메뉴 건너뛰기




Volumn 28, Issue 4, 2014, Pages 381-393

The GRIP1/14-3-3 pathway coordinates cargo trafficking and dendrite development

Author keywords

[No Author keywords available]

Indexed keywords

14-3-3 PROTEINS; ADAPTOR PROTEINS, SIGNAL TRANSDUCING; ANIMALS; CARRIER PROTEINS; DENDRITES; GENE KNOCKOUT TECHNIQUES; KINESIN; MICE; MUTATION; NERVE TISSUE PROTEINS; PROTEIN BINDING; PROTEIN TRANSPORT; SIGNAL TRANSDUCTION; TRANSCRIPTION FACTORS;

EID: 84894361563     PISSN: 15345807     EISSN: 18781551     Source Type: Journal    
DOI: 10.1016/j.devcel.2014.01.018     Document Type: Article
Times cited : (24)

References (51)
  • 2
    • 0033103887 scopus 로고    scopus 로고
    • EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft membrane microdomains
    • Brückner K., Pablo Labrador J., Scheiffele P., Herb A., Seeburg P.H., Klein R. EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft membrane microdomains. Neuron 1999, 22:511-524.
    • (1999) Neuron , vol.22 , pp. 511-524
    • Brückner, K.1    Pablo Labrador, J.2    Scheiffele, P.3    Herb, A.4    Seeburg, P.H.5    Klein, R.6
  • 3
    • 44649201117 scopus 로고    scopus 로고
    • Activity-dependent regulation of synaptic AMPA receptor composition and abundance by beta3 integrins
    • Cingolani L.A., Thalhammer A., Yu L.M., Catalano M., Ramos T., Colicos M.A., Goda Y. Activity-dependent regulation of synaptic AMPA receptor composition and abundance by beta3 integrins. Neuron 2008, 58:749-762.
    • (2008) Neuron , vol.58 , pp. 749-762
    • Cingolani, L.A.1    Thalhammer, A.2    Yu, L.M.3    Catalano, M.4    Ramos, T.5    Colicos, M.A.6    Goda, Y.7
  • 4
    • 0036584774 scopus 로고    scopus 로고
    • Differential palmitoylation directs the AMPA receptor-binding protein ABP to spines or to intracellular clusters
    • DeSouza S., Fu J., States B.A., Ziff E.B. Differential palmitoylation directs the AMPA receptor-binding protein ABP to spines or to intracellular clusters. J.Neurosci. 2002, 22:3493-3503.
    • (2002) J.Neurosci. , vol.22 , pp. 3493-3503
    • DeSouza, S.1    Fu, J.2    States, B.A.3    Ziff, E.B.4
  • 5
    • 44449121279 scopus 로고    scopus 로고
    • A direct role for FMRP in activity-dependent dendritic mRNA transport links filopodial-spine morphogenesis to fragile X syndrome
    • Dictenberg J.B., Swanger S.A., Antar L.N., Singer R.H., Bassell G.J. A direct role for FMRP in activity-dependent dendritic mRNA transport links filopodial-spine morphogenesis to fragile X syndrome. Dev. Cell 2008, 14:926-939.
    • (2008) Dev. Cell , vol.14 , pp. 926-939
    • Dictenberg, J.B.1    Swanger, S.A.2    Antar, L.N.3    Singer, R.H.4    Bassell, G.J.5
  • 6
    • 0030900558 scopus 로고    scopus 로고
    • GRIP: a synaptic PDZ domain-containing protein that interacts with AMPA receptors
    • Dong H., O'Brien R.J., Fung E.T., Lanahan A.A., Worley P.F., Huganir R.L. GRIP: a synaptic PDZ domain-containing protein that interacts with AMPA receptors. Nature 1997, 386:279-284.
    • (1997) Nature , vol.386 , pp. 279-284
    • Dong, H.1    O'Brien, R.J.2    Fung, E.T.3    Lanahan, A.A.4    Worley, P.F.5    Huganir, R.L.6
  • 7
    • 0033567072 scopus 로고    scopus 로고
    • Characterization of the glutamate receptor-interacting proteins GRIP1 and GRIP2
    • Dong H., Zhang P., Song I., Petralia R.S., Liao D., Huganir R.L. Characterization of the glutamate receptor-interacting proteins GRIP1 and GRIP2. J.Neurosci. 1999, 19:6930-6941.
    • (1999) J.Neurosci. , vol.19 , pp. 6930-6941
    • Dong, H.1    Zhang, P.2    Song, I.3    Petralia, R.S.4    Liao, D.5    Huganir, R.L.6
  • 8
    • 34548291030 scopus 로고    scopus 로고
    • Secrets of the secretory pathway in dendrite growth
    • Ehlers M.D. Secrets of the secretory pathway in dendrite growth. Neuron 2007, 55:686-689.
    • (2007) Neuron , vol.55 , pp. 686-689
    • Ehlers, M.D.1
  • 10
    • 84880014019 scopus 로고    scopus 로고
    • Microtubule-based transport - basic mechanisms, traffic rules and role in neurological pathogenesis
    • Franker M.A., Hoogenraad C.C. Microtubule-based transport - basic mechanisms, traffic rules and role in neurological pathogenesis. J.Cell Sci. 2013, 126:2319-2329.
    • (2013) J.Cell Sci. , vol.126 , pp. 2319-2329
    • Franker, M.A.1    Hoogenraad, C.C.2
  • 11
    • 0037223301 scopus 로고    scopus 로고
    • KIF17 dynamics and regulation of NR2B trafficking in hippocampal neurons
    • Guillaud L., Setou M., Hirokawa N. KIF17 dynamics and regulation of NR2B trafficking in hippocampal neurons. J.Neurosci. 2003, 23:131-140.
    • (2003) J.Neurosci. , vol.23 , pp. 131-140
    • Guillaud, L.1    Setou, M.2    Hirokawa, N.3
  • 12
    • 78449269612 scopus 로고    scopus 로고
    • Molecular motors in neurons: transport mechanisms and roles in brain function, development, and disease
    • Hirokawa N., Niwa S., Tanaka Y. Molecular motors in neurons: transport mechanisms and roles in brain function, development, and disease. Neuron 2010, 68:610-638.
    • (2010) Neuron , vol.68 , pp. 610-638
    • Hirokawa, N.1    Niwa, S.2    Tanaka, Y.3
  • 15
    • 0005312677 scopus 로고
    • Molecular cloning of cDNA coding for brain-specific 14-3-3 protein, a protein kinase-dependent activator of tyrosine and tryptophan hydroxylases
    • Ichimura T., Isobe T., Okuyama T., Takahashi N., Araki K., Kuwano R., Takahashi Y. Molecular cloning of cDNA coding for brain-specific 14-3-3 protein, a protein kinase-dependent activator of tyrosine and tryptophan hydroxylases. Proc. Natl. Acad. Sci. USA 1988, 85:7084-7088.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7084-7088
    • Ichimura, T.1    Isobe, T.2    Okuyama, T.3    Takahashi, N.4    Araki, K.5    Kuwano, R.6    Takahashi, Y.7
  • 16
    • 77951437255 scopus 로고    scopus 로고
    • Branching out: mechanisms of dendritic arborization
    • Jan Y.N., Jan L.Y. Branching out: mechanisms of dendritic arborization. Nat. Rev. Neurosci. 2010, 11:316-328.
    • (2010) Nat. Rev. Neurosci. , vol.11 , pp. 316-328
    • Jan, Y.N.1    Jan, L.Y.2
  • 17
    • 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
  • 18
    • 78650884653 scopus 로고    scopus 로고
    • Which way to go? Cytoskeletal organization and polarized transport in neurons
    • Kapitein L.C., Hoogenraad C.C. Which way to go? Cytoskeletal organization and polarized transport in neurons. Mol. Cell. Neurosci. 2011, 46:9-20.
    • (2011) Mol. Cell. Neurosci. , vol.46 , pp. 9-20
    • Kapitein, L.C.1    Hoogenraad, C.C.2
  • 20
    • 0033797735 scopus 로고    scopus 로고
    • Dendritic anomalies in disorders associated with mental retardation
    • Kaufmann W.E., Moser H.W. Dendritic anomalies in disorders associated with mental retardation. Cereb. Cortex 2000, 10:981-991.
    • (2000) Cereb. Cortex , vol.10 , pp. 981-991
    • Kaufmann, W.E.1    Moser, H.W.2
  • 21
    • 5044224260 scopus 로고    scopus 로고
    • PDZ domain proteins of synapses
    • Kim E., Sheng M. PDZ domain proteins of synapses. Nat. Rev. Neurosci. 2004, 5:771-781.
    • (2004) Nat. Rev. Neurosci. , vol.5 , pp. 771-781
    • Kim, E.1    Sheng, M.2
  • 22
    • 37549002521 scopus 로고    scopus 로고
    • Supramodular nature of GRIP1 revealed by the structure of its PDZ12 tandem in complex with the carboxyl tail of Fras1
    • Long J., Wei Z., Feng W., Yu C., Zhao Y.X., Zhang M. Supramodular nature of GRIP1 revealed by the structure of its PDZ12 tandem in complex with the carboxyl tail of Fras1. J.Mol. Biol. 2008, 375:1457-1468.
    • (2008) J.Mol. Biol. , vol.375 , pp. 1457-1468
    • Long, J.1    Wei, Z.2    Feng, W.3    Yu, C.4    Zhao, Y.X.5    Zhang, M.6
  • 23
    • 23044457365 scopus 로고    scopus 로고
    • PICK1 interacts with ABP/GRIP to regulate AMPA receptor trafficking
    • Lu W., Ziff E.B. PICK1 interacts with ABP/GRIP to regulate AMPA receptor trafficking. Neuron 2005, 47:407-421.
    • (2005) Neuron , vol.47 , pp. 407-421
    • Lu, W.1    Ziff, E.B.2
  • 25
    • 3242788127 scopus 로고    scopus 로고
    • Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes
    • Mackintosh C. Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes. Biochem. J. 2004, 381:329-342.
    • (2004) Biochem. J. , vol.381 , pp. 329-342
    • Mackintosh, C.1
  • 26
    • 0033586783 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with a nonphosphorylated protein ligand, exoenzyme S of Pseudomonas aeruginosa
    • Masters S.C., Pederson K.J., Zhang L., Barbieri J.T., Fu H. Interaction of 14-3-3 with a nonphosphorylated protein ligand, exoenzyme S of Pseudomonas aeruginosa. Biochemistry 1999, 38:5216-5221.
    • (1999) Biochemistry , vol.38 , pp. 5216-5221
    • Masters, S.C.1    Pederson, K.J.2    Zhang, L.3    Barbieri, J.T.4    Fu, H.5
  • 27
    • 1942470024 scopus 로고    scopus 로고
    • Design and validation of a tool for neurite tracing and analysis in fluorescence microscopy images
    • Meijering E., Jacob M., Sarria J.C., Steiner P., Hirling H., Unser M. Design and validation of a tool for neurite tracing and analysis in fluorescence microscopy images. Cytometry A 2004, 58:167-176.
    • (2004) Cytometry A , vol.58 , pp. 167-176
    • Meijering, E.1    Jacob, M.2    Sarria, J.C.3    Steiner, P.4    Hirling, H.5    Unser, M.6
  • 28
    • 84875443717 scopus 로고    scopus 로고
    • Axonal transport deficits and neurodegenerative diseases
    • Millecamps S., Julien J.P. Axonal transport deficits and neurodegenerative diseases. Nat. Rev. Neurosci. 2013, 14:161-176.
    • (2013) Nat. Rev. Neurosci. , vol.14 , pp. 161-176
    • Millecamps, S.1    Julien, J.P.2
  • 29
    • 77649236954 scopus 로고    scopus 로고
    • Regulation of synaptic structure and function by palmitoylated AMPA receptor binding protein
    • Misra C., Restituito S., Ferreira J., Rameau G.A., Fu J., Ziff E.B. Regulation of synaptic structure and function by palmitoylated AMPA receptor binding protein. Mol. Cell. Neurosci. 2010, 43:341-352.
    • (2010) Mol. Cell. Neurosci. , vol.43 , pp. 341-352
    • Misra, C.1    Restituito, S.2    Ferreira, J.3    Rameau, G.A.4    Fu, J.5    Ziff, E.B.6
  • 30
    • 0029871708 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine
    • Muslin A.J., Tanner J.W., Allen P.M., Shaw A.S. Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell 1996, 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
  • 31
    • 84863488995 scopus 로고    scopus 로고
    • Regulation of AMPA receptor surface diffusion by PSD-95 slots
    • Opazo P., Sainlos M., Choquet D. Regulation of AMPA receptor surface diffusion by PSD-95 slots. Curr. Opin. Neurobiol. 2012, 22:453-460.
    • (2012) Curr. Opin. Neurobiol. , vol.22 , pp. 453-460
    • Opazo, P.1    Sainlos, M.2    Choquet, D.3
  • 34
    • 69449091821 scopus 로고    scopus 로고
    • Basic mechanisms for recognition and transport of synaptic cargos
    • Schlager M.A., Hoogenraad C.C. Basic mechanisms for recognition and transport of synaptic cargos. Mol. Brain 2009, 2:25.
    • (2009) Mol. Brain , vol.2 , pp. 25
    • Schlager, M.A.1    Hoogenraad, C.C.2
  • 35
    • 33847196732 scopus 로고    scopus 로고
    • Grb4 and GIT1 transduce ephrinB reverse signals modulating spine morphogenesis and synapse formation
    • Segura I., Essmann C.L., Weinges S., Acker-Palmer A. Grb4 and GIT1 transduce ephrinB reverse signals modulating spine morphogenesis and synapse formation. Nat. Neurosci. 2007, 10:301-310.
    • (2007) Nat. Neurosci. , vol.10 , pp. 301-310
    • Segura, I.1    Essmann, C.L.2    Weinges, S.3    Acker-Palmer, A.4
  • 36
    • 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 2000, 288:1796-1802.
    • (2000) Science , vol.288 , pp. 1796-1802
    • Setou, M.1    Nakagawa, T.2    Seog, D.H.3    Hirokawa, N.4
  • 37
    • 0037007668 scopus 로고    scopus 로고
    • Glutamate-receptor-interacting protein GRIP1 directly steers kinesin to dendrites
    • Setou M., Seog D.H., Tanaka Y., Kanai Y., Takei Y., Kawagishi M., Hirokawa N. Glutamate-receptor-interacting protein GRIP1 directly steers kinesin to dendrites. Nature 2002, 417:83-87.
    • (2002) Nature , vol.417 , pp. 83-87
    • Setou, M.1    Seog, D.H.2    Tanaka, Y.3    Kanai, Y.4    Takei, Y.5    Kawagishi, M.6    Hirokawa, N.7
  • 38
    • 34548436564 scopus 로고    scopus 로고
    • The postsynaptic architecture of excitatory synapses: a more quantitative view
    • Sheng M., Hoogenraad C.C. The postsynaptic architecture of excitatory synapses: a more quantitative view. Annu. Rev. Biochem. 2007, 76:823-847.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 823-847
    • Sheng, M.1    Hoogenraad, C.C.2
  • 39
    • 38149016966 scopus 로고    scopus 로고
    • The cell biology of synaptic plasticity: AMPA receptor trafficking
    • Shepherd J.D., Huganir R.L. The cell biology of synaptic plasticity: AMPA receptor trafficking. Annu. Rev. Cell Dev. Biol. 2007, 23:613-643.
    • (2007) Annu. Rev. Cell Dev. Biol. , vol.23 , pp. 613-643
    • Shepherd, J.D.1    Huganir, R.L.2
  • 43
    • 84863012668 scopus 로고    scopus 로고
    • Palmitoylation by DHHC5/8 targets GRIP1 to dendritic endosomes to regulate AMPA-R trafficking
    • Thomas G.M., Hayashi T., Chiu S.L., Chen C.M., Huganir R.L. Palmitoylation by DHHC5/8 targets GRIP1 to dendritic endosomes to regulate AMPA-R trafficking. Neuron 2012, 73:482-496.
    • (2012) Neuron , vol.73 , pp. 482-496
    • Thomas, G.M.1    Hayashi, T.2    Chiu, S.L.3    Chen, C.M.4    Huganir, R.L.5
  • 47
    • 34347242492 scopus 로고    scopus 로고
    • More than just synaptic building blocks: scaffolding proteins of the post-synaptic density regulate dendritic patterning
    • Vessey J.P., Karra D. More than just synaptic building blocks: scaffolding proteins of the post-synaptic density regulate dendritic patterning. J.Neurochem. 2007, 102:324-332.
    • (2007) J.Neurochem. , vol.102 , pp. 324-332
    • Vessey, J.P.1    Karra, D.2
  • 48
    • 0033592326 scopus 로고    scopus 로고
    • Isolation of high-affinity peptide antagonists of 14-3-3 proteins by phage display
    • Wang B., Yang H., Liu Y.C., Jelinek T., Zhang L., Ruoslahti E., Fu H. Isolation of high-affinity peptide antagonists of 14-3-3 proteins by phage display. Biochemistry 1999, 38:12499-12504.
    • (1999) Biochemistry , vol.38 , pp. 12499-12504
    • Wang, B.1    Yang, H.2    Liu, Y.C.3    Jelinek, T.4    Zhang, L.5    Ruoslahti, E.6    Fu, H.7
  • 49
    • 0036779579 scopus 로고    scopus 로고
    • Activity-dependent regulation of dendritic growth and patterning
    • Wong R.O., Ghosh A. Activity-dependent regulation of dendritic growth and patterning. Nat. Rev. Neurosci. 2002, 3:803-812.
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 803-812
    • Wong, R.O.1    Ghosh, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.