substrate at the plasma membrane. J. Biol. Chem. 2013, 288(9):6726-6742.
    • (2013) J. Biol. Chem. , vol.288 , Issue.9 , pp. 6726-6742
    • Theis, T.1    Mishra, B.2    von der Ohe, M.3    Loers, G.4    Prondzynski, M.5    Pless, O.6    Blackshear, P.J.7    Schachner, M.8    Kleene, R.9
  • 67
    • 0029147499 scopus 로고
    • The myristoyl moiety of myristoylated alanine-rich C kinase substrate (MARCKS) and MARCKS-related protein is embedded in the membrane
    • Vergeres G., Manenti S., Weber T., Sturzinger C. The myristoyl moiety of myristoylated alanine-rich C kinase substrate (MARCKS) and MARCKS-related protein is embedded in the membrane. J. Biol. Chem. 1995, 270(34):19879-19887.
    • (1995) J. Biol. Chem. , vol.270 , Issue.34 , pp. 19879-19887
    • Vergeres, G.1    Manenti, S.2    Weber, T.3    Sturzinger, C.4
  • 68
    • 0034212426 scopus 로고    scopus 로고
    • Modulation of calcium-evoked [3H]noradrenaline release from permeabilized cerebrocortical synaptosomes by the MARCKS protein, calmodulin and the actin cytoskeleton
    • Walaas S.I., Sefland I. Modulation of calcium-evoked [3H]noradrenaline release from permeabilized cerebrocortical synaptosomes by the MARCKS protein, calmodulin and the actin cytoskeleton. Neurochem. Int. 2000, 36(7):581-593.
    • (2000) Neurochem. Int. , vol.36 , Issue.7 , pp. 581-593
    • Walaas, S.I.1    Sefland, I.2
  • 69
    • 0035895882 scopus 로고    scopus 로고
    • The effector domain of myristoylated alanine-rich C kinase substrate binds strongly to phosphatidylinositol 4,5-bisphosphate
    • Wang J., Arbuzova A., Hangyas-Mihalyne G., McLaughlin S. The effector domain of myristoylated alanine-rich C kinase substrate binds strongly to phosphatidylinositol 4,5-bisphosphate. J. Biol. Chem. 2001, 276(7):5012-5019.
    • (2001) J. Biol. Chem. , vol.276 , Issue.7 , pp. 5012-5019
    • Wang, J.1    Arbuzova, A.2    Hangyas-Mihalyne, G.3    McLaughlin, S.4
  • 70
    • 0037072757 scopus 로고    scopus 로고
    • Lateral sequestration of phosphatidylinositol 4,5-bisphosphate by the basic effector domain of myristoylated alanine-rich C kinase substrate is due to nonspecific electrostatic interactions
    • Wang J., Gambhir A., Hangyas-Mihalyne G., Murray D., Golebiewska U., McLaughlin S. Lateral sequestration of phosphatidylinositol 4,5-bisphosphate by the basic effector domain of myristoylated alanine-rich C kinase substrate is due to nonspecific electrostatic interactions. J. Biol. Chem. 2002, 277(37):34401-34412.
    • (2002) J. Biol. Chem. , vol.277 , Issue.37 , pp. 34401-34412
    • Wang, J.1    Gambhir, A.2    Hangyas-Mihalyne, G.3    Murray, D.4    Golebiewska, U.5    McLaughlin, S.6
  • 71
    • 0023870115 scopus 로고
    • Protein phosphorylation in nerve terminals: comparison of calcium/calmodulin-dependent and calcium/diacylglycerol-dependent systems
    • Wang J.K., Walaas S.I., Greengard P. Protein phosphorylation in nerve terminals: comparison of calcium/calmodulin-dependent and calcium/diacylglycerol-dependent systems. J. Neurosci. 1988, 8(1):281-288.
    • (1988) J. Neurosci. , vol.8 , Issue.1 , pp. 281-288
    • Wang, J.K.1    Walaas, S.I.2    Greengard, P.3
  • 72
    • 0030036555 scopus 로고    scopus 로고
    • Chronic lithium-induced down-regulation of MARCKS in immortalized hippocampal cells: potentiation by muscarinic receptor activation
    • Watson D.G., Lenox R.H. Chronic lithium-induced down-regulation of MARCKS in immortalized hippocampal cells: potentiation by muscarinic receptor activation. J. Neurochem. 1996, 67(2):767-777.
    • (1996) J. Neurochem. , vol.67 , Issue.2 , pp. 767-777
    • Watson, D.G.1    Lenox, R.H.2
  • 73
    • 0036181154 scopus 로고    scopus 로고
    • Obligatory role of protein kinase Cbeta and MARCKS in vesicular trafficking in living neurons
    • Yang H., Wang X., Sumners C., Raizada M.K. Obligatory role of protein kinase Cbeta and MARCKS in vesicular trafficking in living neurons. Hypertension 2002, 39(2 Pt 2):567-572.
    • (2002) Hypertension , vol.39 , Issue.2 PART 2 , pp. 567-572
    • Yang, H.1    Wang, X.2    Sumners, C.3    Raizada, M.K.4


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