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Volumn 39, Issue , 2016, Pages 8-16

Specialization of biosynthetic membrane trafficking for neuronal form and function

Author keywords

[No Author keywords available]

Indexed keywords

CELL ORGANELLE; DENDRITE; DENDRITIC SPINE; ENDOPLASMIC RETICULUM; GOLGI COMPLEX; HUMAN; MEMBRANE TRANSPORT; NERVE CELL; NERVE CELL DIFFERENTIATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROCESSING; REVIEW; SECRETORY PATHWAY; SYNAPTIC TRANSMISSION; ANIMAL; CYTOLOGY; METABOLISM; PHYSIOLOGY; PROTEIN TRANSPORT;

EID: 84986630448     PISSN: 09594388     EISSN: 18736882     Source Type: Journal    
DOI: 10.1016/j.conb.2016.03.004     Document Type: Review
Times cited : (51)

References (96)
  • 1
    • 49749105225 scopus 로고    scopus 로고
    • Secretory outposts for the local processing of membrane cargo in neuronal dendrites
    • Hanus, C., Ehlers, M.D., Secretory outposts for the local processing of membrane cargo in neuronal dendrites. Traffic 9 (2008), 1437–1445.
    • (2008) Traffic , vol.9 , pp. 1437-1445
    • Hanus, C.1    Ehlers, M.D.2
  • 2
    • 84946557920 scopus 로고    scopus 로고
    • Diversifying the secretory routes in neurons
    • Valenzuela, J.I., Perez, F., Diversifying the secretory routes in neurons. Front Neurosci, 9, 2015, 358.
    • (2015) Front Neurosci , vol.9 , pp. 358
    • Valenzuela, J.I.1    Perez, F.2
  • 3
    • 84862728161 scopus 로고    scopus 로고
    • Vertebrate protein glycosylation: diversity, synthesis and function
    • Moremen, K.W., Tiemeyer, M., Nairn, A.V., Vertebrate protein glycosylation: diversity, synthesis and function. Nat Rev Mol Cell Biol 13 (2012), 448–462.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 448-462
    • Moremen, K.W.1    Tiemeyer, M.2    Nairn, A.V.3
  • 5
    • 85044265881 scopus 로고
    • The fine structure of the nervous system: the neurons and supporting cells
    • Peters, A., Palay, S.L., Webster, H.D., The fine structure of the nervous system: the neurons and supporting cells. Saunders, 1991.
    • (1991) Saunders
    • Peters, A.1    Palay, S.L.2    Webster, H.D.3
  • 6
    • 0020612480 scopus 로고
    • The neuronal endoplasmic reticulum: its cytochemistry and contribution to the endomembrane system. I. Cell bodies and dendrites
    • Broadwell, R.D., Cataldo, A.M., The neuronal endoplasmic reticulum: its cytochemistry and contribution to the endomembrane system. I. Cell bodies and dendrites. J Histochem Cytochem 31 (1983), 1077–1088.
    • (1983) J Histochem Cytochem , vol.31 , pp. 1077-1088
    • Broadwell, R.D.1    Cataldo, A.M.2
  • 7
    • 0032963006 scopus 로고    scopus 로고
    • Dendritic and postsynaptic protein synthetic machinery
    • Gardiol, A., Racca, C., Triller, A., Dendritic and postsynaptic protein synthetic machinery. J Neurosci 19 (1999), 168–179.
    • (1999) J Neurosci , vol.19 , pp. 168-179
    • Gardiol, A.1    Racca, C.2    Triller, A.3
  • 8
    • 0037088917 scopus 로고    scopus 로고
    • Endosomal compartments serve multiple hippocampal dendritic spines from a widespread rather than a local store of recycling membrane
    • Cooney, J.R., Hurlburt, J.L., Selig, D.K., Harris, K.M., Fiala, J.C., Endosomal compartments serve multiple hippocampal dendritic spines from a widespread rather than a local store of recycling membrane. J Neurosci 22 (2002), 2215–2224.
    • (2002) J Neurosci , vol.22 , pp. 2215-2224
    • Cooney, J.R.1    Hurlburt, J.L.2    Selig, D.K.3    Harris, K.M.4    Fiala, J.C.5
  • 9
    • 79953161238 scopus 로고    scopus 로고
    • The endoplasmic reticulum and protein trafficking in dendrites and axons
    • Ramírez, O.A., Couve, A., The endoplasmic reticulum and protein trafficking in dendrites and axons. Trends Cell Biol 21 (2011), 219–227.
    • (2011) Trends Cell Biol , vol.21 , pp. 219-227
    • Ramírez, O.A.1    Couve, A.2
  • 10
    • 0035974791 scopus 로고    scopus 로고
    • Stores not just for storage. Intracellular calcium release and synaptic plasticity
    • Rose, C.R., Konnerth, A., Stores not just for storage. Intracellular calcium release and synaptic plasticity. Neuron 31 (2001), 519–522.
    • (2001) Neuron , vol.31 , pp. 519-522
    • Rose, C.R.1    Konnerth, A.2
  • 11
    • 84955677104 scopus 로고    scopus 로고
    • Structure and function of ERmembrane contact sites with other organelles
    • Phillips, M.J., Voeltz, G.K., Structure and function of ERmembrane contact sites with other organelles. Nat Rev Mol Cell Biol 17 (2015), 69–82.
    • (2015) Nat Rev Mol Cell Biol , vol.17 , pp. 69-82
    • Phillips, M.J.1    Voeltz, G.K.2
  • 12
    • 0031023590 scopus 로고    scopus 로고
    • Three-dimensional organization of smooth endoplasmic reticulum in hippocampal CA1 dendrites and dendritic spines of the immature and mature rat
    • Spacek, J., Harris, K.M., Three-dimensional organization of smooth endoplasmic reticulum in hippocampal CA1 dendrites and dendritic spines of the immature and mature rat. J Neurosci 17 (1997), 190–203.
    • (1997) J Neurosci , vol.17 , pp. 190-203
    • Spacek, J.1    Harris, K.M.2
  • 13
    • 0029789053 scopus 로고    scopus 로고
    • Protein synthesis within dendrites: glycosylation of newly synthesized proteins in dendrites of hippocampal neurons in culture
    • Torre, E.R., Steward, O., Protein synthesis within dendrites: glycosylation of newly synthesized proteins in dendrites of hippocampal neurons in culture. J Neurosci 16 (1996), 5967–5978.
    • (1996) J Neurosci , vol.16 , pp. 5967-5978
    • Torre, E.R.1    Steward, O.2
  • 14
    • 0034110919 scopus 로고    scopus 로고
    • Translocation machinery for synthesis of integral membrane and secretory proteins in dendritic spines
    • Pierce, J.P., van Leyen, K., McCarthy, J.B., Translocation machinery for synthesis of integral membrane and secretory proteins in dendritic spines. Nat Neurosci 3 (2000), 311–313.
    • (2000) Nat Neurosci , vol.3 , pp. 311-313
    • Pierce, J.P.1    van Leyen, K.2    McCarthy, J.B.3
  • 15
    • 84856099972 scopus 로고    scopus 로고
    • Local zones of endoplasmic reticulum complexity confine cargo in neuronal dendrites
    • Cui-Wang, T., Hanus, C., Cui, T., Helton, T., Bourne, J., Watson, D., Harris, K.M., Ehlers, M.D., Local zones of endoplasmic reticulum complexity confine cargo in neuronal dendrites. Cell 148 (2012), 309–321.
    • (2012) Cell , vol.148 , pp. 309-321
    • Cui-Wang, T.1    Hanus, C.2    Cui, T.3    Helton, T.4    Bourne, J.5    Watson, D.6    Harris, K.M.7    Ehlers, M.D.8
  • 16
    • 1942489824 scopus 로고    scopus 로고
    • Endoplasmic reticulum export site formation and function in dendrites
    • Aridor, M., Endoplasmic reticulum export site formation and function in dendrites. J Neurosci 24 (2004), 3770–3776.
    • (2004) J Neurosci , vol.24 , pp. 3770-3776
    • Aridor, M.1
  • 17
    • 33745485316 scopus 로고    scopus 로고
    • The ER-Golgi intermediate compartment (ERGIC): in search of its identity and function
    • Appenzeller-Herzog, C., The ER-Golgi intermediate compartment (ERGIC): in search of its identity and function. J Cell Sci 119 (2006), 2173–2183.
    • (2006) J Cell Sci , vol.119 , pp. 2173-2183
    • Appenzeller-Herzog, C.1
  • 18
    • 0028817907 scopus 로고
    • The organization of the endoplasmic reticulum and the intermediate compartment in cultured rat hippocampal neurons
    • Krijnse-Locker, J., Parton, R.G., Fuller, S.D., Griffiths, G., Dotti, C.G., The organization of the endoplasmic reticulum and the intermediate compartment in cultured rat hippocampal neurons. Mol Biol Cell 6 (1995), 1315–1332.
    • (1995) Mol Biol Cell , vol.6 , pp. 1315-1332
    • Krijnse-Locker, J.1    Parton, R.G.2    Fuller, S.D.3    Griffiths, G.4    Dotti, C.G.5
  • 19
    • 84903437476 scopus 로고    scopus 로고
    • Synaptic control of secretory trafficking in dendrites
    • This study shows that synaptic activity restricts the long-range transport of nascent secretory cargo through a CaMK/KIF17 pathway, elucidating a novel mechanism for compartmentalized secretory processing in dendrites.
    • Hanus, C., Kochen, L., Dieck, S.T., Racine, V., Sibarita, J.-B., Schuman, E.M., Ehlers, M.D., Synaptic control of secretory trafficking in dendrites. Cell Rep, 2014, 10.1016/j.celrep.2014.05.028 This study shows that synaptic activity restricts the long-range transport of nascent secretory cargo through a CaMK/KIF17 pathway, elucidating a novel mechanism for compartmentalized secretory processing in dendrites.
    • (2014) Cell Rep
    • Hanus, C.1    Kochen, L.2    Dieck, S.T.3    Racine, V.4    Sibarita, J.-B.5    Schuman, E.M.6    Ehlers, M.D.7
  • 20
  • 23
    • 67651055363 scopus 로고    scopus 로고
    • Establishment of axon-dendrite polarity in developing neurons
    • Barnes, A.P., Polleux, F., Establishment of axon-dendrite polarity in developing neurons. Annu Rev Neurosci 32 (2009), 347–381.
    • (2009) Annu Rev Neurosci , vol.32 , pp. 347-381
    • Barnes, A.P.1    Polleux, F.2
  • 25
    • 0031461323 scopus 로고    scopus 로고
    • Neuronal polarity: vectorial cytoplasmic flow precedes axon formation
    • Bradke, F., Dotti, C.G., Neuronal polarity: vectorial cytoplasmic flow precedes axon formation. Neuron 19 (1997), 1175–1186.
    • (1997) Neuron , vol.19 , pp. 1175-1186
    • Bradke, F.1    Dotti, C.G.2
  • 26
    • 28744433842 scopus 로고    scopus 로고
    • Polarized secretory trafficking directs cargo for asymmetric dendrite growth and morphogenesis
    • Horton, A.C., Rácz, B., Monson, E.E., Lin, A.L., Weinberg, R.J., Ehlers, M.D., Polarized secretory trafficking directs cargo for asymmetric dendrite growth and morphogenesis. Neuron 48 (2005), 757–771.
    • (2005) Neuron , vol.48 , pp. 757-771
    • Horton, A.C.1    Rácz, B.2    Monson, E.E.3    Lin, A.L.4    Weinberg, R.J.5    Ehlers, M.D.6
  • 27
    • 0001186564 scopus 로고
    • Axo-somatic and axo-dendritic synapses of the cerebral cortex: an electron microscope study
    • Gray, D.W., Axo-somatic and axo-dendritic synapses of the cerebral cortex: an electron microscope study. J Anat 93 (1959), 420–433.
    • (1959) J Anat , vol.93 , pp. 420-433
    • Gray, D.W.1
  • 30
    • 0035814906 scopus 로고    scopus 로고
    • Evidence for a satellite secretory pathway in neuronal dendritic spines
    • Pierce, J.P., Mayer, T., McCarthy, J.B., Evidence for a satellite secretory pathway in neuronal dendritic spines. Curr Biol 11 (2001), 351–355.
    • (2001) Curr Biol , vol.11 , pp. 351-355
    • Pierce, J.P.1    Mayer, T.2    McCarthy, J.B.3
  • 31
    • 0032167980 scopus 로고    scopus 로고
    • Cell type and pathway dependence of synaptic AMPA receptor number and variability in the hippocampus
    • Nusser, Z., Lujan, R., Laube, G., Roberts, J.D., Molnar, E., Somogyi, P., Cell type and pathway dependence of synaptic AMPA receptor number and variability in the hippocampus. Neuron 21 (1998), 545–559.
    • (1998) Neuron , vol.21 , pp. 545-559
    • Nusser, Z.1    Lujan, R.2    Laube, G.3    Roberts, J.D.4    Molnar, E.5    Somogyi, P.6
  • 32
    • 0034175501 scopus 로고    scopus 로고
    • NMDA receptor content of synapses in stratum radiatum of the hippocampal CA1 area
    • Racca, C., Stephenson, F.A., Streit, P., Roberts, J.D., Somogyi, P., NMDA receptor content of synapses in stratum radiatum of the hippocampal CA1 area. J Neurosci 20 (2000), 2512–2522.
    • (2000) J Neurosci , vol.20 , pp. 2512-2522
    • Racca, C.1    Stephenson, F.A.2    Streit, P.3    Roberts, J.D.4    Somogyi, P.5
  • 34
    • 0035882286 scopus 로고    scopus 로고
    • Remodeling of synaptic membranes after induction of long-term potentiation
    • Toni, N., Buchs, P.A., Nikonenko, I., Povilaitite, P., Parisi, L., Muller, D., Remodeling of synaptic membranes after induction of long-term potentiation. J Neurosci 21 (2001), 6245–6251.
    • (2001) J Neurosci , vol.21 , pp. 6245-6251
    • Toni, N.1    Buchs, P.A.2    Nikonenko, I.3    Povilaitite, P.4    Parisi, L.5    Muller, D.6
  • 35
    • 0038382300 scopus 로고    scopus 로고
    • Dual modes of endoplasmic reticulum-to-Golgi transport in dendrites revealed by live-cell imaging
    • Horton, A.C., Ehlers, M.D., Dual modes of endoplasmic reticulum-to-Golgi transport in dendrites revealed by live-cell imaging. J Neurosci 23 (2003), 6188–6199.
    • (2003) J Neurosci , vol.23 , pp. 6188-6199
    • Horton, A.C.1    Ehlers, M.D.2
  • 36
    • 0022534294 scopus 로고
    • Heterogeneous distribution of the cAMP receptor protein RII in the nervous system: evidence for its intracellular accumulation on microtubules, microtubule-organizing centers, and in the area of the Golgi complex
    • De Camilli, P., Moretti, M., Donini, S.D., Walter, U., Lohmann, S.M., Heterogeneous distribution of the cAMP receptor protein RII in the nervous system: evidence for its intracellular accumulation on microtubules, microtubule-organizing centers, and in the area of the Golgi complex. J Cell Biol 103 (1986), 189–203.
    • (1986) J Cell Biol , vol.103 , pp. 189-203
    • De Camilli, P.1    Moretti, M.2    Donini, S.D.3    Walter, U.4    Lohmann, S.M.5
  • 37
    • 0028167602 scopus 로고
    • Polarized distribution of the trans-Golgi network marker TGN38 during the in vitro development of neocortical neurons: effects of nocodazole and brefeldin A
    • Lowenstein, P.R., Morrison, E.E., Bain, D., Shering, A.F., Banting, G., Douglas, P., Castro, M.G., Polarized distribution of the trans-Golgi network marker TGN38 during the in vitro development of neocortical neurons: effects of nocodazole and brefeldin A. Eur J Neurosci 6 (1994), 1453–1465.
    • (1994) Eur J Neurosci , vol.6 , pp. 1453-1465
    • Lowenstein, P.R.1    Morrison, E.E.2    Bain, D.3    Shering, A.F.4    Banting, G.5    Douglas, P.6    Castro, M.G.7
  • 38
    • 34547937104 scopus 로고    scopus 로고
    • Growing dendrites and axons differ in their reliance on the secretory pathway
    • Ye, B., Zhang, Y., Song, W., Younger, S.H., Jan, L.Y., Jan, Y.N., Growing dendrites and axons differ in their reliance on the secretory pathway. Cell 130 (2007), 717–729.
    • (2007) Cell , vol.130 , pp. 717-729
    • Ye, B.1    Zhang, Y.2    Song, W.3    Younger, S.H.4    Jan, L.Y.5    Jan, Y.N.6
  • 39
    • 84872696532 scopus 로고    scopus 로고
    • Golgi outposts shape dendrite morphology by functioning as sites of acentrosomal microtubule nucleation in neurons
    • Ori-McKenney, K.M., Jan, L.Y., Jan, Y.N., Golgi outposts shape dendrite morphology by functioning as sites of acentrosomal microtubule nucleation in neurons. Neuron 76 (2012), 921–930.
    • (2012) Neuron , vol.76 , pp. 921-930
    • Ori-McKenney, K.M.1    Jan, L.Y.2    Jan, Y.N.3
  • 40
    • 84942504950 scopus 로고    scopus 로고
    • Centrosomin represses dendrite branching by orienting microtubule nucleation
    • This study shows that polarized targeting of centrosomin — a centrosome-associated protein — to the cis face of Golgi outposts favors retrograde microtubule polymerization away from nascent dendritic branches providing important mechanistic insights into how Golgi Outposts shape dendritic morphology by locally organizing microtubule growth in neurons of the fly larvae body wall.
    • Yalgin, C., Ebrahimi, S., Delandre, C., Yoong, L.F., Akimoto, S., Tran, H., Amikura, R., Spokony, R., Torben-Nielsen, B., White, K.P., et al. Centrosomin represses dendrite branching by orienting microtubule nucleation. Nat Neurosci 18 (2015), 1437–1445 This study shows that polarized targeting of centrosomin — a centrosome-associated protein — to the cis face of Golgi outposts favors retrograde microtubule polymerization away from nascent dendritic branches providing important mechanistic insights into how Golgi Outposts shape dendritic morphology by locally organizing microtubule growth in neurons of the fly larvae body wall.
    • (2015) Nat Neurosci , vol.18 , pp. 1437-1445
    • Yalgin, C.1    Ebrahimi, S.2    Delandre, C.3    Yoong, L.F.4    Akimoto, S.5    Tran, H.6    Amikura, R.7    Spokony, R.8    Torben-Nielsen, B.9    White, K.P.10
  • 41
    • 84928771212 scopus 로고    scopus 로고
    • A RhoA signaling pathway regulates dendritic Golgi outpost formation
    • Expanding previous work on the topic, this study shows that the Golgi fission machinery is regulated by a RhoA signaling pathway and regulates the generation of dendritic Golgi outposts by fragmentation of the somatic Golgi.
    • Quassollo, G., Wojnacki, J., Salas, D.A., Gastaldi, L., Marzolo, M.P., Conde, C., Bisbal, M., Couve, A., Caceres A: A RhoA signaling pathway regulates dendritic Golgi outpost formation. Curr Biol 25 (2015), 971–982 Expanding previous work on the topic, this study shows that the Golgi fission machinery is regulated by a RhoA signaling pathway and regulates the generation of dendritic Golgi outposts by fragmentation of the somatic Golgi.
    • (2015) Curr Biol , vol.25 , pp. 971-982
    • Quassollo, G.1    Wojnacki, J.2    Salas, D.A.3    Gastaldi, L.4    Marzolo, M.P.5    Conde, C.6    Bisbal, M.7    Couve, A.8    Caceres A:9
  • 43
    • 84874586539 scopus 로고    scopus 로고
    • The angelman syndrome protein Ube3a/E6AP is required for Golgi acidification and surface protein sialylation
    • Condon, K.H., Ho, J., Robinson, C.G., Hanus, C., Ehlers, M.D., The angelman syndrome protein Ube3a/E6AP is required for Golgi acidification and surface protein sialylation. J Neurosci 33 (2013), 3799–3814.
    • (2013) J Neurosci , vol.33 , pp. 3799-3814
    • Condon, K.H.1    Ho, J.2    Robinson, C.G.3    Hanus, C.4    Ehlers, M.D.5
  • 44
    • 0013085340 scopus 로고    scopus 로고
    • Golgins in the structure and dynamics of the Golgi apparatus
    • Barr, F.A., Short, B., Golgins in the structure and dynamics of the Golgi apparatus. Curr Opin Cell Biol 15 (2003), 405–413.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 405-413
    • Barr, F.A.1    Short, B.2
  • 45
    • 0042266395 scopus 로고    scopus 로고
    • Cell-cycle-specific Golgi fragmentation: how and why?
    • Colanzi, A., Suetterlin, C., Malhotra, V., Cell-cycle-specific Golgi fragmentation: how and why?. Curr Opin Cell Biol 15 (2003), 462–467.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 462-467
    • Colanzi, A.1    Suetterlin, C.2    Malhotra, V.3
  • 46
    • 84946570015 scopus 로고    scopus 로고
    • Golgi fragmentation in Alzheimer's disease
    • Joshi, G., Bekier, M.E., Wang, Y., Golgi fragmentation in Alzheimer's disease. Front Neurosci, 2015, 9.
    • (2015) Front Neurosci , pp. 9
    • Joshi, G.1    Bekier, M.E.2    Wang, Y.3
  • 47
    • 84946574062 scopus 로고    scopus 로고
    • Golgi fragmentation in amyotrophic lateral sclerosis, an overview of possible triggers and consequences
    • Sundaramoorthy, V., Sultana, J.M., Atkin, J.D., Golgi fragmentation in amyotrophic lateral sclerosis, an overview of possible triggers and consequences. Front Neurosci, 2015, 9.
    • (2015) Front Neurosci , pp. 9
    • Sundaramoorthy, V.1    Sultana, J.M.2    Atkin, J.D.3
  • 48
    • 84876479778 scopus 로고    scopus 로고
    • Differential dendritic targeting of AMPA receptor subunit mRNAs in adult rat hippocampal principal neurons and interneurons
    • Cox, D.J., Racca, C., Differential dendritic targeting of AMPA receptor subunit mRNAs in adult rat hippocampal principal neurons and interneurons. J Comp Neurol 521 (2013), 1954–2007.
    • (2013) J Comp Neurol , vol.521 , pp. 1954-2007
    • Cox, D.J.1    Racca, C.2
  • 49
    • 84883173783 scopus 로고    scopus 로고
    • Proteostasis in complex dendrites
    • A review of current research on local translation in dendrites that discusses how local protein synthesis and protein stability influence protein exchanges on a local scale and across the entire dendritic tree This review also documents neuron-type specific variations of the volume of the somatic Golgi apparatus in hippocampal pyramidal neurons.
    • Hanus, C., Schuman, E.M., Proteostasis in complex dendrites. Nat Rev Neurosci 14 (2013), 538–648 A review of current research on local translation in dendrites that discusses how local protein synthesis and protein stability influence protein exchanges on a local scale and across the entire dendritic tree This review also documents neuron-type specific variations of the volume of the somatic Golgi apparatus in hippocampal pyramidal neurons.
    • (2013) Nat Rev Neurosci , vol.14 , pp. 538-648
    • Hanus, C.1    Schuman, E.M.2
  • 50
    • 27744482336 scopus 로고    scopus 로고
    • Traffic of Kv4 K+ channels mediated by KChIP1 is via a novel post-ER vesicular pathway
    • Hasdemir, B., Traffic of Kv4 K+ channels mediated by KChIP1 is via a novel post-ER vesicular pathway. J Cell Biol 171 (2005), 459–469.
    • (2005) J Cell Biol , vol.171 , pp. 459-469
    • Hasdemir, B.1
  • 52
    • 84860661767 scopus 로고    scopus 로고
    • The local transcriptome in the synaptic neuropil revealed by deep sequencing and high-resolution imaging
    • Cajigas, I.J., Tushev, G., Will, T.J., Dieck, S.T., Fuerst, N., Schuman, E.M., The local transcriptome in the synaptic neuropil revealed by deep sequencing and high-resolution imaging. Neuron 74 (2012), 453–466.
    • (2012) Neuron , vol.74 , pp. 453-466
    • Cajigas, I.J.1    Tushev, G.2    Will, T.J.3    Dieck, S.T.4    Fuerst, N.5    Schuman, E.M.6
  • 53
    • 84864306858 scopus 로고    scopus 로고
    • Differential trafficking of transport vesicles contributes to the localization of dendritic proteins
    • Xu, M., Wandless, T.J., Arnold, D.B., Differential trafficking of transport vesicles contributes to the localization of dendritic proteins. Cell Rep 2 (2012), 89–100.
    • (2012) Cell Rep , vol.2 , pp. 89-100
    • Xu, M.1    Wandless, T.J.2    Arnold, D.B.3
  • 54
    • 62649108345 scopus 로고    scopus 로고
    • Activation of CaMKII in single dendritic spines during long-term potentiation
    • Lee, S.-J.R., Escobedo-Lozoya, Y., Szatmari, E.M., Yasuda, R., Activation of CaMKII in single dendritic spines during long-term potentiation. Nature 458 (2009), 299–304.
    • (2009) Nature , vol.458 , pp. 299-304
    • Lee, S.-J.R.1    Escobedo-Lozoya, Y.2    Szatmari, E.M.3    Yasuda, R.4
  • 55
    • 84944680459 scopus 로고    scopus 로고
    • ScienceDirectEstablishment of NE asymmetry — targeting of membrane proteins to the inner nuclear membrane
    • Ungricht, R., Kutay, U., ScienceDirectEstablishment of NE asymmetry — targeting of membrane proteins to the inner nuclear membrane. Curr Opin Cell Biol 34 (2015), 135–141.
    • (2015) Curr Opin Cell Biol , vol.34 , pp. 135-141
    • Ungricht, R.1    Kutay, U.2
  • 57
    • 0037062942 scopus 로고    scopus 로고
    • Transmitter-evoked local calcium release stabilizes developing dendrites
    • Lohmann, C., Myhr, K.L., Wong, R.O.L., Transmitter-evoked local calcium release stabilizes developing dendrites. Nature 418 (2002), 177–181.
    • (2002) Nature , vol.418 , pp. 177-181
    • Lohmann, C.1    Myhr, K.L.2    Wong, R.O.L.3
  • 61
    • 84900422669 scopus 로고    scopus 로고
    • Protrudin regulates endoplasmic reticulum morphology and function associated with the pathogenesis of hereditary spastic paraplegia
    • This study shows that protrudin — a protein that regulates polarized vesicular trafficking in neurons and whose gene is mutated in a subset of individuals with hereditary spastic paraplegia (HSP) — interacts with other HSP-related proteins and regulates ER morphology and function. The study shows that protrudin deregulation by mutation is a causative defect in HSP, delineating a mechanistic link between protrudin, ER-stress and HSP.
    • Hashimoto, Y., Shirane, M., Matsuzaki, F., Saita, S., Ohnishi, T., Nakayama, K.I., Protrudin regulates endoplasmic reticulum morphology and function associated with the pathogenesis of hereditary spastic paraplegia. J Biol Chem 289 (2014), 12946–12961 This study shows that protrudin — a protein that regulates polarized vesicular trafficking in neurons and whose gene is mutated in a subset of individuals with hereditary spastic paraplegia (HSP) — interacts with other HSP-related proteins and regulates ER morphology and function. The study shows that protrudin deregulation by mutation is a causative defect in HSP, delineating a mechanistic link between protrudin, ER-stress and HSP.
    • (2014) J Biol Chem , vol.289 , pp. 12946-12961
    • Hashimoto, Y.1    Shirane, M.2    Matsuzaki, F.3    Saita, S.4    Ohnishi, T.5    Nakayama, K.I.6
  • 62
    • 36849012562 scopus 로고    scopus 로고
    • Endoplasmic reticulum remains continuous and undergoes sheet-to-tubule transformation during cell division in mammalian cells
    • Puhka, M., Vihinen, H., Joensuu, M., Jokitalo, E., Endoplasmic reticulum remains continuous and undergoes sheet-to-tubule transformation during cell division in mammalian cells. J Cell Biol 179 (2007), 895–909.
    • (2007) J Cell Biol , vol.179 , pp. 895-909
    • Puhka, M.1    Vihinen, H.2    Joensuu, M.3    Jokitalo, E.4
  • 63
    • 34347214798 scopus 로고    scopus 로고
    • Marlin-1 and conventional kinesin link GABAB receptors to the cytoskeleton and regulate receptor transport
    • Vidal, R.L., Ramírez, O.A., Sandoval, L., Koenig-Robert, R., Härtel, S., Couve, A., Marlin-1 and conventional kinesin link GABAB receptors to the cytoskeleton and regulate receptor transport. Mol Cell Neurosci 35 (2007), 501–512.
    • (2007) Mol Cell Neurosci , vol.35 , pp. 501-512
    • Vidal, R.L.1    Ramírez, O.A.2    Sandoval, L.3    Koenig-Robert, R.4    Härtel, S.5    Couve, A.6
  • 64
    • 37749000849 scopus 로고    scopus 로고
    • Disruption of KIF17-Mint1 interaction by CaMKII-dependent phosphorylation: a molecular model of kinesin-cargo release
    • Guillaud, L., Wong, R., Hirokawa, N., Disruption of KIF17-Mint1 interaction by CaMKII-dependent phosphorylation: a molecular model of kinesin-cargo release. Nat Cell Biol 10 (2008), 19–29.
    • (2008) Nat Cell Biol , vol.10 , pp. 19-29
    • Guillaud, L.1    Wong, R.2    Hirokawa, N.3
  • 65
    • 0034625631 scopus 로고    scopus 로고
    • Kinesin superfamily motor protein KIF17 and mLin-10 in NMDA receptor-containing vesicle transport
    • Setou, M., Nakagawa, T., Seog, D.H., Hirokawa, N., Kinesin superfamily motor protein KIF17 and mLin-10 in NMDA receptor-containing vesicle transport. Science 288 (2000), 1796–1802.
    • (2000) Science , vol.288 , pp. 1796-1802
    • Setou, M.1    Nakagawa, T.2    Seog, D.H.3    Hirokawa, N.4
  • 66
    • 33644867158 scopus 로고    scopus 로고
    • A role for Kif17 in transport of Kv4.2
    • Chu, P.J., A role for Kif17 in transport of Kv4.2. J Biol Chem 281 (2005), 365–373.
    • (2005) J Biol Chem , vol.281 , pp. 365-373
    • Chu, P.J.1
  • 67
    • 84859758095 scopus 로고    scopus 로고
    • Regulation of NMDA receptor transport: a KIF17-cargo binding/releasing underlies synaptic plasticity and memory in vivo
    • Yin, X., Feng, X., Takei, Y., Hirokawa, N., Regulation of NMDA receptor transport: a KIF17-cargo binding/releasing underlies synaptic plasticity and memory in vivo. J Neurosci 32 (2012), 5486–5499.
    • (2012) J Neurosci , vol.32 , pp. 5486-5499
    • Yin, X.1    Feng, X.2    Takei, Y.3    Hirokawa, N.4
  • 68
    • 84890500709 scopus 로고    scopus 로고
    • Kinesin-1 regulates synaptic strength by mediating the delivery, removal, and redistribution of AMPA receptors
    • Hoerndli, F.J., Maxfield, D.A., Brockie, P.J., Mellem, J.E., Jensen, E., Wang, R., Madsen, D.M., Maricq, A.V., Kinesin-1 regulates synaptic strength by mediating the delivery, removal, and redistribution of AMPA receptors. Neuron 80 (2013), 1421–1437.
    • (2013) Neuron , vol.80 , pp. 1421-1437
    • Hoerndli, F.J.1    Maxfield, D.A.2    Brockie, P.J.3    Mellem, J.E.4    Jensen, E.5    Wang, R.6    Madsen, D.M.7    Maricq, A.V.8
  • 71
    • 84880331334 scopus 로고    scopus 로고
    • The ALS8 protein VAPB interacts with the ER-Golgi recycling protein YIF1A and regulates membrane delivery into dendrites
    • This study shows that VAPB — an integral membrane protein localized to the endoplasmic reticulum (ER) — whose mutation (P56S) has been linked to motor neuron degeneration in amyotrophic lateral sclerosis type 8 (ALS8) — binds to the ERGIC protein YIF1A Both proteins are required for intracellular membrane trafficking into dendrites and normal dendritic morphology. VAPB — P56S also interacts with YIF1A but disrupts YIF1A localization to ERGIC, suggesting a mechanistic link between deregulation of ER-to-Golgi transport and VAPB-associated motor neuron disease.
    • Kuijpers, M., Lou Yu, K., Teuling, E., Akhmanova, A., Jaarsma, D., Hoogenraad, C.C., The ALS8 protein VAPB interacts with the ER-Golgi recycling protein YIF1A and regulates membrane delivery into dendrites. EMBO J 32 (2013), 2056–2072 This study shows that VAPB — an integral membrane protein localized to the endoplasmic reticulum (ER) — whose mutation (P56S) has been linked to motor neuron degeneration in amyotrophic lateral sclerosis type 8 (ALS8) — binds to the ERGIC protein YIF1A Both proteins are required for intracellular membrane trafficking into dendrites and normal dendritic morphology. VAPB — P56S also interacts with YIF1A but disrupts YIF1A localization to ERGIC, suggesting a mechanistic link between deregulation of ER-to-Golgi transport and VAPB-associated motor neuron disease.
    • (2013) EMBO J , vol.32 , pp. 2056-2072
    • Kuijpers, M.1    Lou Yu, K.2    Teuling, E.3    Akhmanova, A.4    Jaarsma, D.5    Hoogenraad, C.C.6
  • 73
    • 0027953550 scopus 로고
    • Dominant inhibitory mutants of ARF1 block endoplasmic reticulum to Golgi transport and trigger disassembly of the Golgi apparatus
    • Dascher, C., Balch, W.E., Dominant inhibitory mutants of ARF1 block endoplasmic reticulum to Golgi transport and trigger disassembly of the Golgi apparatus. J Biol Chem 269 (1994), 1437–1448.
    • (1994) J Biol Chem , vol.269 , pp. 1437-1448
    • Dascher, C.1    Balch, W.E.2
  • 77
    • 33745421381 scopus 로고    scopus 로고
    • Rab1 defines a novel pathway connecting the pre-Golgi intermediate compartment with the cell periphery
    • Sannerud, R., Marie, M., Nizak, C., Dale, H.A., Pernet-Gallay, K., Perez, F., Goud, B., Saraste, J., Rab1 defines a novel pathway connecting the pre-Golgi intermediate compartment with the cell periphery. Mol Biol Cell 17 (2006), 1514–1526.
    • (2006) Mol Biol Cell , vol.17 , pp. 1514-1526
    • Sannerud, R.1    Marie, M.2    Nizak, C.3    Dale, H.A.4    Pernet-Gallay, K.5    Perez, F.6    Goud, B.7    Saraste, J.8
  • 78
    • 0016785996 scopus 로고
    • Intracellular aspects of the process of protein synthesis
    • Palade, G., Intracellular aspects of the process of protein synthesis. Science 189 (1975), 347–358.
    • (1975) Science , vol.189 , pp. 347-358
    • Palade, G.1
  • 79
    • 34547556737 scopus 로고    scopus 로고
    • Rapid synthesis and synaptic insertion of GluR2 for mGluR-LTD in the ventral tegmental area
    • Mameli, M., Balland, B., Luján, R., Lüscher, C., Rapid synthesis and synaptic insertion of GluR2 for mGluR-LTD in the ventral tegmental area. Science 317 (2007), 530–533.
    • (2007) Science , vol.317 , pp. 530-533
    • Mameli, M.1    Balland, B.2    Luján, R.3    Lüscher, C.4
  • 80
    • 84862266808 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor activation of CaM-kinase kinase via transient receptor potential canonical channels induces the translation and synaptic incorporation of GluA1-containing calcium-permeable AMPA receptors
    • Fortin, D.A., Srivastava, T., Dwarakanath, D., Pierre, P., Nygaard, S., Derkach, V.A., Soderling, T.R., Brain-derived neurotrophic factor activation of CaM-kinase kinase via transient receptor potential canonical channels induces the translation and synaptic incorporation of GluA1-containing calcium-permeable AMPA receptors. J Neurosci 32 (2012), 8127–8137.
    • (2012) J Neurosci , vol.32 , pp. 8127-8137
    • Fortin, D.A.1    Srivastava, T.2    Dwarakanath, D.3    Pierre, P.4    Nygaard, S.5    Derkach, V.A.6    Soderling, T.R.7
  • 81
    • 84877791275 scopus 로고    scopus 로고
    • Dendritic GluN2A synthesis mediates activity-induced NMDA receptor insertion
    • Swanger, S.A., He, Y.A., Richter, J.D., Bassell, G.J., Dendritic GluN2A synthesis mediates activity-induced NMDA receptor insertion. J Neurosci 33 (2013), 8898–8908.
    • (2013) J Neurosci , vol.33 , pp. 8898-8908
    • Swanger, S.A.1    He, Y.A.2    Richter, J.D.3    Bassell, G.J.4
  • 82
    • 0025940101 scopus 로고
    • Brefeldin A's effects on endosomes, lysosomes, and the TGN suggest a general mechanism for regulating organelle structure and membrane traffic
    • Lippincott-Schwartz, J., Yuan, L., Tipper, C., Amherdt, M., Orci, L., Klausner, R.D., Brefeldin A's effects on endosomes, lysosomes, and the TGN suggest a general mechanism for regulating organelle structure and membrane traffic. Cell 67 (1991), 601–616.
    • (1991) Cell , vol.67 , pp. 601-616
    • Lippincott-Schwartz, J.1    Yuan, L.2    Tipper, C.3    Amherdt, M.4    Orci, L.5    Klausner, R.D.6
  • 83
    • 84943574493 scopus 로고    scopus 로고
    • RAB-10-dependent membrane transport is required for dendrite arborization
    • Zou, W., Yadav, S., DeVault, L., Jan, Y.N., Sherwood, D.R., RAB-10-dependent membrane transport is required for dendrite arborization. PLoS Genet, 11, 2015, e1005484.
    • (2015) PLoS Genet , vol.11 , pp. e1005484
    • Zou, W.1    Yadav, S.2    DeVault, L.3    Jan, Y.N.4    Sherwood, D.R.5
  • 84
    • 78751512146 scopus 로고    scopus 로고
    • Cell polarity during motile processes: keeping on track with the exocyst complex
    • Hertzog, M., Chavrier, P., Cell polarity during motile processes: keeping on track with the exocyst complex. Biochem J 433 (2011), 403–409.
    • (2011) Biochem J , vol.433 , pp. 403-409
    • Hertzog, M.1    Chavrier, P.2
  • 85
    • 28544437382 scopus 로고    scopus 로고
    • Ral GTPases regulate neurite branching through GAP-43 and the exocyst complex
    • Lalli, G., Hall, A., Ral GTPases regulate neurite branching through GAP-43 and the exocyst complex. J Cell Biol 171 (2005), 857–869.
    • (2005) J Cell Biol , vol.171 , pp. 857-869
    • Lalli, G.1    Hall, A.2
  • 86
    • 84953307348 scopus 로고    scopus 로고
    • RAB-10 regulates dendritic branching by balancing dendritic transport
    • Taylor, C.A., Yan, J., Howell, A.S., Dong, X., Shen, K., RAB-10 regulates dendritic branching by balancing dendritic transport. PLoS Genet, 11, 2015, e1005695.
    • (2015) PLoS Genet , vol.11 , pp. e1005695
    • Taylor, C.A.1    Yan, J.2    Howell, A.S.3    Dong, X.4    Shen, K.5
  • 87
    • 77953240454 scopus 로고    scopus 로고
    • Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints
    • Zielinska, D.F., Gnad, F., Wiśniewski, J.R., Mann, M., Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints. Cell 141 (2010), 897–907.
    • (2010) Cell , vol.141 , pp. 897-907
    • Zielinska, D.F.1    Gnad, F.2    Wiśniewski, J.R.3    Mann, M.4
  • 88
    • 84921651569 scopus 로고    scopus 로고
    • TARP γ-8 glycosylation regulates the surface expression of AMPA receptors
    • Zheng, C.-Y., Chang, K., Suh, Y.H., Roche, K.W., TARP γ-8 glycosylation regulates the surface expression of AMPA receptors. Biochem J 465 (2015), 471–477.
    • (2015) Biochem J , vol.465 , pp. 471-477
    • Zheng, C.-Y.1    Chang, K.2    Suh, Y.H.3    Roche, K.W.4
  • 89
    • 84937684236 scopus 로고    scopus 로고
    • Two N-glycosylation sites in the GluN1 subunit are essential for releasing NMDA receptors from the endoplasmic reticulum
    • Lichnerova, K., Kaniakova, M., Park, S.P., Skrenkova, K., Wang, Y.-X., Petralia, R.S., Suh, Y.H., Horak, M., Two N-glycosylation sites in the GluN1 subunit are essential for releasing NMDA receptors from the endoplasmic reticulum. J Biol Chem, 2015, 10.1074/jbc.M115.656546.
    • (2015) J Biol Chem
    • Lichnerova, K.1    Kaniakova, M.2    Park, S.P.3    Skrenkova, K.4    Wang, Y.-X.5    Petralia, R.S.6    Suh, Y.H.7    Horak, M.8
  • 91
    • 84928928913 scopus 로고    scopus 로고
    • Direct visualization of newly synthesized target proteins in situ
    • This study describes a novel method that couples noncanonical amino acid tagging or puromycylation with the proximity ligation assay to visualize specific newly synthesized proteins and monitor their origin, redistribution and turnover in situ.
    • tom Dieck, S., Kochen, L., Hanus, C., Heumüller, M., Bartnik, I., Nassim-Assir, B., Merk, K., Mosler, T., Garg, S., Bunse, S., et al. Direct visualization of newly synthesized target proteins in situ. Nat Meth, 2015, 10.1038/nmeth.3319 This study describes a novel method that couples noncanonical amino acid tagging or puromycylation with the proximity ligation assay to visualize specific newly synthesized proteins and monitor their origin, redistribution and turnover in situ.
    • (2015) Nat Meth
    • tom Dieck, S.1    Kochen, L.2    Hanus, C.3    Heumüller, M.4    Bartnik, I.5    Nassim-Assir, B.6    Merk, K.7    Mosler, T.8    Garg, S.9    Bunse, S.10
  • 92
    • 84890685452 scopus 로고    scopus 로고
    • Imaging the glycosylation state of cell surface glycoproteins by two-photon fluorescence lifetime imaging microscopy
    • This study describes a novel FRET-based method that couples noncanonical sugar tagging with antibody binding to visualize specific surface-expressed proteins based on their glycosylation profile, opening new avenues to study the distribution and dynamics of glycoproteins in living cells.
    • Belardi, B., la Zerda de, A., Spiciarich, D.R., Maund, S.L., Peehl, D.M., Bertozzi, C.R., Imaging the glycosylation state of cell surface glycoproteins by two-photon fluorescence lifetime imaging microscopy. Angew Chem Int Ed Engl 52 (2013), 14045–14049 This study describes a novel FRET-based method that couples noncanonical sugar tagging with antibody binding to visualize specific surface-expressed proteins based on their glycosylation profile, opening new avenues to study the distribution and dynamics of glycoproteins in living cells.
    • (2013) Angew Chem Int Ed Engl , vol.52 , pp. 14045-14049
    • Belardi, B.1    la Zerda de, A.2    Spiciarich, D.R.3    Maund, S.L.4    Peehl, D.M.5    Bertozzi, C.R.6
  • 95
    • 84864306858 scopus 로고    scopus 로고
    • Differential trafficking of transport vesicles contributes to the localizationof dendritic proteins
    • Al-Bassam, S., Xu, M., Wandless, T.J., Arnold, D.B., Differential trafficking of transport vesicles contributes to the localizationof dendritic proteins. Cell Rep 2 (2012), 89–100.
    • (2012) Cell Rep , vol.2 , pp. 89-100
    • Al-Bassam, S.1    Xu, M.2    Wandless, T.J.3    Arnold, D.B.4
  • 96
    • 84878586112 scopus 로고    scopus 로고
    • A light-triggered protein secretion system
    • This study describes novel optogenetic tools to control the progression of model cargo in the secretory pathway with high spatio-temporal resolution, and makes use of this assay to demonstrate restricted, local trafficking of nascent cargo near dendritic branch points.
    • Chen, D., Gibson, E.S., Kennedy, M.J., A light-triggered protein secretion system. J Cell Biol 201 (2013), 631–640 This study describes novel optogenetic tools to control the progression of model cargo in the secretory pathway with high spatio-temporal resolution, and makes use of this assay to demonstrate restricted, local trafficking of nascent cargo near dendritic branch points.
    • (2013) J Cell Biol , vol.201 , pp. 631-640
    • Chen, D.1    Gibson, E.S.2    Kennedy, M.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.