메뉴 건너뛰기




Volumn 196, Issue 1, 2012, Pages 85-101

RAB-6.2 and the retromer regulate glutamate receptor recycling through a retrograde pathway

Author keywords

[No Author keywords available]

Indexed keywords

AMPA RECEPTOR; GLUTAMATE RECEPTOR; GLUTAMATE RECEPTOR 1; MEMBRANE PROTEIN; PDZ PROTEIN; PROTEIN LIN 10; PROTEIN TYROSINE PHOSPHATASE; RAB 6.2 PROTEIN; RAB PROTEIN; RME 8 PROTEIN; SNX 1 PROTEIN; SORTING NEXIN; UNCLASSIFIED DRUG; VPS 35 PROTEIN;

EID: 84863012293     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201104141     Document Type: Article
Times cited : (49)

References (83)
  • 2
    • 2442530398 scopus 로고    scopus 로고
    • Role of the mammalian retromer in sorting of the cation-independent mannose 6-phosphate receptor
    • Arighi, C.N., L.M. Hartnell, R.C. Aguilar, C.R. Haft, and J.S. Bonifacino. 2004. Role of the mammalian retromer in sorting of the cation-independent mannose 6-phosphate receptor. J. Cell Biol. 165:123-133. http://dx.doi.org/10.1083/jcb.200312055
    • (2004) J. Cell Biol. , vol.165 , pp. 123-133
    • Arighi, C.N.1    Hartnell, L.M.2    Aguilar, R.C.3    Haft, C.R.4    Bonifacino, J.S.5
  • 3
    • 0036697166 scopus 로고    scopus 로고
    • Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body
    • Babst, M., D.J. Katzmann, W.B. Snyder, B. Wendland, and S.D. Emr. 2002. Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body. Dev. Cell. 3:283-289.http://dx.doi.org/10.1016/S1534-5807(02)00219-8
    • (2002) Dev. Cell. , vol.3 , pp. 283-289
    • Babst, M.1    Katzmann, D.J.2    Snyder, W.B.3    Wendland, B.4    Emr, S.D.5
  • 5
    • 33748313351 scopus 로고    scopus 로고
    • Retrograde transport from endosomes to the trans-Golgi network
    • Bonifacino, J.S., and R. Rojas. 2006. Retrograde transport from endosomes to the trans-Golgi network. Nat. Rev. Mol. Cell Biol. 7:568-579. http://dx.doi.org/10.1038/nrm1985
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 568-579
    • Bonifacino, J.S.1    Rojas, R.2
  • 6
    • 78650245035 scopus 로고    scopus 로고
    • In a pickle: is cornichon just relish or part of the main dish?
    • Brockie, P.J., and A.V. Maricq. 2010. In a pickle: is cornichon just relish or part of the main dish? Neuron. 68:1017-1019. http://dx.doi.org/10.1016/j.neuron.2010.12.013
    • (2010) Neuron , vol.68 , pp. 1017-1019
    • Brockie, P.J.1    Maricq, A.V.2
  • 7
    • 0037014445 scopus 로고    scopus 로고
    • Ubiquitin and AP180 regulate the abundance of GLR-1 glutamate receptors at postsynaptic elements in C. elegans
    • Burbea, M., L. Dreier, J.S. Dittman, M.E. Grunwald, and J.M. Kaplan. 2002. Ubiquitin and AP180 regulate the abundance of GLR-1 glutamate receptors at postsynaptic elements in C. elegans. Neuron. 35:107-120. http://dx.doi.org/10.1016/S0896-6273(02)00749-3
    • (2002) Neuron , vol.35 , pp. 107-120
    • Burbea, M.1    Dreier, L.2    Dittman, J.S.3    Grunwald, M.E.4    Kaplan, J.M.5
  • 8
    • 6944255481 scopus 로고    scopus 로고
    • Sorting nexin-1 mediates tubular endosome-to-TGN transport through coincidence sensing of high- curvature membranes and 3-phosphoinositides
    • Carlton, J., M. Bujny, B.J. Peter, V.M. Oorschot, A. Rutherford, H. Mellor, J. Klumperman, H.T. McMahon, and P.J. Cullen. 2004. Sorting nexin-1 mediates tubular endosome-to-TGN transport through coincidence sensing of high- curvature membranes and 3-phosphoinositides. Curr. Biol. 14:1791-1800. http://dx.doi.org/10.1016/j.cub.2004.09.077
    • (2004) Curr. Biol. , vol.14 , pp. 1791-1800
    • Carlton, J.1    Bujny, M.2    Peter, B.J.3    Oorschot, V.M.4    Rutherford, A.5    Mellor, H.6    Klumperman, J.7    McMahon, H.T.8    Cullen, P.J.9
  • 9
    • 19444375713 scopus 로고    scopus 로고
    • Cytosolic tail sequences and subunit interactions are critical for synaptic localization of glutamate receptors
    • Chang, H.C., and C. Rongo. 2005. Cytosolic tail sequences and subunit interactions are critical for synaptic localization of glutamate receptors. J. Cell Sci. 118:1945-1956. http://dx.doi.org/10.1242/jcs.02320
    • (2005) J. Cell Sci. , vol.118 , pp. 1945-1956
    • Chang, H.C.1    Rongo, C.2
  • 10
    • 51349154176 scopus 로고    scopus 로고
    • UNC-108/Rab2 regulates postendocytic trafficking in Caenorhabditis elegans
    • Chun, D.K., J.M. McEwen, M. Burbea, and J.M. Kaplan. 2008. UNC-108/Rab2 regulates postendocytic trafficking in Caenorhabditis elegans. Mol. Biol. Cell. 19:2682-2695. http://dx.doi.org/10.1091/mbc.E07-11-1120
    • (2008) Mol. Biol. Cell. , vol.19 , pp. 2682-2695
    • Chun, D.K.1    McEwen, J.M.2    Burbea, M.3    Kaplan, J.M.4
  • 11
    • 0034307444 scopus 로고    scopus 로고
    • Phosphorylation of the AMPA receptor subunit GluR2 differentially regulates its interaction with PDZ domain-containing proteins
    • Chung, H.J., J. Xia, R.H. Scannevin, X. Zhang, and R.L. Huganir. 2000. Phosphorylation of the AMPA receptor subunit GluR2 differentially regulates its interaction with PDZ domain-containing proteins. J. Neurosci. 20:7258-7267.
    • (2000) J. Neurosci. , vol.20 , pp. 7258-7267
    • Chung, H.J.1    Xia, J.2    Scannevin, R.H.3    Zhang, X.4    Huganir, R.L.5
  • 12
    • 33644870151 scopus 로고    scopus 로고
    • Rab6A and Rab6A' GTPases play non-overlapping roles in membrane trafficking
    • Del Nery, E., S. Miserey-Lenkei, T. Falguières, C. Nizak, L. Johannes, F. Perez, and B. Goud. 2006. Rab6A and Rab6A' GTPases play non-overlapping roles in membrane trafficking. Traffic. 7:394-407. http://dx.doi.org/10.1111/j.1600-0854.2006.00395.x
    • (2006) Traffic , vol.7 , pp. 394-407
    • Del Nery, E.1    Miserey-Lenkei, S.2    Falguières, T.3    Nizak, C.4    Johannes, L.5    Perez, F.6    Goud, B.7
  • 13
    • 77958153797 scopus 로고    scopus 로고
    • Regulation of AMPA receptors by transmembrane accessory proteins
    • Díaz, E. 2010. Regulation of AMPA receptors by transmembrane accessory proteins. Eur. J. Neurosci. 32:261-268. http://dx.doi.org/10.1111/j.1460-9568.2010.07357.x
    • (2010) Eur. J. Neurosci. , vol.32 , pp. 261-268
    • Díaz, E.1
  • 15
    • 84864286265 scopus 로고    scopus 로고
    • MAGI-1 modulates AMPA receptor synaptic localization and behavioral plasticity in response to prior experience
    • Emtage, L., H. Chang, R. Tiver, and C. Rongo. 2009. MAGI-1 modulates AMPA receptor synaptic localization and behavioral plasticity in response to prior experience. PLoS ONE. 4:e4613. http://dx.doi.org/10.1371/journal.pone.0004613
    • (2009) PLoS ONE , vol.4
    • Emtage, L.1    Chang, H.2    Tiver, R.3    Rongo, C.4
  • 16
    • 0037312605 scopus 로고    scopus 로고
    • PKA phosphorylation of AMPA receptor subunits controls synaptic trafficking underlying plasticity
    • Esteban, J.A., S.H. Shi, C. Wilson, M. Nuriya, R.L. Huganir, and R. Malinow. 2003. PKA phosphorylation of AMPA receptor subunits controls synaptic trafficking underlying plasticity. Nat. Neurosci. 6:136-143. http://dx.doi.org/10.1038/nn997
    • (2003) Nat. Neurosci. , vol.6 , pp. 136-143
    • Esteban, J.A.1    Shi, S.H.2    Wilson, C.3    Nuriya, M.4    Huganir, R.L.5    Malinow, R.6
  • 17
    • 6344237504 scopus 로고    scopus 로고
    • Local control of AMPA receptor trafficking at the postsynaptic terminal by a small GTPase of the Rab family
    • Gerges, N.Z., D.S. Backos, and J.A. Esteban. 2004. Local control of AMPA receptor trafficking at the postsynaptic terminal by a small GTPase of the Rab family. J. Biol. Chem. 279:43870-43878. http://dx.doi.org/10.1074/jbc.M404982200
    • (2004) J. Biol. Chem. , vol.279 , pp. 43870-43878
    • Gerges, N.Z.1    Backos, D.S.2    Esteban, J.A.3
  • 18
    • 14844297363 scopus 로고    scopus 로고
    • Distinct LIN-10 domains are required for its neuronal function, its epithelial function, and its synaptic localization
    • Glodowski, D.R., T. Wright, K. Martinowich, H.C. Chang, D. Beach, and C. Rongo. 2005. Distinct LIN-10 domains are required for its neuronal function, its epithelial function, and its synaptic localization. Mol. Biol. Cell. 16:1417-1426. http://dx.doi.org/10.1091/mbc.E04-10-0885
    • (2005) Mol. Biol. Cell. , vol.16 , pp. 1417-1426
    • Glodowski, D.R.1    Wright, T.2    Martinowich, K.3    Chang, H.C.4    Beach, D.5    Rongo, C.6
  • 19
    • 35848951167 scopus 로고    scopus 로고
    • RAB-10 regulates glutamate receptor recycling in a cholesterol-dependent endocytosis pathway
    • Glodowski, D.R., C.C. Chen, H. Schaefer, B.D. Grant, and C. Rongo. 2007. RAB-10 regulates glutamate receptor recycling in a cholesterol-dependent endocytosis pathway. Mol. Biol. Cell. 18:4387-4396. http://dx.doi.org/10.1091/mbc.E07-05-0486
    • (2007) Mol. Biol. Cell. , vol.18 , pp. 4387-4396
    • Glodowski, D.R.1    Chen, C.C.2    Schaefer, H.3    Grant, B.D.4    Rongo, C.5
  • 20
    • 38449103028 scopus 로고    scopus 로고
    • Intracellular trafficking
    • Grant, B.D., and M. Sato. 2006. Intracellular trafficking. WormBook.:1-9.
    • (2006) WormBook , pp. 1-9
    • Grant, B.D.1    Sato, M.2
  • 21
    • 1542297719 scopus 로고    scopus 로고
    • Clathrin-mediated endocytosis is required for compensatory regulation of GLR-1 glutamate receptors after activity blockade
    • Grunwald, M.E., J.E. Mellem, N. Strutz, A.V. Maricq, and J.M. Kaplan. 2004. Clathrin-mediated endocytosis is required for compensatory regulation of GLR-1 glutamate receptors after activity blockade. Proc. Natl. Acad. Sci. USA. 101:3190-3195. http://dx.doi.org/10.1073/pnas.0306156101
    • (2004) Proc. Natl. Acad. Sci. USA. , vol.101 , pp. 3190-3195
    • Grunwald, M.E.1    Mellem, J.E.2    Strutz, N.3    Maricq, A.V.4    Kaplan, J.M.5
  • 22
    • 77953241394 scopus 로고    scopus 로고
    • Endosomal sorting of AMPA receptors in hippocampal neurons
    • Hanley, J.G. 2010. Endosomal sorting of AMPA receptors in hippocampal neurons. Biochem. Soc. Trans. 38:460-465. http://dx.doi.org/10.1042/BST0380460
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 460-465
    • Hanley, J.G.1
  • 23
    • 0028867824 scopus 로고
    • Synaptic code for sensory modalities revealed by C. elegans GLR-1 glutamate receptor
    • Hart, A.C., S. Sims, and J.M. Kaplan. 1995. Synaptic code for sensory modalities revealed by C. elegans GLR-1 glutamate receptor. Nature. 378:82-85. http://dx.doi.org/10.1038/378082a0
    • (1995) Nature , vol.378 , pp. 82-85
    • Hart, A.C.1    Sims, S.2    Kaplan, J.M.3
  • 24
    • 0034708587 scopus 로고    scopus 로고
    • Driving AMPA receptors into synapses by LTP and CaMKII: requirement for GluR1 and PDZ domain interaction
    • Hayashi, Y., S.H. Shi, J.A. Esteban, A. Piccini, J.C. Poncer, and R. Malinow. 2000. Driving AMPA receptors into synapses by LTP and CaMKII: requirement for GluR1 and PDZ domain interaction. Science. 287:2262-2267. http://dx.doi.org/10.1126/science.287.5461.2262
    • (2000) Science , vol.287 , pp. 2262-2267
    • Hayashi, Y.1    Shi, S.H.2    Esteban, J.A.3    Piccini, A.4    Poncer, J.C.5    Malinow, R.6
  • 25
    • 15744380393 scopus 로고    scopus 로고
    • GGA proteins mediate the recycling pathway of memapsin 2 (BACE)
    • He, X., F. Li, W.P. Chang, and J. Tang. 2005. GGA proteins mediate the recycling pathway of memapsin 2 (BACE). J. Biol. Chem. 280:11696-11703.http://dx.doi.org/10.1074/jbc.M411296200
    • (2005) J. Biol. Chem. , vol.280 , pp. 11696-11703
    • He, X.1    Li, F.2    Chang, W.P.3    Tang, J.4
  • 26
    • 79955715308 scopus 로고    scopus 로고
    • Routes, destinations and delays: recent advances in AMPA receptor trafficking
    • Henley, J.M., E.A. Barker, and O.O. Glebov. 2011. Routes, destinations and delays: recent advances in AMPA receptor trafficking. Trends Neurosci. 34:258-268. http://dx.doi.org/10.1016/j.tins.2011.02.004
    • (2011) Trends Neurosci , vol.34 , pp. 258-268
    • Henley, J.M.1    Barker, E.A.2    Glebov, O.O.3
  • 27
    • 0141481046 scopus 로고    scopus 로고
    • Munc18 interacting proteins: ADPribosylation factor-dependent coat proteins that regulate the traffic of beta-Alzheimer's precursor protein
    • Hill, K., Y. Li, M. Bennett, M. McKay, X. Zhu, J. Shern, E. Torre, J.J. Lah, A.I. Levey, and R.A. Kahn. 2003. Munc18 interacting proteins: ADPribosylation factor-dependent coat proteins that regulate the traffic of beta-Alzheimer's precursor protein. J. Biol. Chem. 278:36032-36040. http://dx.doi.org/10.1074/jbc.M301632200
    • (2003) J. Biol. Chem. , vol.278 , pp. 36032-36040
    • Hill, K.1    Li, Y.2    Bennett, M.3    McKay, M.4    Zhu, X.5    Shern, J.6    Torre, E.7    Lah, J.J.8    Levey, A.I.9    Kahn, R.A.10
  • 28
    • 58149400148 scopus 로고    scopus 로고
    • Deletion of Mint proteins decreases amyloid production in transgenic mouse models of Alzheimer's disease
    • Ho, A., X. Liu, and T.C. Südhof. 2008. Deletion of Mint proteins decreases amyloid production in transgenic mouse models of Alzheimer's disease. J. Neurosci. 28:14392-14400. http://dx.doi.org/10.1523/JNEUROSCI.2481-08.2008
    • (2008) J. Neurosci. , vol.28 , pp. 14392-14400
    • Ho, A.1    Liu, X.2    Südhof, T.C.3
  • 29
    • 33748423078 scopus 로고    scopus 로고
    • AtSNX1 defines an endosome for auxin-carrier trafficking in Arabidopsis
    • Jaillais, Y., I. Fobis-Loisy, C. Miège, C. Rollin, and T. Gaude. 2006. AtSNX1 defines an endosome for auxin-carrier trafficking in Arabidopsis. Nature. 443:106-109. http://dx.doi.org/10.1038/nature05046
    • (2006) Nature , vol.443 , pp. 106-109
    • Jaillais, Y.1    Fobis-Loisy, I.2    Miège, C.3    Rollin, C.4    Gaude, T.5
  • 30
    • 34548704766 scopus 로고    scopus 로고
    • The retromer protein VPS29 links cell polarity and organ initiation in plants
    • Jaillais, Y., M. Santambrogio, F. Rozier, I. Fobis-Loisy, C. Miège, and T. Gaude. 2007. The retromer protein VPS29 links cell polarity and organ initiation in plants. Cell. 130:1057-1070. http://dx.doi.org/10.1016/j.cell.2007.08.040
    • (2007) Cell , vol.130 , pp. 1057-1070
    • Jaillais, Y.1    Santambrogio, M.2    Rozier, F.3    Fobis-Loisy, I.4    Miège, C.5    Gaude, T.6
  • 32
    • 57749196733 scopus 로고    scopus 로고
    • Tracing the retrograde route in protein trafficking
    • Johannes, L., and V. Popoff. 2008. Tracing the retrograde route in protein trafficking. Cell. 135:1175-1187. http://dx.doi.org/10.1016/j.cell.2008.12.009
    • (2008) Cell , vol.135 , pp. 1175-1187
    • Johannes, L.1    Popoff, V.2
  • 34
    • 59649114125 scopus 로고    scopus 로고
    • Synaptic AMPA receptor plasticity and behavior
    • Kessels, H.W., and R. Malinow. 2009. Synaptic AMPA receptor plasticity and behavior. Neuron. 61:340-350. http://dx.doi.org/10.1016/j.neuron.2009.01.015
    • (2009) Neuron , vol.61 , pp. 340-350
    • Kessels, H.W.1    Malinow, R.2
  • 35
    • 0344012486 scopus 로고    scopus 로고
    • The neuronal adaptor protein X11alpha reduces Abeta levels in the brains of Alzheimer's APPswe Tg2576 transgenic mice
    • Lee, J.H., K.F. Lau, M.S. Perkinton, C.L. Standen, S.J. Shemilt, L. Mercken, J.D. Cooper, D.M. McLoughlin, and C.C. Miller. 2003. The neuronal adaptor protein X11alpha reduces Abeta levels in the brains of Alzheimer's APPswe Tg2576 transgenic mice. J. Biol. Chem. 278:47025-47029.http://dx.doi.org/10.1074/jbc.M300503200
    • (2003) J. Biol. Chem. , vol.278 , pp. 47025-47029
    • Lee, J.H.1    Lau, K.F.2    Perkinton, M.S.3    Standen, C.L.4    Shemilt, S.J.5    Mercken, L.6    Cooper, J.D.7    McLoughlin, D.M.8    Miller, C.C.9
  • 36
    • 79952335924 scopus 로고    scopus 로고
    • Endosome-to-Golgi transport pathways in physiological processes
    • Lieu, Z.Z., and P.A. Gleeson. 2011. Endosome-to-Golgi transport pathways in physiological processes. Histol. Histopathol. 26:395-408.
    • (2011) Histol. Histopathol. , vol.26 , pp. 395-408
    • Lieu, Z.Z.1    Gleeson, P.A.2
  • 37
    • 23044457365 scopus 로고    scopus 로고
    • PICK1 interacts with ABP/GRIP to regulate AMPA receptor trafficking
    • Lu, W., and E.B. Ziff. 2005. PICK1 interacts with ABP/GRIP to regulate AMPA receptor trafficking. Neuron. 47:407-421. http://dx.doi.org/10.1016/j.neuron.2005.07.006
    • (2005) Neuron , vol.47 , pp. 407-421
    • Lu, W.1    Ziff, E.B.2
  • 38
    • 70350752569 scopus 로고    scopus 로고
    • AMPA receptor incorporation into synapses during LTP: the role of lateral movement and exocytosis
    • Makino, H., and R. Malinow. 2009. AMPA receptor incorporation into synapses during LTP: the role of lateral movement and exocytosis. Neuron. 64:381-390. http://dx.doi.org/10.1016/j.neuron.2009.08.035
    • (2009) Neuron , vol.64 , pp. 381-390
    • Makino, H.1    Malinow, R.2
  • 40
    • 0028837546 scopus 로고
    • Mechanosensory signalling in C. elegans mediated by the GLR-1 glutamate receptor
    • Maricq, A.V., E. Peckol, M. Driscoll, and C.I. Bargmann. 1995. Mechanosensory signalling in C. elegans mediated by the GLR-1 glutamate receptor. Nature. 378:78-81. http://dx.doi.org/10.1038/378078a0
    • (1995) Nature , vol.378 , pp. 78-81
    • Maricq, A.V.1    Peckol, E.2    Driscoll, M.3    Bargmann, C.I.4
  • 41
    • 0037028037 scopus 로고    scopus 로고
    • Decoding of polymodal sensory stimuli by postsynaptic glutamate receptors in C. elegans
    • Mellem, J.E., P.J. Brockie, Y. Zheng, D.M. Madsen, and A.V. Maricq. 2002. Decoding of polymodal sensory stimuli by postsynaptic glutamate receptors in C. elegans. Neuron. 36:933-944. http://dx.doi.org/10.1016/S0896-6273(02)01088-7
    • (2002) Neuron , vol.36 , pp. 933-944
    • Mellem, J.E.1    Brockie, P.J.2    Zheng, Y.3    Madsen, D.M.4    Maricq, A.V.5
  • 42
    • 0034671933 scopus 로고    scopus 로고
    • Modulation of amyloid precursor protein metabolism by X11alpha /Mint-1. A deletion analysis of protein-protein interaction domains
    • Mueller, H.T., J.P. Borg, B. Margolis, and R.S. Turner. 2000. Modulation of amyloid precursor protein metabolism by X11alpha /Mint-1. A deletion analysis of protein-protein interaction domains. J. Biol. Chem. 275: 39302-39306. http://dx.doi.org/10.1074/jbc.M008453200
    • (2000) J. Biol. Chem. , vol.275 , pp. 39302-39306
    • Mueller, H.T.1    Borg, J.P.2    Margolis, B.3    Turner, R.S.4
  • 44
    • 0031975266 scopus 로고    scopus 로고
    • Synaptic transmission deficits in Caenorhabditis elegans synaptobrevin mutants
    • Nonet, M.L., O. Saifee, H. Zhao, J.B. Rand, and L. Wei. 1998. Synaptic transmission deficits in Caenorhabditis elegans synaptobrevin mutants. J. Neurosci. 18:70-80.
    • (1998) J. Neurosci. , vol.18 , pp. 70-80
    • Nonet, M.L.1    Saifee, O.2    Zhao, H.3    Rand, J.B.4    Wei, L.5
  • 46
    • 32544435097 scopus 로고    scopus 로고
    • The lipoprotein receptor LR11 regulates amyloid beta production and amyloid precursor protein traffic in endosomal compartments
    • Offe, K., S.E. Dodson, J.T. Shoemaker, J.J. Fritz, M. Gearing, A.I. Levey, and J.J. Lah. 2006. The lipoprotein receptor LR11 regulates amyloid beta production and amyloid precursor protein traffic in endosomal compartments. J. Neurosci. 26:1596-1603. http://dx.doi.org/10.1523/JNEUROSCI.4946-05.2006
    • (2006) J. Neurosci. , vol.26 , pp. 1596-1603
    • Offe, K.1    Dodson, S.E.2    Shoemaker, J.T.3    Fritz, J.J.4    Gearing, M.5    Levey, A.I.6    Lah, J.J.7
  • 47
    • 37749052695 scopus 로고    scopus 로고
    • C. elegans AP-2 and retromer control Wnt signaling by regulating mig-14/Wntless
    • Pan, C.L., P.D. Baum, M. Gu, E.M. Jorgensen, S.G. Clark, and G. Garriga. 2008. C. elegans AP-2 and retromer control Wnt signaling by regulating mig-14/Wntless. Dev. Cell. 14:132-139. http://dx.doi.org/10.1016/j.devcel.2007.12.001
    • (2008) Dev. Cell. , vol.14 , pp. 132-139
    • Pan, C.L.1    Baum, P.D.2    Gu, M.3    Jorgensen, E.M.4    Clark, S.G.5    Garriga, G.6
  • 48
    • 73349097586 scopus 로고    scopus 로고
    • AMPH-1/Amphiphysin/Bin1 functions with RME-1/Ehd1 in endocytic recycling
    • Pant, S., M. Sharma, K. Patel, S. Caplan, C.M. Carr, and B.D. Grant. 2009. AMPH-1/Amphiphysin/Bin1 functions with RME-1/Ehd1 in endocytic recycling. Nat. Cell Biol. 11:1399-1410. http://dx.doi.org/10.1038/ncb1986
    • (2009) Nat. Cell Biol. , vol.11 , pp. 1399-1410
    • Pant, S.1    Sharma, M.2    Patel, K.3    Caplan, S.4    Carr, C.M.5    Grant, B.D.6
  • 49
    • 59349099346 scopus 로고    scopus 로고
    • The ubiquitin ligase RPM-1 and the p38 MAPK PMK-3 regulate AMPA receptor trafficking
    • Park, E.C., D.R. Glodowski, and C. Rongo. 2009. The ubiquitin ligase RPM-1 and the p38 MAPK PMK-3 regulate AMPA receptor trafficking. PLoS ONE. 4:e4284. http://dx.doi.org/10.1371/journal.pone.0004284
    • (2009) PLoS ONE , vol.4
    • Park, E.C.1    Glodowski, D.R.2    Rongo, C.3
  • 50
    • 4644287672 scopus 로고    scopus 로고
    • Recycling endosomes supply AMPA receptors for LTP
    • Park, M., E.C. Penick, J.G. Edwards, J.A. Kauer, and M.D. Ehlers. 2004. Recycling endosomes supply AMPA receptors for LTP. Science. 305: 1972-1975. http://dx.doi.org/10.1126/science.1102026
    • (2004) Science , vol.305 , pp. 1972-1975
    • Park, M.1    Penick, E.C.2    Edwards, J.G.3    Kauer, J.A.4    Ehlers, M.D.5
  • 51
    • 0034869177 scopus 로고    scopus 로고
    • Subunit-specific temporal and spatial patterns of AMPA receptor exocytosis in hippocampal neurons
    • Passafaro, M., V. Piëch, and M. Sheng. 2001. Subunit-specific temporal and spatial patterns of AMPA receptor exocytosis in hippocampal neurons. Nat. Neurosci. 4:917-926. http://dx.doi.org/10.1038/nn0901-917
    • (2001) Nat. Neurosci. , vol.4 , pp. 917-926
    • Passafaro, M.1    Piëch, V.2    Sheng, M.3
  • 52
    • 42949140333 scopus 로고    scopus 로고
    • The role of transmembrane AMPA receptor regulatory proteins (TARPs) in neurotransmission and receptor trafficking (Review)
    • Payne, H.L. 2008. The role of transmembrane AMPA receptor regulatory proteins (TARPs) in neurotransmission and receptor trafficking (Review). Mol. Membr. Biol. 25:353-362. http://dx.doi.org/10.1080/09687680801986480
    • (2008) Mol. Membr. Biol. , vol.25 , pp. 353-362
    • Payne, H.L.1
  • 53
    • 0032837679 scopus 로고    scopus 로고
    • The Menkes protein (ATP7A; MNK) cycles via the plasma membrane both in basal and elevated extracellular copper using a C-terminal di-leucine endocytic signal
    • Petris, M.J., and J.F. Mercer. 1999. The Menkes protein (ATP7A; MNK) cycles via the plasma membrane both in basal and elevated extracellular copper using a C-terminal di-leucine endocytic signal. Hum. Mol. Genet. 8:2107-2115. http://dx.doi.org/10.1093/hmg/8.11.2107
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 2107-2115
    • Petris, M.J.1    Mercer, J.F.2
  • 54
    • 84856756381 scopus 로고    scopus 로고
    • Entry at the trans-face of the Golgi
    • Pfeffer, S.R. 2011. Entry at the trans-face of the Golgi. Cold Spring Harb. Perspect. Biol. 3. http://dx.doi.org/10.1101/cshperspect.a005272
    • (2011) Cold Spring Harb. Perspect. Biol. , pp. 3
    • Pfeffer, S.R.1
  • 55
    • 33846587097 scopus 로고    scopus 로고
    • Interchangeable but essential functions of SNX1 and SNX2 in the association of retromer with endosomes and the trafficking of mannose 6-phosphate receptors
    • Rojas, R., S. Kametaka, C.R. Haft, and J.S. Bonifacino. 2007. Interchangeable but essential functions of SNX1 and SNX2 in the association of retromer with endosomes and the trafficking of mannose 6-phosphate receptors. Mol. Cell. Biol. 27:1112-1124. http://dx.doi.org/10.1128/MCB.00156-06
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 1112-1124
    • Rojas, R.1    Kametaka, S.2    Haft, C.R.3    Bonifacino, J.S.4
  • 56
    • 0036000025 scopus 로고    scopus 로고
    • Targeting of rough endoplasmic reticulum membrane proteins and ribosomes in invertebrate neurons
    • Rolls, M.M., D.H. Hall, M. Victor, E.H. Stelzer, and T.A. Rapoport. 2002. Targeting of rough endoplasmic reticulum membrane proteins and ribosomes in invertebrate neurons. Mol. Biol. Cell. 13:1778-1791. http://dx.doi.org/10.1091/mbc.01-10-0514
    • (2002) Mol. Biol. Cell. , vol.13 , pp. 1778-1791
    • Rolls, M.M.1    Hall, D.H.2    Victor, M.3    Stelzer, E.H.4    Rapoport, T.A.5
  • 57
    • 0032544612 scopus 로고    scopus 로고
    • LIN-10 is a shared component of the polarized protein localization pathways in neurons and epithelia
    • Rongo, C., C.W. Whitfield, A. Rodal, S.K. Kim, and J.M. Kaplan. 1998. LIN-10 is a shared component of the polarized protein localization pathways in neurons and epithelia. Cell. 94:751-759. http://dx.doi.org/10.1016/S0092-8674(00)81734-1
    • (1998) Cell , vol.94 , pp. 751-759
    • Rongo, C.1    Whitfield, C.W.2    Rodal, A.3    Kim, S.K.4    Kaplan, J.M.5
  • 58
    • 58149095671 scopus 로고    scopus 로고
    • X11 proteins regulate the translocation of amyloid beta-protein precursor (APP) into detergent-resistant membrane and suppress the amyloidogenic cleavage of APP by beta-site-cleaving enzyme in brain
    • Saito, Y., Y. Sano, R. Vassar, S. Gandy, T. Nakaya, T. Yamamoto, and T. Suzuki. 2008. X11 proteins regulate the translocation of amyloid beta-protein precursor (APP) into detergent-resistant membrane and suppress the amyloidogenic cleavage of APP by beta-site-cleaving enzyme in brain. J. Biol. Chem. 283:35763-35771. http://dx.doi.org/10.1074/jbc.M801353200
    • (2008) J. Biol. Chem. , vol.283 , pp. 35763-35771
    • Saito, Y.1    Sano, Y.2    Vassar, R.3    Gandy, S.4    Nakaya, T.5    Yamamoto, T.6    Suzuki, T.7
  • 59
    • 33845991184 scopus 로고    scopus 로고
    • Enhanced amyloidogenic metabolism of the amyloid beta-protein precursor in the X11L-deficient mouse brain
    • Sano, Y., A. Syuzo-Takabatake, T. Nakaya, Y. Saito, S. Tomita, S. Itohara, and T. Suzuki. 2006. Enhanced amyloidogenic metabolism of the amyloid beta-protein precursor in the X11L-deficient mouse brain. J. Biol. Chem. 281:37853-37860. http://dx.doi.org/10.1074/jbc.M609312200
    • (2006) J. Biol. Chem. , vol.281 , pp. 37853-37860
    • Sano, Y.1    Syuzo-Takabatake, A.2    Nakaya, T.3    Saito, Y.4    Tomita, S.5    Itohara, S.6    Suzuki, T.7
  • 60
    • 0032575559 scopus 로고    scopus 로고
    • X11 interaction with beta-amyloid precursor protein modulates its cellular stabilization and reduces amyloid beta-protein secretion
    • Sastre, M., R.S. Turner, and E. Levy. 1998. X11 interaction with beta-amyloid precursor protein modulates its cellular stabilization and reduces amyloid beta-protein secretion. J. Biol. Chem. 273:22351-22357. http://dx.doi.org/10.1074/jbc.273.35.22351
    • (1998) J. Biol. Chem. , vol.273 , pp. 22351-22357
    • Sastre, M.1    Turner, R.S.2    Levy, E.3
  • 63
    • 38149016966 scopus 로고    scopus 로고
    • The cell biology of synaptic plasticity: AMPA receptor trafficking
    • Shepherd, J.D., and R.L. Huganir. 2007. The cell biology of synaptic plasticity: AMPA receptor trafficking. Annu. Rev. Cell Dev. Biol. 23:613-643. http://dx.doi.org/10.1146/annurev.cellbio.23.090506.123516
    • (2007) Annu. Rev. Cell Dev. Biol. , vol.23 , pp. 613-643
    • Shepherd, J.D.1    Huganir, R.L.2
  • 64
    • 0037341432 scopus 로고    scopus 로고
    • GLUT4 recycles via a trans-Golgi network (TGN) subdomain enriched in Syntaxins 6 and 16 but not TGN38: Involvement of an acidic targeting motif
    • Shewan, A.M., E.M. van Dam, S. Martin, T.B. Luen, W. Hong, N.J. Bryant, and D.E. James. 2003. GLUT4 recycles via a trans-Golgi network (TGN) subdomain enriched in Syntaxins 6 and 16 but not TGN38: involvement of an acidic targeting motif. Mol. Biol. Cell. 14:973-986. http://dx.doi.org/10.1091/mbc.E02-06-0315
    • (2003) Mol. Biol. Cell. , vol.14 , pp. 973-986
    • Shewan, A.M.1    van Dam, E.M.2    Martin, S.3    Luen, T.B.4    Hong, W.5    Bryant, N.J.6    James, D.E.7
  • 65
    • 70350751557 scopus 로고    scopus 로고
    • Regulation of endosomal clathrin and retromer-mediated endosome to Golgi retrograde transport by the J-domain protein RME-8
    • Shi, A., L. Sun, R. Banerjee, M. Tobin, Y. Zhang, and B.D. Grant. 2009. Regulation of endosomal clathrin and retromer-mediated endosome to Golgi retrograde transport by the J-domain protein RME-8. EMBO J. 28:3290-3302. http://dx.doi.org/10.1038/emboj.2009.272
    • (2009) EMBO J , vol.28 , pp. 3290-3302
    • Shi, A.1    Sun, L.2    Banerjee, R.3    Tobin, M.4    Zhang, Y.5    Grant, B.D.6
  • 66
    • 0035805143 scopus 로고    scopus 로고
    • Subunit-specific rules governing AMPA receptor trafficking to synapses in hippocampal pyramidal neurons
    • Shi, S., Y. Hayashi, J.A. Esteban, and R. Malinow. 2001. Subunit-specific rules governing AMPA receptor trafficking to synapses in hippocampal pyramidal neurons. Cell. 105:331-343. http://dx.doi.org/10.1016/S0092-8674(01)00321-X
    • (2001) Cell , vol.105 , pp. 331-343
    • Shi, S.1    Hayashi, Y.2    Esteban, J.A.3    Malinow, R.4
  • 67
    • 77957981618 scopus 로고    scopus 로고
    • Functional comparison of the effects of TARPs and cornichons on AMPA receptor trafficking and gating
    • Shi, Y., Y.H. Suh, A.D. Milstein, K. Isozaki, S.M. Schmid, K.W. Roche, and R.A. Nicoll. 2010. Functional comparison of the effects of TARPs and cornichons on AMPA receptor trafficking and gating. Proc. Natl. Acad. Sci. USA. 107:16315-16319. http://dx.doi.org/10.1073/pnas.1011706107
    • (2010) Proc. Natl. Acad. Sci. USA. , vol.107 , pp. 16315-16319
    • Shi, Y.1    Suh, Y.H.2    Milstein, A.D.3    Isozaki, K.4    Schmid, S.M.5    Roche, K.W.6    Nicoll, R.A.7
  • 68
    • 6344225824 scopus 로고    scopus 로고
    • The unfolded protein response regulates glutamate receptor export from the endoplasmic reticulum
    • Shim, J., T. Umemura, E. Nothstein, and C. Rongo. 2004. The unfolded protein response regulates glutamate receptor export from the endoplasmic reticulum. Mol. Biol. Cell. 15:4818-4828. http://dx.doi.org/10.1091/mbc.E04-02-0108
    • (2004) Mol. Biol. Cell. , vol.15 , pp. 4818-4828
    • Shim, J.1    Umemura, T.2    Nothstein, E.3    Rongo, C.4
  • 69
    • 40849139207 scopus 로고    scopus 로고
    • Retromer sorting: a pathogenic pathway in late-onset Alzheimer disease
    • Small, S.A. 2008. Retromer sorting: a pathogenic pathway in late-onset Alzheimer disease. Arch. Neurol. 65:323-328. http://dx.doi.org/10.1001/archneurol.2007.64
    • (2008) Arch. Neurol. , vol.65 , pp. 323-328
    • Small, S.A.1
  • 70
    • 34247143246 scopus 로고    scopus 로고
    • Grd19/Snx3p functions as a cargo-specific adapter for retromer-dependent endocytic recycling
    • Strochlic, T.I., T.G. Setty, A. Sitaram, and C.G. Burd. 2007. Grd19/Snx3p functions as a cargo-specific adapter for retromer-dependent endocytic recycling. J. Cell Biol. 177:115-125. http://dx.doi.org/10.1083/jcb.200609161
    • (2007) J. Cell Biol. , vol.177 , pp. 115-125
    • Strochlic, T.I.1    Setty, T.G.2    Sitaram, A.3    Burd, C.G.4
  • 72
    • 77953021275 scopus 로고    scopus 로고
    • Characterizing the interaction between the Rab6 GTPase and Mint3 via flow cytometry based FRET analysis
    • Thyrock, A., M. Stehling, D. Waschbüsch, and A. Barnekow. 2010. Characterizing the interaction between the Rab6 GTPase and Mint3 via flow cytometry based FRET analysis. Biochem. Biophys. Res. Commun. 396:679-683. http://dx.doi.org/10.1016/j.bbrc.2010.04.161
    • (2010) Biochem. Biophys. Res. Commun. , vol.396 , pp. 679-683
    • Thyrock, A.1    Stehling, M.2    Waschbüsch, D.3    Barnekow, A.4
  • 73
    • 54549125798 scopus 로고    scopus 로고
    • The self-tuning neuron: synaptic scaling of excitatory synapses
    • Turrigiano, G.G. 2008. The self-tuning neuron: synaptic scaling of excitatory synapses. Cell. 135:422-435. http://dx.doi.org/10.1016/j.cell.2008.10.008
    • (2008) Cell , vol.135 , pp. 422-435
    • Turrigiano, G.G.1
  • 74
    • 24344501669 scopus 로고    scopus 로고
    • The role of regulatory domain interactions in UNC-43 CaMKII localization and trafficking
    • Umemura, T., P. Rapp, and C. Rongo. 2005. The role of regulatory domain interactions in UNC-43 CaMKII localization and trafficking. J. Cell Sci. 118:3327-3338. http://dx.doi.org/10.1242/jcs.02457
    • (2005) J. Cell Sci. , vol.118 , pp. 3327-3338
    • Umemura, T.1    Rapp, P.2    Rongo, C.3
  • 75
    • 20444377260 scopus 로고    scopus 로고
    • GGA proteins regulate retrograde transport of BACE1 from endosomes to the trans-Golgi network
    • Wahle, T., K. Prager, N. Raffler, C. Haass, M. Famulok, and J. Walter. 2005. GGA proteins regulate retrograde transport of BACE1 from endosomes to the trans-Golgi network. Mol. Cell. Neurosci. 29:453-461. http://dx.doi.org/10.1016/j.mcn.2005.03.014
    • (2005) Mol. Cell. Neurosci. , vol.29 , pp. 453-461
    • Wahle, T.1    Prager, K.2    Raffler, N.3    Haass, C.4    Famulok, M.5    Walter, J.6
  • 76
    • 52049124794 scopus 로고    scopus 로고
    • Evolutionary conserved role for TARPs in the gating of glutamate receptors and tuning of synaptic function
    • Wang, R., C.S. Walker, P.J. Brockie, M.M. Francis, J.E. Mellem, D.M. Madsen, and A.V. Maricq. 2008. Evolutionary conserved role for TARPs in the gating of glutamate receptors and tuning of synaptic function. Neuron. 59:997-1008. http://dx.doi.org/10.1016/j.neuron.2008.07.023
    • (2008) Neuron , vol.59 , pp. 997-1008
    • Wang, R.1    Walker, C.S.2    Brockie, P.J.3    Francis, M.M.4    Mellem, J.E.5    Madsen, D.M.6    Maricq, A.V.7
  • 77
    • 48149099744 scopus 로고    scopus 로고
    • Light-sensitive neurons and channels mediate phototaxis in C. elegans
    • Ward, A., J. Liu, Z. Feng, and X.Z. Xu. 2008. Light-sensitive neurons and channels mediate phototaxis in C. elegans. Nat. Neurosci. 11:916-922. http://dx.doi.org/10.1038/nn.2155
    • (2008) Nat. Neurosci. , vol.11 , pp. 916-922
    • Ward, A.1    Liu, J.2    Feng, Z.3    Xu, X.Z.4
  • 78
    • 0344731071 scopus 로고    scopus 로고
    • Basolateral localization of the Caenorhabditis elegans epidermal growth factor receptor in epithelial cells by the PDZ protein LIN-10
    • Whitfield, C.W., C. Bénard, T. Barnes, S. Hekimi, and S.K. Kim. 1999. Basolateral localization of the Caenorhabditis elegans epidermal growth factor receptor in epithelial cells by the PDZ protein LIN-10. Mol. Biol. Cell. 10:2087-2100.
    • (1999) Mol. Biol. Cell. , vol.10 , pp. 2087-2100
    • Whitfield, C.W.1    Bénard, C.2    Barnes, T.3    Hekimi, S.4    Kim, S.K.5
  • 79
    • 17644409092 scopus 로고    scopus 로고
    • RNA interference-mediated silencing of X11alpha and X11beta attenuates amyloid beta-protein levels via differential effects on beta-amyloid precursor protein processing
    • Xie, Z., D.M. Romano, and R.E. Tanzi. 2005. RNA interference-mediated silencing of X11alpha and X11beta attenuates amyloid beta-protein levels via differential effects on beta-amyloid precursor protein processing. J. Biol. Chem. 280:15413-15421. http://dx.doi.org/10.1074/jbc.M414353200
    • (2005) J. Biol. Chem. , vol.280 , pp. 15413-15421
    • Xie, Z.1    Romano, D.M.2    Tanzi, R.E.3
  • 80
    • 37749043874 scopus 로고    scopus 로고
    • Wnt signaling requires retromer-dependent recycling of MIG-14/Wntless in Wnt-producing cells
    • Yang, P.T., M.J. Lorenowicz, M. Silhankova, D.Y. Coudreuse, M.C. Betist, and H.C. Korswagen. 2008. Wnt signaling requires retromer-dependent recycling of MIG-14/Wntless in Wnt-producing cells. Dev. Cell. 14:140-147. http://dx.doi.org/10.1016/j.devcel.2007.12.004
    • (2008) Dev. Cell. , vol.14 , pp. 140-147
    • Yang, P.T.1    Lorenowicz, M.J.2    Silhankova, M.3    Coudreuse, D.Y.4    Betist, M.C.5    Korswagen, H.C.6
  • 81
    • 12444278931 scopus 로고    scopus 로고
    • Vps20p and Vta1p interact with Vps4p and function in multivesicular body sorting and endosomal transport in Saccharomyces cerevisiae
    • Yeo, S.C., L. Xu, J. Ren, V.J. Boulton, M.D. Wagle, C. Liu, G. Ren, P. Wong, R. Zahn, P. Sasajala, et al. 2003. Vps20p and Vta1p interact with Vps4p and function in multivesicular body sorting and endosomal transport in Saccharomyces cerevisiae. J. Cell Sci. 116:3957-3970. http://dx.doi.org/10.1242/jcs.00751
    • (2003) J. Cell Sci. , vol.116 , pp. 3957-3970
    • Yeo, S.C.1    Xu, L.2    Ren, J.3    Boulton, V.J.4    Wagle, M.D.5    Liu, C.6    Ren, G.7    Wong, P.8    Zahn, R.9    Sasajala, P.10
  • 82
    • 0033212996 scopus 로고    scopus 로고
    • Neuronal control of locomotion in C. elegans is modified by a dominant mutation in the GLR-1 ionotropic glutamate receptor
    • Zheng, Y., P.J. Brockie, J.E. Mellem, D.M. Madsen, and A.V. Maricq. 1999. Neuronal control of locomotion in C. elegans is modified by a dominant mutation in the GLR-1 ionotropic glutamate receptor. Neuron. 24:347-361. http://dx.doi.org/10.1016/S0896-6273(00)80849-1
    • (1999) Neuron , vol.24 , pp. 347-361
    • Zheng, Y.1    Brockie, P.J.2    Mellem, J.E.3    Madsen, D.M.4    Maricq, A.V.5
  • 83
    • 0842307484 scopus 로고    scopus 로고
    • SOL-1 is a CUB-domain protein required for GLR-1 glutamate receptor function in C. elegans
    • Zheng, Y., J.E. Mellem, P.J. Brockie, D.M. Madsen, and A.V. Maricq. 2004. SOL-1 is a CUB-domain protein required for GLR-1 glutamate receptor function in C. elegans. Nature. 427:451-457. http://dx.doi.org/10.1038/nature02244
    • (2004) Nature , vol.427 , pp. 451-457
    • Zheng, Y.1    Mellem, J.E.2    Brockie, P.J.3    Madsen, D.M.4    Maricq, A.V.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.