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Volumn 8, Issue 3, 2013, Pages

Regulation of Presynaptic Anchoring of the Scaffold Protein Bassoon by Phosphorylation-Dependent Interaction with 14-3-3 Adaptor Proteins

Author keywords

[No Author keywords available]

Indexed keywords

BASSOON PROTEIN; PROTEIN 14 3 3; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG;

EID: 84875031997     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0058814     Document Type: Article
Times cited : (18)

References (65)
  • 1
    • 84863471483 scopus 로고    scopus 로고
    • Molecular organization and plasticity of the cytomatrix at the active zone
    • Gundelfinger ED, Fejtova A, (2012) Molecular organization and plasticity of the cytomatrix at the active zone. Curr Opin Neurobiol 22: 423-430.
    • (2012) Curr Opin Neurobiol , vol.22 , pp. 423-430
    • Gundelfinger, E.D.1    Fejtova, A.2
  • 2
    • 33749033079 scopus 로고    scopus 로고
    • Molecular organization and assembly of the presynaptic active zone of neurotransmitter release
    • Fejtova A, Gundelfinger ED, (2006) Molecular organization and assembly of the presynaptic active zone of neurotransmitter release. Results Probl Cell Differ 43: 49-68.
    • (2006) Results Probl Cell Differ , vol.43 , pp. 49-68
    • Fejtova, A.1    Gundelfinger, E.D.2
  • 3
    • 78449280421 scopus 로고    scopus 로고
    • Bassoon and the synaptic ribbon organize ca(2+) channels and vesicles to add release sites and promote refilling
    • Frank T, Rutherford MA, Strenzke N, Neef A, Pangrsic T, et al. (2010) Bassoon and the synaptic ribbon organize ca(2+) channels and vesicles to add release sites and promote refilling. Neuron 68: 724-738.
    • (2010) Neuron , vol.68 , pp. 724-738
    • Frank, T.1    Rutherford, M.A.2    Strenzke, N.3    Neef, A.4    Pangrsic, T.5
  • 4
    • 0037421990 scopus 로고    scopus 로고
    • Functional inactivation of a fraction of excitatory synapses in mice deficient for the active zone protein bassoon
    • Altrock WD, tom Dieck S, Sokolov M, Meyer AC, Sigler A, et al. (2003) Functional inactivation of a fraction of excitatory synapses in mice deficient for the active zone protein bassoon. Neuron 37: 787-800.
    • (2003) Neuron , vol.37 , pp. 787-800
    • Altrock, W.D.1    tom Dieck, S.2    Sokolov, M.3    Meyer, A.C.4    Sigler, A.5
  • 6
    • 76849114494 scopus 로고    scopus 로고
    • Hippocampal Synaptic Plasticity, Memory, and Epilepsy: Effects of Long-Term Valproic Acid Treatment
    • Sgobio C, Ghiglieri V, Costa C, Bagetta V, Siliquini S, et al. (2010) Hippocampal Synaptic Plasticity, Memory, and Epilepsy: Effects of Long-Term Valproic Acid Treatment. Biol Psychiatry 67: 567-574.
    • (2010) Biol Psychiatry , vol.67 , pp. 567-574
    • Sgobio, C.1    Ghiglieri, V.2    Costa, C.3    Bagetta, V.4    Siliquini, S.5
  • 7
    • 14044254894 scopus 로고    scopus 로고
    • Proteomic analysis of in vivo phosphorylated synaptic proteins
    • Collins MO, Yu L, Coba MP, Husi H, Campuzano I, et al. (2005) Proteomic analysis of in vivo phosphorylated synaptic proteins. J Biol Chem 280: 5972-5982.
    • (2005) J Biol Chem , vol.280 , pp. 5972-5982
    • Collins, M.O.1    Yu, L.2    Coba, M.P.3    Husi, H.4    Campuzano, I.5
  • 8
    • 33847661220 scopus 로고    scopus 로고
    • Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations
    • Munton RP, Tweedie-Cullen R, Livingstone-Zatchej M, Weinandy F, Waidelich M, et al. (2007) Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations. Mol Cell Proteomics 6: 283-293.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 283-293
    • Munton, R.P.1    Tweedie-Cullen, R.2    Livingstone-Zatchej, M.3    Weinandy, F.4    Waidelich, M.5
  • 10
    • 0027402975 scopus 로고
    • Synaptic vesicle phosphoproteins and regulation of synaptic function
    • Greengard P, Valtorta F, Czernik AJ, Benfenati F, (1993) Synaptic vesicle phosphoproteins and regulation of synaptic function. Science 259: 780-785.
    • (1993) Science , vol.259 , pp. 780-785
    • Greengard, P.1    Valtorta, F.2    Czernik, A.J.3    Benfenati, F.4
  • 11
    • 0024592727 scopus 로고
    • Persistent and transcriptionally-dependent increase in protein phosphorylation in long-term facilitation of Aplysia sensory neurons
    • Sweatt JD, Kandel ER, (1989) Persistent and transcriptionally-dependent increase in protein phosphorylation in long-term facilitation of Aplysia sensory neurons. Nature 339: 51-54.
    • (1989) Nature , vol.339 , pp. 51-54
    • Sweatt, J.D.1    Kandel, E.R.2
  • 12
    • 3242788127 scopus 로고    scopus 로고
    • Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes
    • Mackintosh C, (2004) Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes. Biochem J 381: 329-342.
    • (2004) Biochem J , vol.381 , pp. 329-342
    • Mackintosh, C.1
  • 13
    • 70349876488 scopus 로고    scopus 로고
    • A protein interaction node at the neurotransmitter release site: domains of Aczonin/Piccolo, Bassoon, CAST, and rim converge on the N-terminal domain of Munc13-1
    • Wang X, Hu B, Zieba A, Neumann NG, Kasper-Sonnenberg M, et al. (2009) A protein interaction node at the neurotransmitter release site: domains of Aczonin/Piccolo, Bassoon, CAST, and rim converge on the N-terminal domain of Munc13-1. J Neurosci 29: 12584-12596.
    • (2009) J Neurosci , vol.29 , pp. 12584-12596
    • Wang, X.1    Hu, B.2    Zieba, A.3    Neumann, N.G.4    Kasper-Sonnenberg, M.5
  • 14
    • 58849123660 scopus 로고    scopus 로고
    • Exchange and redistribution dynamics of the cytoskeleton of the active zone molecule bassoon
    • Tsuriel S, Fisher A, Wittenmayer N, Dresbach T, Garner CC, et al. (2009) Exchange and redistribution dynamics of the cytoskeleton of the active zone molecule bassoon. J Neurosci 29: 351-358.
    • (2009) J Neurosci , vol.29 , pp. 351-358
    • Tsuriel, S.1    Fisher, A.2    Wittenmayer, N.3    Dresbach, T.4    Garner, C.C.5
  • 15
    • 33845669155 scopus 로고    scopus 로고
    • Molecular dynamics of a presynaptic active zone protein studied in Munc13-1-enhanced yellow fluorescent protein knock-in mutant mice
    • Kalla S, Stern M, Basu J, Varoqueaux F, Reim K, et al. (2006) Molecular dynamics of a presynaptic active zone protein studied in Munc13-1-enhanced yellow fluorescent protein knock-in mutant mice. J Neurosci 26: 13054-13066.
    • (2006) J Neurosci , vol.26 , pp. 13054-13066
    • Kalla, S.1    Stern, M.2    Basu, J.3    Varoqueaux, F.4    Reim, K.5
  • 16
    • 0345701204 scopus 로고    scopus 로고
    • Synaptic vesicle mobilization is regulated by distinct synapsin I phosphorylation pathways at different frequencies
    • Chi P, Greengard P, Ryan TA, (2003) Synaptic vesicle mobilization is regulated by distinct synapsin I phosphorylation pathways at different frequencies. Neuron 38: 69-78.
    • (2003) Neuron , vol.38 , pp. 69-78
    • Chi, P.1    Greengard, P.2    Ryan, T.A.3
  • 17
    • 33344462841 scopus 로고    scopus 로고
    • Constitutive sharing of recycling synaptic vesicles between presynaptic boutons
    • Darcy KJ, Staras K, Collinson LM, Goda Y, (2006) Constitutive sharing of recycling synaptic vesicles between presynaptic boutons. Nat Neurosci 9: 315-321.
    • (2006) Nat Neurosci , vol.9 , pp. 315-321
    • Darcy, K.J.1    Staras, K.2    Collinson, L.M.3    Goda, Y.4
  • 18
    • 33745901961 scopus 로고    scopus 로고
    • Synaptic vesicles interchange their membrane proteins with a large surface reservoir during recycling
    • Fernandez-Alfonso T, Kwan R, Ryan TA, (2006) Synaptic vesicles interchange their membrane proteins with a large surface reservoir during recycling. Neuron 51: 179-186.
    • (2006) Neuron , vol.51 , pp. 179-186
    • Fernandez-Alfonso, T.1    Kwan, R.2    Ryan, T.A.3
  • 19
    • 33748619210 scopus 로고    scopus 로고
    • Local sharing as a predominant determinant of synaptic matrix molecular dynamics
    • Tsuriel S, Geva R, Zamorano P, Dresbach T, Boeckers T, et al. (2006) Local sharing as a predominant determinant of synaptic matrix molecular dynamics. PLoS Biol 4: e271.
    • (2006) PLoS Biol , vol.4
    • Tsuriel, S.1    Geva, R.2    Zamorano, P.3    Dresbach, T.4    Boeckers, T.5
  • 20
  • 21
    • 79960383831 scopus 로고    scopus 로고
    • Extensive Remodeling of the Presynaptic Cytomatrix upon Homeostatic Adaptation to Network Activity Silencing
    • Lazarevic V, Schone C, Heine M, Gundelfinger ED, Fejtova A, (2011) Extensive Remodeling of the Presynaptic Cytomatrix upon Homeostatic Adaptation to Network Activity Silencing. J Neurosci 31: 10189-10200.
    • (2011) J Neurosci , vol.31 , pp. 10189-10200
    • Lazarevic, V.1    Schone, C.2    Heine, M.3    Gundelfinger, E.D.4    Fejtova, A.5
  • 22
    • 77952729399 scopus 로고    scopus 로고
    • Rapid structural alterations of the active zone lead to sustained changes in neurotransmitter release
    • Matz J, Gilyan A, Kolar A, McCarvill T, Krueger SR, (2010) Rapid structural alterations of the active zone lead to sustained changes in neurotransmitter release. Proc Natl Acad Sci U S A 107: 8836-8841.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 8836-8841
    • Matz, J.1    Gilyan, A.2    Kolar, A.3    McCarvill, T.4    Krueger, S.R.5
  • 23
    • 14444271321 scopus 로고    scopus 로고
    • Bassoon, a novel zinc-finger CAG/glutamine-repeat protein selectively localized at the active zone of presynaptic nerve terminals
    • tom Dieck S, Sanmarti-Vila L, Langnaese K, Richter K, Kindler S, et al. (1998) Bassoon, a novel zinc-finger CAG/glutamine-repeat protein selectively localized at the active zone of presynaptic nerve terminals. J Cell Biol 142: 499-509.
    • (1998) J Cell Biol , vol.142 , pp. 499-509
    • tom Dieck, S.1    Sanmarti-Vila, L.2    Langnaese, K.3    Richter, K.4    Kindler, S.5
  • 24
    • 0012345034 scopus 로고    scopus 로고
    • Functional regions of the presynaptic cytomatrix protein bassoon: significance for synaptic targeting and cytomatrix anchoring
    • Dresbach T, Hempelmann A, Spilker C, tom Dieck S, Altrock WD, et al. (2003) Functional regions of the presynaptic cytomatrix protein bassoon: significance for synaptic targeting and cytomatrix anchoring. Mol Cell Neurosci 23: 279-291.
    • (2003) Mol Cell Neurosci , vol.23 , pp. 279-291
    • Dresbach, T.1    Hempelmann, A.2    Spilker, C.3    tom Dieck, S.4    Altrock, W.D.5
  • 25
    • 65349109217 scopus 로고    scopus 로고
    • Dynein light chain regulates axonal trafficking and synaptic levels of Bassoon
    • Fejtova A, Davydova D, Bischof F, Lazarevic V, Altrock WD, et al. (2009) Dynein light chain regulates axonal trafficking and synaptic levels of Bassoon. J Cell Biol 185: 341-355.
    • (2009) J Cell Biol , vol.185 , pp. 341-355
    • Fejtova, A.1    Davydova, D.2    Bischof, F.3    Lazarevic, V.4    Altrock, W.D.5
  • 26
    • 39549119763 scopus 로고    scopus 로고
    • Activity-induced synaptic capture and exocytosis of the neuronal serine protease neurotrypsin
    • Frischknecht R, Fejtova A, Viesti M, Stephan A, Sonderegger P, (2008) Activity-induced synaptic capture and exocytosis of the neuronal serine protease neurotrypsin. J Neurosci 28: 1568-1579.
    • (2008) J Neurosci , vol.28 , pp. 1568-1579
    • Frischknecht, R.1    Fejtova, A.2    Viesti, M.3    Stephan, A.4    Sonderegger, P.5
  • 27
    • 2142765951 scopus 로고    scopus 로고
    • A syntaxin 1, Galpha(o), and N-type calcium channel complex at a presynaptic nerve terminal: analysis by quantitative immunocolocalization
    • Li Q, Lau A, Morris TJ, Guo L, Fordyce CB, et al. (2004) A syntaxin 1, Galpha(o), and N-type calcium channel complex at a presynaptic nerve terminal: analysis by quantitative immunocolocalization. J Neurosci 24: 4070-4081.
    • (2004) J Neurosci , vol.24 , pp. 4070-4081
    • Li, Q.1    Lau, A.2    Morris, T.J.3    Guo, L.4    Fordyce, C.B.5
  • 29
    • 0029871708 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine
    • Muslin AJ, Tanner JW, Allen PM, Shaw AS, (1996) Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell 84: 889-897.
    • (1996) Cell , vol.84 , pp. 889-897
    • Muslin, A.J.1    Tanner, J.W.2    Allen, P.M.3    Shaw, A.S.4
  • 30
    • 0031470652 scopus 로고    scopus 로고
    • The structural basis for 14-3-3:phosphopeptide binding specificity
    • Yaffe MB, Rittinger K, Volinia S, Caron PR, Aitken A, et al. (1997) The structural basis for 14-3-3:phosphopeptide binding specificity. Cell 91: 961-971.
    • (1997) Cell , vol.91 , pp. 961-971
    • Yaffe, M.B.1    Rittinger, K.2    Volinia, S.3    Caron, P.R.4    Aitken, A.5
  • 31
    • 31944444822 scopus 로고    scopus 로고
    • SWTY--a general peptide probe for homogeneous solution binding assay of 14-3-3 proteins
    • Wu M, Coblitz B, Shikano S, Long S, Cockrell LM, et al. (2006) SWTY--a general peptide probe for homogeneous solution binding assay of 14-3-3 proteins. Anal Biochem 349: 186-196.
    • (2006) Anal Biochem , vol.349 , pp. 186-196
    • Wu, M.1    Coblitz, B.2    Shikano, S.3    Long, S.4    Cockrell, L.M.5
  • 32
    • 0042622252 scopus 로고    scopus 로고
    • ELM server: A new resource for investigating short functional sites in modular eukaryotic proteins
    • Puntervoll P, Linding R, Gemund C, Chabanis-Davidson S, Mattingsdal M, et al. (2003) ELM server: A new resource for investigating short functional sites in modular eukaryotic proteins. Nucleic Acids Res 31: 3625-3630.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3625-3630
    • Puntervoll, P.1    Linding, R.2    Gemund, C.3    Chabanis-Davidson, S.4    Mattingsdal, M.5
  • 33
    • 2942552470 scopus 로고    scopus 로고
    • Unlocking the code of 14-3-3
    • Dougherty MK, Morrison DK, (2004) Unlocking the code of 14-3-3. J Cell Sci 117: 1875-1884.
    • (2004) J Cell Sci , vol.117 , pp. 1875-1884
    • Dougherty, M.K.1    Morrison, D.K.2
  • 35
    • 0025966605 scopus 로고
    • Distinct forms of the protein kinase-dependent activator of tyrosine and tryptophan hydroxylases
    • Isobe T, Ichimura T, Sunaya T, Okuyama T, Takahashi N, et al. (1991) Distinct forms of the protein kinase-dependent activator of tyrosine and tryptophan hydroxylases. J Mol Biol 217: 125-132.
    • (1991) J Mol Biol , vol.217 , pp. 125-132
    • Isobe, T.1    Ichimura, T.2    Sunaya, T.3    Okuyama, T.4    Takahashi, N.5
  • 36
    • 33646843974 scopus 로고    scopus 로고
    • Assembly of active zone precursor vesicles: obligatory trafficking of presynaptic cytomatrix proteins Bassoon and Piccolo via a trans-Golgi compartment
    • Dresbach T, Torres V, Wittenmayer N, Altrock WD, Zamorano P, et al. (2006) Assembly of active zone precursor vesicles: obligatory trafficking of presynaptic cytomatrix proteins Bassoon and Piccolo via a trans-Golgi compartment. J Biol Chem 281: 6038-6047.
    • (2006) J Biol Chem , vol.281 , pp. 6038-6047
    • Dresbach, T.1    Torres, V.2    Wittenmayer, N.3    Altrock, W.D.4    Zamorano, P.5
  • 37
    • 1242314196 scopus 로고    scopus 로고
    • Postsynaptic density assembly is fundamentally different from presynaptic active zone assembly
    • Bresler T, Shapira M, Boeckers T, Dresbach T, Futter M, et al. (2004) Postsynaptic density assembly is fundamentally different from presynaptic active zone assembly. J Neurosci 24: 1507-1520.
    • (2004) J Neurosci , vol.24 , pp. 1507-1520
    • Bresler, T.1    Shapira, M.2    Boeckers, T.3    Dresbach, T.4    Futter, M.5
  • 38
    • 2942564430 scopus 로고    scopus 로고
    • Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence
    • Blom N, Sicheritz-Ponten T, Gupta R, Gammeltoft S, Brunak S, (2004) Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence. Proteomics 4: 1633-1649.
    • (2004) Proteomics , vol.4 , pp. 1633-1649
    • Blom, N.1    Sicheritz-Ponten, T.2    Gupta, R.3    Gammeltoft, S.4    Brunak, S.5
  • 39
    • 33646358251 scopus 로고    scopus 로고
    • Minimotif Miner: a tool for investigating protein function
    • Balla S, Thapar V, Verma S, Luong T, Faghri T, et al. (2006) Minimotif Miner: a tool for investigating protein function. Nat Methods 3: 175-177.
    • (2006) Nat Methods , vol.3 , pp. 175-177
    • Balla, S.1    Thapar, V.2    Verma, S.3    Luong, T.4    Faghri, T.5
  • 40
    • 0035137129 scopus 로고    scopus 로고
    • Assembling the presynaptic active zone: a characterization of an active one precursor vesicle
    • Zhai RG, Vardinon-Friedman H, Cases-Langhoff C, Becker B, Gundelfinger ED, et al. (2001) Assembling the presynaptic active zone: a characterization of an active one precursor vesicle. Neuron 29: 131-143.
    • (2001) Neuron , vol.29 , pp. 131-143
    • Zhai, R.G.1    Vardinon-Friedman, H.2    Cases-Langhoff, C.3    Becker, B.4    Gundelfinger, E.D.5
  • 41
    • 0038702377 scopus 로고    scopus 로고
    • Unitary assembly of presynaptic active zones from Piccolo-Bassoon transport vesicles
    • Shapira M, Zhai RG, Dresbach T, Bresler T, Torres VI, et al. (2003) Unitary assembly of presynaptic active zones from Piccolo-Bassoon transport vesicles. Neuron 38: 237-252.
    • (2003) Neuron , vol.38 , pp. 237-252
    • Shapira, M.1    Zhai, R.G.2    Dresbach, T.3    Bresler, T.4    Torres, V.I.5
  • 42
    • 84864843505 scopus 로고    scopus 로고
    • Formation of Golgi-derived active zone precursor vesicles
    • Maas C, Torres VI, Altrock WD, Leal-Ortiz S, Wagh D, et al. (2012) Formation of Golgi-derived active zone precursor vesicles. J Neurosci 32: 11095-11108.
    • (2012) J Neurosci , vol.32 , pp. 11095-11108
    • Maas, C.1    Torres, V.I.2    Altrock, W.D.3    Leal-Ortiz, S.4    Wagh, D.5
  • 43
    • 0037421994 scopus 로고    scopus 로고
    • The presynaptic active zone protein bassoon is essential for photoreceptor ribbon synapse formation in the retina
    • Dick O, tom Dieck S, Altrock WD, Ammermuller J, Weiler R, et al. (2003) The presynaptic active zone protein bassoon is essential for photoreceptor ribbon synapse formation in the retina. Neuron 37: 775-786.
    • (2003) Neuron , vol.37 , pp. 775-786
    • Dick, O.1    tom Dieck, S.2    Altrock, W.D.3    Ammermuller, J.4    Weiler, R.5
  • 44
    • 70350187100 scopus 로고    scopus 로고
    • ELKS2alpha/CAST deletion selectively increases neurotransmitter release at inhibitory synapses
    • Kaeser PS, Deng L, Chavez AE, Liu X, Castillo PE, et al. (2009) ELKS2alpha/CAST deletion selectively increases neurotransmitter release at inhibitory synapses. Neuron 64: 227-239.
    • (2009) Neuron , vol.64 , pp. 227-239
    • Kaeser, P.S.1    Deng, L.2    Chavez, A.E.3    Liu, X.4    Castillo, P.E.5
  • 45
    • 0037122458 scopus 로고    scopus 로고
    • RIM1alpha forms a protein scaffold for regulating neurotransmitter release at the active zone
    • Schoch S, Castillo PE, Jo T, Mukherjee K, Geppert M, et al. (2002) RIM1alpha forms a protein scaffold for regulating neurotransmitter release at the active zone. Nature 415: 321-326.
    • (2002) Nature , vol.415 , pp. 321-326
    • Schoch, S.1    Castillo, P.E.2    Jo, T.3    Mukherjee, K.4    Geppert, M.5
  • 46
    • 0033598333 scopus 로고    scopus 로고
    • The liprin protein SYD-2 regulates the differentiation of presynaptic termini in C. elegans
    • Zhen M, Jin Y, (1999) The liprin protein SYD-2 regulates the differentiation of presynaptic termini in C. elegans. Nature 401: 371-375.
    • (1999) Nature , vol.401 , pp. 371-375
    • Zhen, M.1    Jin, Y.2
  • 47
    • 75749114797 scopus 로고    scopus 로고
    • mTOR signaling: at the crossroads of plasticity, memory and disease
    • Hoeffer CA, Klann E, (2010) mTOR signaling: at the crossroads of plasticity, memory and disease. Trends Neurosci 33: 67-75.
    • (2010) Trends Neurosci , vol.33 , pp. 67-75
    • Hoeffer, C.A.1    Klann, E.2
  • 48
    • 52049121528 scopus 로고    scopus 로고
    • Calmodulin-kinases: modulators of neuronal development and plasticity
    • Wayman GA, Lee YS, Tokumitsu H, Silva AJ, Soderling TR, (2008) Calmodulin-kinases: modulators of neuronal development and plasticity. Neuron 59: 914-931.
    • (2008) Neuron , vol.59 , pp. 914-931
    • Wayman, G.A.1    Lee, Y.S.2    Tokumitsu, H.3    Silva, A.J.4    Soderling, T.R.5
  • 49
    • 2942550646 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases in synaptic plasticity and memory
    • Sweatt JD, (2004) Mitogen-activated protein kinases in synaptic plasticity and memory. Curr Opin Neurobiol 14: 311-317.
    • (2004) Curr Opin Neurobiol , vol.14 , pp. 311-317
    • Sweatt, J.D.1
  • 50
    • 0033567121 scopus 로고    scopus 로고
    • Phosphorylation-dependent association of the Ras-related GTP-binding protein Rem with 14-3-3 proteins
    • Finlin BS, Andres DA, (1999) Phosphorylation-dependent association of the Ras-related GTP-binding protein Rem with 14-3-3 proteins. Arch Biochem Biophys 368: 401-412.
    • (1999) Arch Biochem Biophys , vol.368 , pp. 401-412
    • Finlin, B.S.1    Andres, D.A.2
  • 51
    • 59149095847 scopus 로고    scopus 로고
    • Regulation of RAF activity by 14-3-3 proteins: RAF kinases associate functionally with both homo- and heterodimeric forms of 14-3-3 proteins
    • Fischer A, Baljuls A, Reinders J, Nekhoroshkova E, Sibilski C, et al. (2009) Regulation of RAF activity by 14-3-3 proteins: RAF kinases associate functionally with both homo- and heterodimeric forms of 14-3-3 proteins. J Biol Chem 284: 3183-3194.
    • (2009) J Biol Chem , vol.284 , pp. 3183-3194
    • Fischer, A.1    Baljuls, A.2    Reinders, J.3    Nekhoroshkova, E.4    Sibilski, C.5
  • 52
    • 33749403134 scopus 로고    scopus 로고
    • Phospho-specific binding of 14-3-3 proteins to phosphatidylinositol 4-kinase III beta protects from dephosphorylation and stabilizes lipid kinase activity
    • Hausser A, Link G, Hoene M, Russo C, Selchow O, et al. (2006) Phospho-specific binding of 14-3-3 proteins to phosphatidylinositol 4-kinase III beta protects from dephosphorylation and stabilizes lipid kinase activity. J Cell Sci 119: 3613-3621.
    • (2006) J Cell Sci , vol.119 , pp. 3613-3621
    • Hausser, A.1    Link, G.2    Hoene, M.3    Russo, C.4    Selchow, O.5
  • 53
    • 84555189440 scopus 로고    scopus 로고
    • Regulation and function of the RSK family of protein kinases
    • Romeo Y, Zhang X, Roux PP, (2012) Regulation and function of the RSK family of protein kinases. Biochem J 441: 553-569.
    • (2012) Biochem J , vol.441 , pp. 553-569
    • Romeo, Y.1    Zhang, X.2    Roux, P.P.3
  • 54
    • 0036848266 scopus 로고    scopus 로고
    • Expression analysis of RSK gene family members: the RSK2 gene, mutated in Coffin-Lowry syndrome, is prominently expressed in brain structures essential for cognitive function and learning
    • Zeniou M, Ding T, Trivier E, Hanauer A, (2002) Expression analysis of RSK gene family members: the RSK2 gene, mutated in Coffin-Lowry syndrome, is prominently expressed in brain structures essential for cognitive function and learning. Hum Mol Genet 11: 2929-2940.
    • (2002) Hum Mol Genet , vol.11 , pp. 2929-2940
    • Zeniou, M.1    Ding, T.2    Trivier, E.3    Hanauer, A.4
  • 55
    • 0029832136 scopus 로고    scopus 로고
    • Mutations in the kinase Rsk-2 associated with Coffin-Lowry syndrome
    • Trivier E, De Cesare D, Jacquot S, Pannetier S, Zackai E, et al. (1996) Mutations in the kinase Rsk-2 associated with Coffin-Lowry syndrome. Nature 384: 567-570.
    • (1996) Nature , vol.384 , pp. 567-570
    • Trivier, E.1    De Cesare, D.2    Jacquot, S.3    Pannetier, S.4    Zackai, E.5
  • 56
    • 77954626422 scopus 로고    scopus 로고
    • Impaired development of hippocampal mossy fibre synapses in mouse mutants for the presynaptic scaffold protein Bassoon
    • Lanore F, Blanchet C, Fejtova A, Pinheiro P, Richter K, et al. (2010) Impaired development of hippocampal mossy fibre synapses in mouse mutants for the presynaptic scaffold protein Bassoon. J Physiol 588: 2133-2145.
    • (2010) J Physiol , vol.588 , pp. 2133-2145
    • Lanore, F.1    Blanchet, C.2    Fejtova, A.3    Pinheiro, P.4    Richter, K.5
  • 57
    • 1642499114 scopus 로고    scopus 로고
    • Physical and functional interaction of the active zone proteins, CAST, RIM1, and Bassoon, in neurotransmitter release
    • Takao-Rikitsu E, Mochida S, Inoue E, Deguchi-Tawarada M, Inoue M, et al. (2004) Physical and functional interaction of the active zone proteins, CAST, RIM1, and Bassoon, in neurotransmitter release. J Cell Biol 164: 301-311.
    • (2004) J Cell Biol , vol.164 , pp. 301-311
    • Takao-Rikitsu, E.1    Mochida, S.2    Inoue, E.3    Deguchi-Tawarada, M.4    Inoue, M.5
  • 58
    • 0037195108 scopus 로고    scopus 로고
    • A family of RIM-binding proteins regulated by alternative splicing: Implications for the genesis of synaptic active zones
    • Wang Y, Liu X, Biederer T, Sudhof TC, (2002) A family of RIM-binding proteins regulated by alternative splicing: Implications for the genesis of synaptic active zones. Proc Natl Acad Sci U S A 99: 14464-14469.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 14464-14469
    • Wang, Y.1    Liu, X.2    Biederer, T.3    Sudhof, T.C.4
  • 59
    • 0142242179 scopus 로고    scopus 로고
    • Interaction of the ERC family of RIM-binding proteins with the liprin-alpha family of multidomain proteins
    • Ko J, Na M, Kim S, Lee JR, Kim E, (2003) Interaction of the ERC family of RIM-binding proteins with the liprin-alpha family of multidomain proteins. J Biol Chem 278: 42377-42385.
    • (2003) J Biol Chem , vol.278 , pp. 42377-42385
    • Ko, J.1    Na, M.2    Kim, S.3    Lee, J.R.4    Kim, E.5
  • 60
    • 0141987893 scopus 로고    scopus 로고
    • Phosphorylation of RIM1alpha by PKA triggers presynaptic long-term potentiation at cerebellar parallel fiber synapses
    • Lonart G, Schoch S, Kaeser PS, Larkin CJ, Sudhof TC, et al. (2003) Phosphorylation of RIM1alpha by PKA triggers presynaptic long-term potentiation at cerebellar parallel fiber synapses. Cell 115: 49-60.
    • (2003) Cell , vol.115 , pp. 49-60
    • Lonart, G.1    Schoch, S.2    Kaeser, P.S.3    Larkin, C.J.4    Sudhof, T.C.5
  • 61
    • 55749107651 scopus 로고    scopus 로고
    • RIM1alpha phosphorylation at serine-413 by protein kinase A is not required for presynaptic long-term plasticity or learning
    • Kaeser PS, Kwon HB, Blundell J, Chevaleyre V, Morishita W, et al. (2008) RIM1alpha phosphorylation at serine-413 by protein kinase A is not required for presynaptic long-term plasticity or learning. Proc Natl Acad Sci U S A 105: 14680-14685.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 14680-14685
    • Kaeser, P.S.1    Kwon, H.B.2    Blundell, J.3    Chevaleyre, V.4    Morishita, W.5
  • 62
    • 77249154046 scopus 로고    scopus 로고
    • Acute in vivo genetic rescue demonstrates that phosphorylation of RIM1alpha serine 413 is not required for mossy fiber long-term potentiation
    • Yang Y, Calakos N, (2010) Acute in vivo genetic rescue demonstrates that phosphorylation of RIM1alpha serine 413 is not required for mossy fiber long-term potentiation. J Neurosci 30: 2542-2546.
    • (2010) J Neurosci , vol.30 , pp. 2542-2546
    • Yang, Y.1    Calakos, N.2
  • 63
    • 4344598183 scopus 로고    scopus 로고
    • Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization
    • Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, et al. (2004) Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization. Curr Biol 14: 1436-1450.
    • (2004) Curr Biol , vol.14 , pp. 1436-1450
    • Jin, J.1    Smith, F.D.2    Stark, C.3    Wells, C.D.4    Fawcett, J.P.5
  • 64
    • 33845989449 scopus 로고    scopus 로고
    • Transgenic mouse proteomics identifies new 14-3-3-associated proteins involved in cytoskeletal rearrangements and cell signaling
    • Angrand PO, Segura I, Volkel P, Ghidelli S, Terry R, et al. (2006) Transgenic mouse proteomics identifies new 14-3-3-associated proteins involved in cytoskeletal rearrangements and cell signaling. Mol Cell Proteomics 5: 2211-2227.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 2211-2227
    • Angrand, P.O.1    Segura, I.2    Volkel, P.3    Ghidelli, S.4    Terry, R.5
  • 65
    • 13744255989 scopus 로고    scopus 로고
    • Adapter protein 14-3-3 is required for a presynaptic form of LTP in the cerebellum
    • Simsek-Duran F, Linden DJ, Lonart G, (2004) Adapter protein 14-3-3 is required for a presynaptic form of LTP in the cerebellum. Nat Neurosci 7: 1296-1298.
    • (2004) Nat Neurosci , vol.7 , pp. 1296-1298
    • Simsek-Duran, F.1    Linden, D.J.2    Lonart, G.3


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