메뉴 건너뛰기




Volumn 62, Issue , 2014, Pages 42-50

N-myristoylation regulates the axonal distribution of the Fragile X-related protein FXR2P

Author keywords

Fragile X syndrome; FXR2P; Myristoylation; RNA binding proteins

Indexed keywords

FRAGILE X MENTAL RETARDATION PROTEIN; FXR2P PROTEIN; GLYCINE; GLYCINE 2; LIPID; MUTANT PROTEIN; RNA BINDING PROTEIN; UNCLASSIFIED DRUG; MICROTUBULE ASSOCIATED PROTEIN; MYRISTIC ACID DERIVATIVE; PROTEIN;

EID: 84906707915     PISSN: 10447431     EISSN: 10959327     Source Type: Journal    
DOI: 10.1016/j.mcn.2014.08.003     Document Type: Article
Times cited : (18)

References (54)
  • 1
    • 0023874519 scopus 로고
    • Stimulus-dependent myristoylation of a major substrate for protein kinase C
    • Aderem A.A., Albert K.A., Keum M.M., Wang J.K., Greengard P., Cohn Z.A. Stimulus-dependent myristoylation of a major substrate for protein kinase C. Nature 1988, 332:362-364.
    • (1988) Nature , vol.332 , pp. 362-364
    • Aderem, A.A.1    Albert, K.A.2    Keum, M.M.3    Wang, J.K.4    Greengard, P.5    Cohn, Z.A.6
  • 2
    • 79952441030 scopus 로고    scopus 로고
    • Presynaptic translation: stepping out of the postsynaptic structure
    • Akins M.R., Berk-Rauch H.E., Fallon J.R. Presynaptic translation: stepping out of the postsynaptic structure. Front. Neural Circ. 2009, 3:17.
    • (2009) Front. Neural Circ. , vol.3 , pp. 17
    • Akins, M.R.1    Berk-Rauch, H.E.2    Fallon, J.R.3
  • 3
    • 84865848777 scopus 로고    scopus 로고
    • Systematic mapping of fragile X granules in the mouse brain reveals a potential role for presynaptic FMRP in sensorimotor functions
    • Akins M.R., Leblanc H.F., Stackpole E.E., Chyung E., Fallon J.R. Systematic mapping of fragile X granules in the mouse brain reveals a potential role for presynaptic FMRP in sensorimotor functions. J. Comp. Neurol. 2012, 520:3687-3706.
    • (2012) J. Comp. Neurol. , vol.520 , pp. 3687-3706
    • Akins, M.R.1    Leblanc, H.F.2    Stackpole, E.E.3    Chyung, E.4    Fallon, J.R.5
  • 4
    • 33744966575 scopus 로고    scopus 로고
    • Local functions for FMRP in axon growth cone motility and activity-dependent regulation of filopodia and spine synapses
    • Antar L.N., Li C., Zhang H., Carroll R.C., Bassell G.J. Local functions for FMRP in axon growth cone motility and activity-dependent regulation of filopodia and spine synapses. Mol. Cell. Neurosci. 2006, 32:37-48.
    • (2006) Mol. Cell. Neurosci. , vol.32 , pp. 37-48
    • Antar, L.N.1    Li, C.2    Zhang, H.3    Carroll, R.C.4    Bassell, G.J.5
  • 5
    • 17844372504 scopus 로고    scopus 로고
    • From mRNP trafficking to spine dysmorphogenesis: the roots of fragile X syndrome
    • Bagni C., Greenough W.T. From mRNP trafficking to spine dysmorphogenesis: the roots of fragile X syndrome. Nat. Rev. Neurosci. 2005, 6:376-387.
    • (2005) Nat. Rev. Neurosci. , vol.6 , pp. 376-387
    • Bagni, C.1    Greenough, W.T.2
  • 6
    • 53849110899 scopus 로고    scopus 로고
    • Fragile X syndrome: loss of local mRNA regulation alters synaptic development and function
    • Bassell G.J., Warren S.T. Fragile X syndrome: loss of local mRNA regulation alters synaptic development and function. Neuron 2008, 60:201-214.
    • (2008) Neuron , vol.60 , pp. 201-214
    • Bassell, G.J.1    Warren, S.T.2
  • 7
    • 3042647610 scopus 로고    scopus 로고
    • The mGluR theory of fragile X mental retardation
    • Bear M.F., Huber K.M., Warren S.T. The mGluR theory of fragile X mental retardation. Trends Neurosci. 2004, 27:370-377.
    • (2004) Trends Neurosci. , vol.27 , pp. 370-377
    • Bear, M.F.1    Huber, K.M.2    Warren, S.T.3
  • 8
    • 0027392102 scopus 로고
    • The MARCKS family of cellular protein kinase C substrates
    • Blackshear P.J. The MARCKS family of cellular protein kinase C substrates. J. Biol. Chem. 1993, 268:1501-1504.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1501-1504
    • Blackshear, P.J.1
  • 9
    • 34648840173 scopus 로고    scopus 로고
    • Dendritic mRNA: transport, translation, and function
    • Bramham C.R., Wells D.G. Dendritic mRNA: transport, translation, and function. Nat. Rev. Neurosci. 2007, 8:776-789.
    • (2007) Nat. Rev. Neurosci. , vol.8 , pp. 776-789
    • Bramham, C.R.1    Wells, D.G.2
  • 11
    • 59649126241 scopus 로고    scopus 로고
    • The FXG: a presynaptic fragile X granule expressed in a subset of developing brain circuits
    • Christie S.B., Akins M.R., Schwob J.E., Fallon J.R. The FXG: a presynaptic fragile X granule expressed in a subset of developing brain circuits. J. Neurosci. 2009, 29:1512-1524.
    • (2009) J. Neurosci. , vol.29 , pp. 1512-1524
    • Christie, S.B.1    Akins, M.R.2    Schwob, J.E.3    Fallon, J.R.4
  • 13
    • 84878545717 scopus 로고    scopus 로고
    • Overexpression of Down syndrome cell adhesion molecula impairs precise synaptic targeting
    • Cvetkovska V., Hibbert A.D., Emran F., Chen B.E. Overexpression of Down syndrome cell adhesion molecula impairs precise synaptic targeting. Nat. Neurosci. 2013, 16:677-682.
    • (2013) Nat. Neurosci. , vol.16 , pp. 677-682
    • Cvetkovska, V.1    Hibbert, A.D.2    Emran, F.3    Chen, B.E.4
  • 14
    • 84880312659 scopus 로고    scopus 로고
    • RNA protein interaction in neurons
    • Darnell R.B. RNA protein interaction in neurons. Annu. Rev. Neurosci. 2013, 36:243-270.
    • (2013) Annu. Rev. Neurosci. , vol.36 , pp. 243-270
    • Darnell, R.B.1
  • 16
    • 36249016834 scopus 로고    scopus 로고
    • The fragile X mental retardation protein is a molecular adaptor between the neurospecific KIF3C kinesin and dendritic RNA granules
    • Davidovic L., Jaglin X.H., Lepagnoi-Bestel A.M., Tremblay S., Simonneau M., Bardoni B., Khandjian E.W. The fragile X mental retardation protein is a molecular adaptor between the neurospecific KIF3C kinesin and dendritic RNA granules. Hum. Mol. Genet. 2007, 16:3047-3058.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 3047-3058
    • Davidovic, L.1    Jaglin, X.H.2    Lepagnoi-Bestel, A.M.3    Tremblay, S.4    Simonneau, M.5    Bardoni, B.6    Khandjian, E.W.7
  • 17
    • 79960955668 scopus 로고    scopus 로고
    • Abnormal presynaptic short-term plasticity and information processing in a mouse model of fragile X syndrome
    • Deng P.Y., Sojka D., Klyachko V.A. Abnormal presynaptic short-term plasticity and information processing in a mouse model of fragile X syndrome. J. Neurosci. 2011, 31:10971-10982.
    • (2011) J. Neurosci. , vol.31 , pp. 10971-10982
    • Deng, P.Y.1    Sojka, D.2    Klyachko, V.A.3
  • 18
    • 84874256375 scopus 로고    scopus 로고
    • FMRP regulates neurotransmitter release and synaptic information transmission by modulating action potential duration via BK channels
    • Deng P.Y., Rotman Z., Blundon J.A., Cho Y., Cui J., Cavalli V., Zakharenko S.S., Klyachko V.A. FMRP regulates neurotransmitter release and synaptic information transmission by modulating action potential duration via BK channels. Neuron 2013, 77:696-711.
    • (2013) Neuron , vol.77 , pp. 696-711
    • Deng, P.Y.1    Rotman, Z.2    Blundon, J.A.3    Cho, Y.4    Cui, J.5    Cavalli, V.6    Zakharenko, S.S.7    Klyachko, V.A.8
  • 19
    • 0031046778 scopus 로고    scopus 로고
    • Fragile X mental retardation protein: nucleocytoplasmic shuttling and association with somatodendritic ribosomes
    • Feng Y., Gutekunst C.A., Eberhart D.E., Yi H., Warren S.T., Hersch S.M. Fragile X mental retardation protein: nucleocytoplasmic shuttling and association with somatodendritic ribosomes. J. Neurosci. 1997, 17:1539-1547.
    • (1997) J. Neurosci. , vol.17 , pp. 1539-1547
    • Feng, Y.1    Gutekunst, C.A.2    Eberhart, D.E.3    Yi, H.4    Warren, S.T.5    Hersch, S.M.6
  • 20
    • 84902601046 scopus 로고    scopus 로고
    • Fragile X mental retardation protein controls synaptic vesicle exocytosis by modulating N-type calcium channel density
    • Ferron L., Nieto R.M., Cassidy J.S., Dolphin A.C. Fragile X mental retardation protein controls synaptic vesicle exocytosis by modulating N-type calcium channel density. Nat. Commun. 2014, 5:3628.
    • (2014) Nat. Commun. , vol.5 , pp. 3628
    • Ferron, L.1    Nieto, R.M.2    Cassidy, J.S.3    Dolphin, A.C.4
  • 22
    • 9344246891 scopus 로고    scopus 로고
    • Visual experience regulates transient expression and dendritic localization of fragile X mental retardation protein
    • Gabel L.A., Won S., Kawai H., McKinney M., Tartakoff A.M., Fallon J.R. Visual experience regulates transient expression and dendritic localization of fragile X mental retardation protein. J. Neurosci. 2004, 24:10579-10583.
    • (2004) J. Neurosci. , vol.24 , pp. 10579-10583
    • Gabel, L.A.1    Won, S.2    Kawai, H.3    McKinney, M.4    Tartakoff, A.M.5    Fallon, J.R.6
  • 24
    • 34247116144 scopus 로고    scopus 로고
    • Presynaptic FMR1 genotype influences the degree of synaptic connectivity in a mosaic mouse model of fragile X syndrome
    • Hanson J.E., Madison D.V. Presynaptic FMR1 genotype influences the degree of synaptic connectivity in a mosaic mouse model of fragile X syndrome. J. Neurosci. 2007, 27:4014-4018.
    • (2007) J. Neurosci. , vol.27 , pp. 4014-4018
    • Hanson, J.E.1    Madison, D.V.2
  • 25
    • 84855880056 scopus 로고    scopus 로고
    • Multifunction protein labeling via enzymatic N-terminal tagging and elaboration by click chemistry
    • Heal W.P., Wright M.H., Thinon E., Tate E.W. Multifunction protein labeling via enzymatic N-terminal tagging and elaboration by click chemistry. Nat. Protoc. 2011, 7:105-117.
    • (2011) Nat. Protoc. , vol.7 , pp. 105-117
    • Heal, W.P.1    Wright, M.H.2    Thinon, E.3    Tate, E.W.4
  • 27
    • 0024819249 scopus 로고
    • Myristoylation, phosphorylation and subcellular distribution of the 80-kDa protein kinase C substrate in BC3H1 myocytes
    • James G., Olson E.N. Myristoylation, phosphorylation and subcellular distribution of the 80-kDa protein kinase C substrate in BC3H1 myocytes. J. Biol. Chem. 1989, 264:20928-20933.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20928-20933
    • James, G.1    Olson, E.N.2
  • 28
    • 84859954603 scopus 로고    scopus 로고
    • Axonal mRNA localization and protein synthesis in nervous system assembly, maintenance and repair
    • Jung H., Yoon B.C., Holt C.E. Axonal mRNA localization and protein synthesis in nervous system assembly, maintenance and repair. Nat. Rev. Neurosci. 2012, 13:308-324.
    • (2012) Nat. Rev. Neurosci. , vol.13 , pp. 308-324
    • Jung, H.1    Yoon, B.C.2    Holt, C.E.3
  • 29
    • 84870936058 scopus 로고    scopus 로고
    • Genome-wide approaches to dissect the roles of RNA binding proteins in translational control: implications for neurological diseases
    • Kapeli K., Yeo G.W. Genome-wide approaches to dissect the roles of RNA binding proteins in translational control: implications for neurological diseases. Front. Neurosci. 2012, 10.3389/fnins.2012.00144.
    • (2012) Front. Neurosci.
    • Kapeli, K.1    Yeo, G.W.2
  • 30
    • 33748526877 scopus 로고    scopus 로고
    • Neuronal RNA granules: movers and makers
    • Kiebler M.A., Bassell G.J. Neuronal RNA granules: movers and makers. Neuron 2006, 51:685-690.
    • (2006) Neuron , vol.51 , pp. 685-690
    • Kiebler, M.A.1    Bassell, G.J.2
  • 31
    • 84878835421 scopus 로고    scopus 로고
    • Dscam expression levels determine presynaptic arbor sizes in Drosophila sensory neurons
    • Kim J.H., Wang X., Coolon R., Ye B. Dscam expression levels determine presynaptic arbor sizes in Drosophila sensory neurons. Neuron 2013, 78:827-838.
    • (2013) Neuron , vol.78 , pp. 827-838
    • Kim, J.H.1    Wang, X.2    Coolon, R.3    Ye, B.4
  • 32
    • 0344466778 scopus 로고    scopus 로고
    • Microtubule-dependent recruitment of Staufen-green fluorescent protein into large RNA-containing granules and subsequent dendritic transport in living hippocampal neurons
    • Köhrmann M., Luo M., Kaether C., DesGroseillers L., Dotti C.G., Kiebler M.A. Microtubule-dependent recruitment of Staufen-green fluorescent protein into large RNA-containing granules and subsequent dendritic transport in living hippocampal neurons. Mol. Biol. Cell 1999, 10:2945-2953.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2945-2953
    • Köhrmann, M.1    Luo, M.2    Kaether, C.3    DesGroseillers, L.4    Dotti, C.G.5    Kiebler, M.A.6
  • 34
    • 0024078185 scopus 로고
    • Acetylcholine receptor-associated 43K protein contains covalently bound myristate
    • Musil L.S., Carr C., Cohen J.B., Merlie J.P. Acetylcholine receptor-associated 43K protein contains covalently bound myristate. J. Cell Biol. 1988, 107:1113-1121.
    • (1988) J. Cell Biol. , vol.107 , pp. 1113-1121
    • Musil, L.S.1    Carr, C.2    Cohen, J.B.3    Merlie, J.P.4
  • 35
    • 0345599029 scopus 로고    scopus 로고
    • Dynamics and calcium sensitivity of the Ca2+/myristoyl switch protein hippocalcin in living cells
    • O'Callaghan D.W., Tepikin A.V., Burgoyne R.D. Dynamics and calcium sensitivity of the Ca2+/myristoyl switch protein hippocalcin in living cells. J. Cell Biol. 2003, 163:715-721.
    • (2003) J. Cell Biol. , vol.163 , pp. 715-721
    • O'Callaghan, D.W.1    Tepikin, A.V.2    Burgoyne, R.D.3
  • 37
    • 0027432307 scopus 로고
    • Binding of acylated peptides and fatty acids to phospholipid vesicles: pertinence to myristoylated proteins
    • Peitzsch R.M., McLaughlin S. Binding of acylated peptides and fatty acids to phospholipid vesicles: pertinence to myristoylated proteins. Biochemistry 1993, 32:10436-10443.
    • (1993) Biochemistry , vol.32 , pp. 10436-10443
    • Peitzsch, R.M.1    McLaughlin, S.2
  • 39
    • 33747250338 scopus 로고    scopus 로고
    • The RNA binding and transport proteins staufen and fragile X mental retardation protein are expressed by rat primary afferent neurons and localize to peripheral and central axons
    • Price T.J., Flores C.M., Cervero F., Hargreaves K.M. The RNA binding and transport proteins staufen and fragile X mental retardation protein are expressed by rat primary afferent neurons and localize to peripheral and central axons. Neuroscience 2006, 141:2107-2116.
    • (2006) Neuroscience , vol.141 , pp. 2107-2116
    • Price, T.J.1    Flores, C.M.2    Cervero, F.3    Hargreaves, K.M.4
  • 40
    • 0028173679 scopus 로고
    • Myristylation and palmitylation of Src family members: the fats of the matter
    • Resh M.D. Myristylation and palmitylation of Src family members: the fats of the matter. Cell 1994, 76:411-413.
    • (1994) Cell , vol.76 , pp. 411-413
    • Resh, M.D.1
  • 41
    • 7444255626 scopus 로고    scopus 로고
    • Membrane targeting of lipid modified signal transduction proteins
    • Resh M.D. Membrane targeting of lipid modified signal transduction proteins. Subcell. Biochem. 2004, 37:217-232.
    • (2004) Subcell. Biochem. , vol.37 , pp. 217-232
    • Resh, M.D.1
  • 42
    • 0037134973 scopus 로고    scopus 로고
    • A new way to rapidly create function, fluorescent fusion proteins: random insertion of GFP with an in vitro transposition reaction
    • Sheridan D.L., Berlot C.H., Robert A., Inglis F.M., Jakobsdottir K.B., Howe J.R., Hughes T.E. A new way to rapidly create function, fluorescent fusion proteins: random insertion of GFP with an in vitro transposition reaction. BMC Neurosci 2002, 3.
    • (2002) BMC Neurosci , vol.3
    • Sheridan, D.L.1    Berlot, C.H.2    Robert, A.3    Inglis, F.M.4    Jakobsdottir, K.B.5    Howe, J.R.6    Hughes, T.E.7
  • 43
    • 0027327486 scopus 로고
    • The protein product of the fragile X gene, FMR1, has characteristics of an RNA-binding protein
    • Siomi H., Siomi M.C., Nussbaum R.L., Dreyfuss G. The protein product of the fragile X gene, FMR1, has characteristics of an RNA-binding protein. Cell 1993, 74:291-298.
    • (1993) Cell , vol.74 , pp. 291-298
    • Siomi, H.1    Siomi, M.C.2    Nussbaum, R.L.3    Dreyfuss, G.4
  • 44
    • 70450188170 scopus 로고    scopus 로고
    • Protein lipid modifications in signaling and subcellular targeting
    • Sorek N., Bloch D., Yalovsky S. Protein lipid modifications in signaling and subcellular targeting. Curr. Opin. Plant Biol. 2009, 12:714-720.
    • (2009) Curr. Opin. Plant Biol. , vol.12 , pp. 714-720
    • Sorek, N.1    Bloch, D.2    Yalovsky, S.3
  • 45
    • 0036758614 scopus 로고    scopus 로고
    • Reversible translocation and activity-dependent localization of the calcium-myristoyl switch protein VILIP-1 to different compartments in living hippocampal neurons
    • Spilker C., Dresbach T., Braunewell K.H. Reversible translocation and activity-dependent localization of the calcium-myristoyl switch protein VILIP-1 to different compartments in living hippocampal neurons. J. Neurosci. 2002, 22:7331-7339.
    • (2002) J. Neurosci. , vol.22 , pp. 7331-7339
    • Spilker, C.1    Dresbach, T.2    Braunewell, K.H.3
  • 46
    • 0033597319 scopus 로고    scopus 로고
    • Identification of the calmodulin-binding domain of neuron-specific protein kinase C substrate protein CAP-22/NAP-2. Direct involvement of protein myristoylation in calmodulin-target protein interaction
    • Takasaki A., Hayashi N., Matsubara M., Yamauchi E., Taniguchi H. Identification of the calmodulin-binding domain of neuron-specific protein kinase C substrate protein CAP-22/NAP-2. Direct involvement of protein myristoylation in calmodulin-target protein interaction. J. Biol. Chem. 1999, 274:11848-11853.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11848-11853
    • Takasaki, A.1    Hayashi, N.2    Matsubara, M.3    Yamauchi, E.4    Taniguchi, H.5
  • 47
    • 0033552652 scopus 로고    scopus 로고
    • Protein myristoylation in protein-lipid and protein-protein interactions
    • Tanaguchi H. Protein myristoylation in protein-lipid and protein-protein interactions. Biophys. Chem. 1999, 82:129-137.
    • (1999) Biophys. Chem. , vol.82 , pp. 129-137
    • Tanaguchi, H.1
  • 48
    • 44449130390 scopus 로고    scopus 로고
    • Drosophila fragile X mental retardation protein developmentally regulates activity-dependent axon pruning
    • Tessier C.R., Broadie K. Drosophila fragile X mental retardation protein developmentally regulates activity-dependent axon pruning. Development 2008, 135:1547-1557.
    • (2008) Development , vol.135 , pp. 1547-1557
    • Tessier, C.R.1    Broadie, K.2
  • 49
    • 78650987058 scopus 로고    scopus 로고
    • A presynaptic role for FMRP during protein synthesis-dependent long-term plasticity in Aplysia
    • Till S.M., Li H.L., Miniaci M.C., Kandel E.R., Choi Y.B. A presynaptic role for FMRP during protein synthesis-dependent long-term plasticity in Aplysia. Learn. Mem. 2010, 18:39-48.
    • (2010) Learn. Mem. , vol.18 , pp. 39-48
    • Till, S.M.1    Li, H.L.2    Miniaci, M.C.3    Kandel, E.R.4    Choi, Y.B.5
  • 50
    • 0023109534 scopus 로고
    • Amino-terminal processing of proteins by N-myristoylation. Substrate specificity of N-myristoyl transferase
    • Towler D.A., Eubanks S.R., Towery D.S., Adams S.P., Glaser L. Amino-terminal processing of proteins by N-myristoylation. Substrate specificity of N-myristoyl transferase. J. Biol. Chem. 1987, 262:1030-1036.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1030-1036
    • Towler, D.A.1    Eubanks, S.R.2    Towery, D.S.3    Adams, S.P.4    Glaser, L.5
  • 51
    • 0023931431 scopus 로고
    • Myristoyl CoA: protein N-myristoyltransferase activities from rat liver and yeast possess overlapping yet distinct peptide substrate specificities
    • Towler D.A., Adams S.P., Eubanks S.R., Towery D.S., Jackson-Machelski E., Glaser L., Gordon J.I. Myristoyl CoA: protein N-myristoyltransferase activities from rat liver and yeast possess overlapping yet distinct peptide substrate specificities. J. Biol. Chem. 1988, 263:1784-1790.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1784-1790
    • Towler, D.A.1    Adams, S.P.2    Eubanks, S.R.3    Towery, D.S.4    Jackson-Machelski, E.5    Glaser, L.6    Gordon, J.I.7
  • 52
    • 0023666521 scopus 로고
    • Acylation of proteins with myristic acid occurs cotranslationally
    • Wilcox C., Hu J.S., Olson E.N. Acylation of proteins with myristic acid occurs cotranslationally. Science 1987, 27:1275-1278.
    • (1987) Science , vol.27 , pp. 1275-1278
    • Wilcox, C.1    Hu, J.S.2    Olson, E.N.3
  • 53
    • 0035977134 scopus 로고    scopus 로고
    • Drosophila fragile X-related gene regulates the MAP1B homolog Futsch to control synaptic structure and function
    • Zhang Y.Q., Bailey A.M., Matthles H.J., Renden R.B., Smith M.A., Speese S.D., Rubin G.M., Broadie K. Drosophila fragile X-related gene regulates the MAP1B homolog Futsch to control synaptic structure and function. Cell 2001, 107:591-603.
    • (2001) Cell , vol.107 , pp. 591-603
    • Zhang, Y.Q.1    Bailey, A.M.2    Matthles, H.J.3    Renden, R.B.4    Smith, M.A.5    Speese, S.D.6    Rubin, G.M.7    Broadie, K.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.