메뉴 건너뛰기




Volumn 7, Issue 12, 2006, Pages 1581-1589

Intracellular trafficking of RNA in neurons

Author keywords

Micro RNAs; P bodies; RNA granule; Staufen; Stress granules; Translation; Transport particle

Indexed keywords

BETA ACTIN; DEAD BOX PROTEIN; FRAGILE X MENTAL RETARDATION PROTEIN; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN C; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN U; MESSENGER RNA; METABOTROPIC RECEPTOR; MICRORNA; MYELIN BASIC PROTEIN; RIBOSOME PROTEIN; RNA; RNA BINDING PROTEIN;

EID: 33750993210     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2006.00500.x     Document Type: Review
Times cited : (109)

References (83)
  • 1
    • 27144515901 scopus 로고    scopus 로고
    • Movement of eukaryotic mRNAs between polysomes and cytoplasmic processing bodies
    • Brengues M, Teixeira D, Parker R. Movement of eukaryotic mRNAs between polysomes and cytoplasmic processing bodies. Science 2005; 310: 486-489.
    • (2005) Science , vol.310 , pp. 486-489
    • Brengues, M.1    Teixeira, D.2    Parker, R.3
  • 2
    • 0035923735 scopus 로고    scopus 로고
    • Neuronal RNA granules: A link between RNA localization and stimulation-dependent translation
    • Krichevsky AM, Kosik KS. Neuronal RNA granules: A link between RNA localization and stimulation-dependent translation. Neuron 2001; 32: 683-696.
    • (2001) Neuron , vol.32 , pp. 683-696
    • Krichevsky, A.M.1    Kosik, K.S.2
  • 3
    • 18244395316 scopus 로고    scopus 로고
    • A novel RNA-binding protein in neuronal RNA granules: Regulatory machinery for local translation
    • Shiina N, Shinkura K, Tokunaga M. A novel RNA-binding protein in neuronal RNA granules: Regulatory machinery for local translation. J Neurosci 2005; 25: 4420-4434.
    • (2005) J Neurosci , vol.25 , pp. 4420-4434
    • Shiina, N.1    Shinkura, K.2    Tokunaga, M.3
  • 4
    • 0037968357 scopus 로고    scopus 로고
    • Decapping and decay of messenger RNA occur in cytoplasmic processing bodies
    • Sheth U, Parker R. Decapping and decay of messenger RNA occur in cytoplasmic processing bodies. Science 2003; 300: 805-808.
    • (2003) Science , vol.300 , pp. 805-808
    • Sheth, U.1    Parker, R.2
  • 5
    • 25144482816 scopus 로고    scopus 로고
    • General translational repression by activators of mRNA decapping
    • Coller J, Parker R. General translational repression by activators of mRNA decapping. Cell 2005; 122: 875-886.
    • (2005) Cell , vol.122 , pp. 875-886
    • Coller, J.1    Parker, R.2
  • 6
    • 0035674477 scopus 로고    scopus 로고
    • The DEAD box helicase, Dhh1p, functions in mRNA decapping and interacts with both the decapping and deadenylase complexes
    • Coller JM, Tucker M, Sheth U, Valencia-Sanchez MA, Parker R. The DEAD box helicase, Dhh1p, functions in mRNA decapping and interacts with both the decapping and deadenylase complexes. RNA 2001; 7: 1717-1727.
    • (2001) RNA , vol.7 , pp. 1717-1727
    • Coller, J.M.1    Tucker, M.2    Sheth, U.3    Valencia-Sanchez, M.A.4    Parker, R.5
  • 7
    • 15444379718 scopus 로고    scopus 로고
    • Processing bodies require RNA for assembly and contain nontranslating mRNAs
    • Teixeira D, Sheth U, Valencia-Sanchez MA, Brengues M, Parker R. Processing bodies require RNA for assembly and contain nontranslating mRNAs. RNA 2005; 11: 371-382.
    • (2005) RNA , vol.11 , pp. 371-382
    • Teixeira, D.1    Sheth, U.2    Valencia-Sanchez, M.A.3    Brengues, M.4    Parker, R.5
  • 8
    • 33745791191 scopus 로고    scopus 로고
    • Dendritic localization of the translational repressor Pumilio 2 and its contribution to dendritic stress granules
    • Vessey JP, Vaccani A, Xie Y, Dahm R, Karra D, Kiebler MA, Macchi P. Dendritic localization of the translational repressor Pumilio 2 and its contribution to dendritic stress granules. J Neurosci 2006; 26: 6496-6508.
    • (2006) J Neurosci , vol.26 , pp. 6496-6508
    • Vessey, J.P.1    Vaccani, A.2    Xie, Y.3    Dahm, R.4    Karra, D.5    Kiebler, M.A.6    Macchi, P.7
  • 9
    • 0036863320 scopus 로고    scopus 로고
    • Stress granules: Sites of mRNA triage that regulate mRNA stability and translatability
    • Kedersha N, Anderson P. Stress granules: Sites of mRNA triage that regulate mRNA stability and translatability. Biochem Soc Trans 2002; 30: 963-969.
    • (2002) Biochem Soc Trans , vol.30 , pp. 963-969
    • Kedersha, N.1    Anderson, P.2
  • 10
    • 0036154218 scopus 로고    scopus 로고
    • Evidence that ternary complex (eIF2-GTP-tRNA(i)(Met))-deficient preinitiation complexes are core constituents of mammalian stress granules
    • Kedersha N, Chen S, Gilks N, Li W, Miller IJ, Stahl J, Anderson P. Evidence that ternary complex (eIF2-GTP-tRNA(i)(Met))-deficient preinitiation complexes are core constituents of mammalian stress granules. Mol Biol Cell 2002; 13: 195-210.
    • (2002) Mol Biol Cell , vol.13 , pp. 195-210
    • Kedersha, N.1    Chen, S.2    Gilks, N.3    Li, W.4    Miller, I.J.5    Stahl, J.6    Anderson, P.7
  • 16
    • 22144489833 scopus 로고    scopus 로고
    • RNAi: The nuts and bolts of the RISC machine
    • Filipowicz W. RNAi: The nuts and bolts of the RISC machine. Cell 2005; 122: 17-20.
    • (2005) Cell , vol.122 , pp. 17-20
    • Filipowicz, W.1
  • 18
    • 33644768174 scopus 로고    scopus 로고
    • Control of translation and mRNA degradation by miRNAs and siRNAs
    • Valencia-Sanchez MA, Liu J, Hannon GJ, Parker R. Control of translation and mRNA degradation by miRNAs and siRNAs. Genes Dev 2006; 20: 515-524.
    • (2006) Genes Dev , vol.20 , pp. 515-524
    • Valencia-Sanchez, M.A.1    Liu, J.2    Hannon, G.J.3    Parker, R.4
  • 19
    • 28044457883 scopus 로고    scopus 로고
    • MicroRNAs control translation initiation by inhibiting eukaryotic initiation factor 4E/cap and poly(A) tail function
    • Humphreys DT, Westman BJ, Martin DI, Preiss T. MicroRNAs control translation initiation by inhibiting eukaryotic initiation factor 4E/cap and poly(A) tail function. Proc Natl Acad Sci U S A 2005; 102: 16961-16966.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 16961-16966
    • Humphreys, D.T.1    Westman, B.J.2    Martin, D.I.3    Preiss, T.4
  • 24
    • 13544261683 scopus 로고    scopus 로고
    • RNA localization in yeast: Moving towards a mechanism
    • Gonsalvez GB, Urbinati CR, Long RM. RNA localization in yeast: Moving towards a mechanism. Biol Cell 2005; 97: 75-86.
    • (2005) Biol Cell , vol.97 , pp. 75-86
    • Gonsalvez, G.B.1    Urbinati, C.R.2    Long, R.M.3
  • 25
    • 0033519623 scopus 로고    scopus 로고
    • Localization and anchoring of mRNA in budding yeast
    • Beach DL, Salmon ED, Bloom K. Localization and anchoring of mRNA in budding yeast. Curr Biol 1999; 9: 569-578.
    • (1999) Curr Biol , vol.9 , pp. 569-578
    • Beach, D.L.1    Salmon, E.D.2    Bloom, K.3
  • 28
    • 0037020098 scopus 로고    scopus 로고
    • Identification of mRNA/Protein (mRNP) complexes containing Puralpha, mStaufen, fragile X protein, and myosin Va and their association with rough endoplasmic reticulum equipped with a kinesin motor
    • Ohashi S, Koike K, Omori A, Ichinose S, Ohara S, Kobayashi S, Sato T-A, Anzai K. Identification of mRNA/Protein (mRNP) complexes containing Puralpha, mStaufen, fragile X protein, and myosin Va and their association with rough endoplasmic reticulum equipped with a kinesin motor. J Biol Chem 2002; 277: 37804-37810.
    • (2002) J Biol Chem , vol.277 , pp. 37804-37810
    • Ohashi, S.1    Koike, K.2    Omori, A.3    Ichinose, S.4    Ohara, S.5    Kobayashi, S.6    Sato, T.-A.7    Anzai, K.8
  • 31
    • 0027367040 scopus 로고
    • Transport and localization of exogenous myelin basic protein mRNA microinjected into oligodendrocytes
    • Ainger K, Avossa D, Morgan F, Hill SJ, Barry C, Barbarese E, Carson JH. Transport and localization of exogenous myelin basic protein mRNA microinjected into oligodendrocytes. J Cell Biol 1993; 123: 431-441.
    • (1993) J Cell Biol , vol.123 , pp. 431-441
    • Ainger, K.1    Avossa, D.2    Morgan, F.3    Hill, S.J.4    Barry, C.5    Barbarese, E.6    Carson, J.H.7
  • 34
    • 4143088149 scopus 로고    scopus 로고
    • Kinesin transports RNA: Isolation and characterization of an RNA-transporting granule
    • Kanai Y, Dohmae N, Hirokawa N. Kinesin transports RNA: Isolation and characterization of an RNA-transporting granule. Neuron 2004; 43: 513-525.
    • (2004) Neuron , vol.43 , pp. 513-525
    • Kanai, Y.1    Dohmae, N.2    Hirokawa, N.3
  • 36
    • 0141640944 scopus 로고    scopus 로고
    • A molecular mechanism for mRNA trafficking in neuronal dendrites
    • Shan J, Munro TP, Barbarese E, Carson JH, Smith R. A molecular mechanism for mRNA trafficking in neuronal dendrites. J Neurosci 2003; 23: 8859-8866.
    • (2003) J Neurosci , vol.23 , pp. 8859-8866
    • Shan, J.1    Munro, T.P.2    Barbarese, E.3    Carson, J.H.4    Smith, R.5
  • 38
    • 0036512117 scopus 로고    scopus 로고
    • Messenger-RNA-binding proteins and the messages they carry
    • Dreyfuss G, Kim VN, Kataoka N. Messenger-RNA-binding proteins and the messages they carry. Nat Rev Mol Cell Biol 2002; 3: 195-205.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 195-205
    • Dreyfuss, G.1    Kim, V.N.2    Kataoka, N.3
  • 39
    • 0023772979 scopus 로고
    • The product of the Drosophila gene vasa is very similar to eukaryotic initiation factor-4A
    • Lasko PF, Ashburner M. The product of the Drosophila gene vasa is very similar to eukaryotic initiation factor-4A. Nature 1988; 335: 611-617.
    • (1988) Nature , vol.335 , pp. 611-617
    • Lasko, P.F.1    Ashburner, M.2
  • 41
    • 0036809125 scopus 로고    scopus 로고
    • The nuclear connection in RNA transport and localization
    • Farina KL, Singer RH. The nuclear connection in RNA transport and localization. Trends Cell Biol 2002; 12: 466-472.
    • (2002) Trends Cell Biol , vol.12 , pp. 466-472
    • Farina, K.L.1    Singer, R.H.2
  • 42
    • 0037314639 scopus 로고    scopus 로고
    • Real-time visualization of ZBP1 association with beta-actin mRNA during transcription and localization
    • Oleynikov Y, Singer RH. Real-time visualization of ZBP1 association with beta-actin mRNA during transcription and localization. Curr Biol 2003; 13: 199-207.
    • (2003) Curr Biol , vol.13 , pp. 199-207
    • Oleynikov, Y.1    Singer, R.H.2
  • 43
    • 2142827074 scopus 로고    scopus 로고
    • Nuclear RNP complex assembly initiates cytoplasmic RNA localization
    • Kress TL, Yoon YJ, Mowry KL. Nuclear RNP complex assembly initiates cytoplasmic RNA localization. J Cell Biol 2004; 165: 203-211.
    • (2004) J Cell Biol , vol.165 , pp. 203-211
    • Kress, T.L.1    Yoon, Y.J.2    Mowry, K.L.3
  • 45
    • 19344374029 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay: Molecular insights and mechanistic variations across species
    • Conti E, Izaurralde E. Nonsense-mediated mRNA decay: Molecular insights and mechanistic variations across species. Curr Opin Cell Biol 2005; 17: 316-325.
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 316-325
    • Conti, E.1    Izaurralde, E.2
  • 46
    • 1442354190 scopus 로고    scopus 로고
    • An eIF4AIII-containing complex required for mRNA localization and nonsense-mediated mRNA decay
    • Palacios IM, Gatfield D, St Johnston D, Izaurralde E. An eIF4AIII-containing complex required for mRNA localization and nonsense-mediated mRNA decay. Nature 2004; 427: 753-757.
    • (2004) Nature , vol.427 , pp. 753-757
    • Palacios, I.M.1    Gatfield, D.2    St Johnston, D.3    Izaurralde, E.4
  • 47
    • 13444259647 scopus 로고    scopus 로고
    • Regulation of cap-dependent translation by eIF4E inhibitory proteins
    • Richter JD, Sonenberg N. Regulation of cap-dependent translation by eIF4E inhibitory proteins. Nature 2005; 433: 477-480.
    • (2005) Nature , vol.433 , pp. 477-480
    • Richter, J.D.1    Sonenberg, N.2
  • 48
    • 27144474796 scopus 로고    scopus 로고
    • The translation repressor 4E-BP2 is critical for eIF4F complex formation, synaptic plasticity, and memory in the hippocampus
    • Banko JL, Poulin F, Hou L, DeMaria CT, Sonenberg N, Klann E. The translation repressor 4E-BP2 is critical for eIF4F complex formation, synaptic plasticity, and memory in the hippocampus. J Neurosci 2005; 25: 9581-9590.
    • (2005) J Neurosci , vol.25 , pp. 9581-9590
    • Banko, J.L.1    Poulin, F.2    Hou, L.3    DeMaria, C.T.4    Sonenberg, N.5    Klann, E.6
  • 49
    • 0037099704 scopus 로고    scopus 로고
    • Dissolution of the maskin-eIF4E complex by cytoplasmic polyadenylation and poly(A)-binding protein controls cyclin B1 mRNA translation and oocyte maturation
    • Cao Q, Richter JD. Dissolution of the maskin-eIF4E complex by cytoplasmic polyadenylation and poly(A)-binding protein controls cyclin B1 mRNA translation and oocyte maturation. EMBO J 2002; 21: 3852-3862.
    • (2002) EMBO J , vol.21 , pp. 3852-3862
    • Cao, Q.1    Richter, J.D.2
  • 50
    • 33646865953 scopus 로고    scopus 로고
    • Translational control by neuroguidin, a eukaryotic initiation factor 4E and CPEB binding protein
    • Jung MY, Lorenz L, Richter JD. Translational control by neuroguidin, a eukaryotic initiation factor 4E and CPEB binding protein. Mol Cell Biol 2006; 26: 4277-4287.
    • (2006) Mol Cell Biol , vol.26 , pp. 4277-4287
    • Jung, M.Y.1    Lorenz, L.2    Richter, J.D.3
  • 52
    • 0346503888 scopus 로고    scopus 로고
    • Drosophila cup is an eIF4E binding protein that associates with Bruno and regulates oskar mRNA translation in oogenesis
    • Nakamura A, Sato K, Hanyu-Nakamura K. Drosophila cup is an eIF4E binding protein that associates with Bruno and regulates oskar mRNA translation in oogenesis. Dev Cell 2004; 6: 69-78.
    • (2004) Dev Cell , vol.6 , pp. 69-78
    • Nakamura, A.1    Sato, K.2    Hanyu-Nakamura, K.3
  • 53
    • 0346554981 scopus 로고    scopus 로고
    • Cup is an eIF4E binding protein required for both the translational repression of oskar and the recruitment of Barentsz
    • Wilhelm JE, Hilton M, Amos Q, Henzel WJ. Cup is an eIF4E binding protein required for both the translational repression of oskar and the recruitment of Barentsz. J Cell Biol 2003; 163: 1197-1204.
    • (2003) J Cell Biol , vol.163 , pp. 1197-1204
    • Wilhelm, J.E.1    Hilton, M.2    Amos, Q.3    Henzel, W.J.4
  • 55
    • 18844397041 scopus 로고    scopus 로고
    • A new paradigm for translational control: Inhibition via 5′-3′ mRNA tethering by Bicoid and the eIF4E cognate 4EHP
    • Cho PF, Poulin F, Cho-Park YA, Cho-Park IB, Chicoine JD, Lasko P, Sonenberg N. A new paradigm for translational control: Inhibition via 5′-3′ mRNA tethering by Bicoid and the eIF4E cognate 4EHP. Cell 2005; 121: 411-423.
    • (2005) Cell , vol.121 , pp. 411-423
    • Cho, P.F.1    Poulin, F.2    Cho-Park, Y.A.3    Cho-Park, I.B.4    Chicoine, J.D.5    Lasko, P.6    Sonenberg, N.7
  • 56
    • 0032215079 scopus 로고    scopus 로고
    • CPEB-mediated cytoplasmic polyadenylation and the regulation of experience-dependent translation of alpha-CaMKII mRNA at synapses
    • Wu L, Wells D, Tay J, Mendis D, Abbott MA, Barnitt A, Quinlan E, Heynen A, Fallon JR, Richter JD. CPEB-mediated cytoplasmic polyadenylation and the regulation of experience-dependent translation of alpha-CaMKII mRNA at synapses. Neuron 1998; 21: 1129-1139.
    • (1998) Neuron , vol.21 , pp. 1129-1139
    • Wu, L.1    Wells, D.2    Tay, J.3    Mendis, D.4    Abbott, M.A.5    Barnitt, A.6    Quinlan, E.7    Heynen, A.8    Fallon, J.R.9    Richter, J.D.10
  • 57
    • 12344290346 scopus 로고    scopus 로고
    • Mechanisms of translational control by the 3′ UTR in development and differentiation
    • de Moor CH, Meijer H, Lissenden S. Mechanisms of translational control by the 3′ UTR in development and differentiation. Semin Cell Dev Biol 2005; 16: 49-58.
    • (2005) Semin Cell Dev Biol , vol.16 , pp. 49-58
    • de Moor, C.H.1    Meijer, H.2    Lissenden, S.3
  • 58
    • 30344449514 scopus 로고    scopus 로고
    • Synaptic protein synthesis associated with memory is regulated by the RISC pathway in Drosophila
    • Ashraf SI, McLoon AL, Sclarsic SM, Kunes S. Synaptic protein synthesis associated with memory is regulated by the RISC pathway in Drosophila. Cell 2006; 124: 191-205.
    • (2006) Cell , vol.124 , pp. 191-205
    • Ashraf, S.I.1    McLoon, A.L.2    Sclarsic, S.M.3    Kunes, S.4
  • 63
    • 0030929165 scopus 로고    scopus 로고
    • Localization of Xenopus Vg1 mRNA by Vera protein and the endoplasmic reticulum
    • Deshler JO, Highett MI, Schnapp BJ. Localization of Xenopus Vg1 mRNA by Vera protein and the endoplasmic reticulum. Science 1997; 276: 1128-1131.
    • (1997) Science , vol.276 , pp. 1128-1131
    • Deshler, J.O.1    Highett, M.I.2    Schnapp, B.J.3
  • 65
    • 0035797518 scopus 로고    scopus 로고
    • Neurotrophin-induced transport of a beta-actin mRNP complex increases beta-actin levels and stimulates growth cone motility
    • Zhang HL, Eom T, Oleynikov Y, Shenoy SM, Liebelt DA, Dictenberg JB, Singer RH, Bassell GJ. Neurotrophin-induced transport of a beta-actin mRNP complex increases beta-actin levels and stimulates growth cone motility. Neuron 2001; 31: 261-275.
    • (2001) Neuron , vol.31 , pp. 261-275
    • Zhang, H.L.1    Eom, T.2    Oleynikov, Y.3    Shenoy, S.M.4    Liebelt, D.A.5    Dictenberg, J.B.6    Singer, R.H.7    Bassell, G.J.8
  • 66
    • 0032510715 scopus 로고    scopus 로고
    • hnRNP A2 selectively binds the cytoplasmic transport sequence of myelin basic protein mRNA
    • Hoek KS, Kidd GJ, Carson JH, Smith R. hnRNP A2 selectively binds the cytoplasmic transport sequence of myelin basic protein mRNA. Biochemistry 1998; 37: 7021-7029.
    • (1998) Biochemistry , vol.37 , pp. 7021-7029
    • Hoek, K.S.1    Kidd, G.J.2    Carson, J.H.3    Smith, R.4
  • 68
    • 17844372504 scopus 로고    scopus 로고
    • From mRNP trafficking to spine dysmorphogenesis: The roots of fragile X syndrome
    • Bagni C, Greenough WT. 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
  • 69
    • 33646194363 scopus 로고    scopus 로고
    • Metabotropic receptor-dependent long-term depression persists in the absence of protein synthesis in the mouse model of fragile X syndrome
    • Nosyreva ED, Huber KM. Metabotropic receptor-dependent long-term depression persists in the absence of protein synthesis in the mouse model of fragile X syndrome. J Neurophysiol 2006; 95: 3291-3295.
    • (2006) J Neurophysiol , vol.95 , pp. 3291-3295
    • Nosyreva, E.D.1    Huber, K.M.2
  • 70
    • 9644300809 scopus 로고    scopus 로고
    • FMRP and its target RNAs: Fishing for the specificity
    • Veneri M, Zalfa F, Bagni C. FMRP and its target RNAs: Fishing for the specificity. Neuroreport 2004; 15: 2447-2450.
    • (2004) Neuroreport , vol.15 , pp. 2447-2450
    • Veneri, M.1    Zalfa, F.2    Bagni, C.3
  • 71
    • 0347382502 scopus 로고    scopus 로고
    • Phosphorylation influences the translation state of FMRP-associated polyribosomes
    • Ceman S, O'Donnell WT, Reed M, Patton S, Pohl J, Warren ST. Phosphorylation influences the translation state of FMRP-associated polyribosomes. Hum Mol Genet 2003; 12: 3295-3305.
    • (2003) Hum Mol Genet , vol.12 , pp. 3295-3305
    • Ceman, S.1    O'Donnell, W.T.2    Reed, M.3    Patton, S.4    Pohl, J.5    Warren, S.T.6
  • 72
    • 0034687228 scopus 로고    scopus 로고
    • Synthesis of the posterior determinant Nanos is spatially restricted by a novel cotranslational regulatory mechanism
    • Clark IE, Wyckoff D, Gavis ER. Synthesis of the posterior determinant Nanos is spatially restricted by a novel cotranslational regulatory mechanism. Curr Biol 2000; 10: 1311-1314.
    • (2000) Curr Biol , vol.10 , pp. 1311-1314
    • Clark, I.E.1    Wyckoff, D.2    Gavis, E.R.3
  • 73
    • 4344679663 scopus 로고    scopus 로고
    • Localization-dependent oskar protein accumulation; control after the initiation of translation
    • Braat AK, Yan N, Arn E, Harrison D, Macdonald PM. Localization-dependent oskar protein accumulation; control after the initiation of translation. Dev Cell 2004; 7: 125-131.
    • (2004) Dev Cell , vol.7 , pp. 125-131
    • Braat, A.K.1    Yan, N.2    Arn, E.3    Harrison, D.4    Macdonald, P.M.5
  • 74
    • 0034109216 scopus 로고    scopus 로고
    • Molecular insights into mRNA transport and local translation in the mammalian nervous system
    • Kiebler MA, DesGroseillers L. Molecular insights into mRNA transport and local translation in the mammalian nervous system. Neuron 2000; 25: 19-28.
    • (2000) Neuron , vol.25 , pp. 19-28
    • Kiebler, M.A.1    DesGroseillers, L.2
  • 75
    • 0034653570 scopus 로고    scopus 로고
    • Distinct roles of two conserved Staufen domains in oskar mRNA localization and translation
    • Micklem DR, Adams J, Grunert S, St Johnston D. Distinct roles of two conserved Staufen domains in oskar mRNA localization and translation. EMBO J 2000; 19: 1366-1377.
    • (2000) EMBO J , vol.19 , pp. 1366-1377
    • Micklem, D.R.1    Adams, J.2    Grunert, S.3    St Johnston, D.4
  • 77
    • 3843145108 scopus 로고    scopus 로고
    • The brain-specific double-stranded RNA-binding protein Staufen2: Nucleolar accumulation and isoform-specific exportin-5-dependent export
    • Macchi P, Brownawell AM, Grunewald B, DesGroseillers L, Macara IG, Kiebler MA. The brain-specific double-stranded RNA-binding protein Staufen2: Nucleolar accumulation and isoform-specific exportin-5-dependent export. J Biol Chem 2004; 279: 31440-31444.
    • (2004) J Biol Chem , vol.279 , pp. 31440-31444
    • Macchi, P.1    Brownawell, A.M.2    Grunewald, B.3    DesGroseillers, L.4    Macara, I.G.5    Kiebler, M.A.6
  • 78
    • 30044443622 scopus 로고    scopus 로고
    • Staufen1 is imported into the nucleolus via a bipartite nuclear localization signal and several modulatory determinants
    • Martel C, Macchi P, Furic L, Kiebler MA, Desgroseillers L. Staufen1 is imported into the nucleolus via a bipartite nuclear localization signal and several modulatory determinants. Biochem J 2006; 393: 245-254.
    • (2006) Biochem J , vol.393 , pp. 245-254
    • Martel, C.1    Macchi, P.2    Furic, L.3    Kiebler, M.A.4    Desgroseillers, L.5
  • 79
    • 12944327374 scopus 로고    scopus 로고
    • Mammalian Staufen1 recruits Upf1 to specific mRNA 3′UTRs so as to elicit mRNA decay
    • Kim YK, Furic L, Desgroseillers L, Maquat LE. Mammalian Staufen1 recruits Upf1 to specific mRNA 3′UTRs so as to elicit mRNA decay. Cell 2005; 120: 195-208.
    • (2005) Cell , vol.120 , pp. 195-208
    • Kim, Y.K.1    Furic, L.2    Desgroseillers, L.3    Maquat, L.E.4
  • 81
    • 0037168109 scopus 로고    scopus 로고
    • Disruption of dendritic translation of CaMKIIalpha impairs stabilization of synaptic plasticity and memory consolidation
    • Miller S, Yasuda M, Coats JK, Jones Y, Martone ME, Mayford M. Disruption of dendritic translation of CaMKIIalpha impairs stabilization of synaptic plasticity and memory consolidation. Neuron 2002; 36: 507-519.
    • (2002) Neuron , vol.36 , pp. 507-519
    • Miller, S.1    Yasuda, M.2    Coats, J.K.3    Jones, Y.4    Martone, M.E.5    Mayford, M.6
  • 83
    • 0032191909 scopus 로고    scopus 로고
    • Synaptic activation causes the mRNA for the IEG Arc to localize selectively near activated postsynaptic sites on dendrites
    • Steward O, Wallace CS, Lyford GL, Worley PF. Synaptic activation causes the mRNA for the IEG Arc to localize selectively near activated postsynaptic sites on dendrites. Neuron 1998; 21: 741-751.
    • (1998) Neuron , vol.21 , pp. 741-751
    • Steward, O.1    Wallace, C.S.2    Lyford, G.L.3    Worley, P.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.