메뉴 건너뛰기




Volumn 289, Issue 6, 2014, Pages 3444-3456

The WD40-repeat Proteins WDR-20 and WDR-48 Bind and activate the Deubiquitinating Enzyme USP-46 to promote the abundance of the Glutamate Receptor GLR-1 in the ventral Nerve Cord of Caenorhabditis elegans

Author keywords

[No Author keywords available]

Indexed keywords

CAENORHABDITIS ELEGANS; DEUBIQUITINATION; GLUTAMATE RECEPTORS IONOTROPIC (AMPA, NMDA); NEURONS; SYNAPSES; UBIQUITIN;

EID: 84893711029     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.507541     Document Type: Article
Times cited : (35)

References (54)
  • 1
    • 38149016966 scopus 로고    scopus 로고
    • The cell biology of synaptic plasticity. Ampa receptor trafficking
    • Shepherd, J. D., and Huganir, R. L. (2007) The cell biology of synaptic plasticity. AMPA receptor trafficking. Annu. Rev. Cell Dev. Biol. 23, 613-643
    • (2007) Annu. Rev. Cell Dev. Biol. , vol.23 , pp. 613-643
    • Shepherd, J.D.1    Huganir, R.L.2
  • 2
    • 84858292500 scopus 로고    scopus 로고
    • Ubiquitin-dependent endocytosis, trafficking and turnover of neuronal membrane proteins
    • Schwarz, L. A., and Patrick, G. N. (2012) Ubiquitin-dependent endocytosis, trafficking and turnover of neuronal membrane proteins. Mol. Cell Neurosci. 49, 387-393
    • (2012) Mol. Cell Neurosci. , vol.49 , pp. 387-393
    • Schwarz, L.A.1    Patrick, G.N.2
  • 3
    • 0037014445 scopus 로고    scopus 로고
    • Ubiquitin and ap180 regulate the abundance of glr-1 glutamate receptors at postsynaptic elements in c. Elegans
    • Burbea, M., Dreier, L., Dittman, J. S., Grunwald, M. E., and Kaplan, J. M. (2002) Ubiquitin and AP180 regulate the abundance of GLR-1 glutamate receptors at postsynaptic elements in C. elegans. Neuron 35, 107-120
    • (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
  • 5
  • 7
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains. Structure and function of the deubiquitinases
    • Komander, D., Clague, M. J., and Urbé, S. (2009) Breaking the chains. Structure and function of the deubiquitinases. Nat. Rev. Mol. Cell Biol. 10, 550-563
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbé, S.3
  • 8
    • 84872163803 scopus 로고    scopus 로고
    • The role of deubiquitinating enzymes in synaptic function and nervous system diseases
    • Kowalski, J. R., and Juo, P. (2012) The role of deubiquitinating enzymes in synaptic function and nervous system diseases. Neural Plast. 2012, 892749
    • (2012) Neural Plast. , vol.2012 , pp. 892749
    • Kowalski, J.R.1    Juo, P.2
  • 9
    • 51349154176 scopus 로고    scopus 로고
    • Unc-108/rab2 regulates postendocytic trafficking in caenorhabditis elegans
    • Chun, D. K., McEwen, J. M., Burbea, M., and Kaplan, J. M. (2008) UNC-108/Rab2 regulates postendocytic trafficking in Caenorhabditis elegans. Mol. Biol. Cell 19, 2682-2695
    • (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
    • 0344663966 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteasome activity is required for agonist-induced endocytosis of glurs
    • Patrick, G. N., Bingol, B., Weld, H. A., and Schuman, E. M. (2003) Ubiquitin-mediated proteasome activity is required for agonist-induced endocytosis of GluRs. Curr. Biol. 13, 2073-2081
    • (2003) Curr. Biol. , vol.13 , pp. 2073-2081
    • Patrick, G.N.1    Bingol, B.2    Weld, H.A.3    Schuman, E.M.4
  • 12
    • 16844385820 scopus 로고    scopus 로고
    • Lin-23-mediated degradation of beta-catenin regulates the abundance of glr-1 glutamate receptors in the ventral nerve cord of c. Elegans
    • Dreier, L., Burbea, M., and Kaplan, J. M. (2005) LIN-23-mediated degradation of beta-catenin regulates the abundance of GLR-1 glutamate receptors in the ventral nerve cord of C. elegans. Neuron 46, 51-64
    • (2005) Neuron , vol.46 , pp. 51-64
    • Dreier, L.1    Burbea, M.2    Kaplan, J.M.3
  • 13
    • 9244263049 scopus 로고    scopus 로고
    • The anaphase-promoting complex regulates the abundance of glr-1 glutamate receptors in the ventral nerve cord of c. Elegans
    • Juo, P., and Kaplan, J. M. (2004) The anaphase-promoting complex regulates the abundance of GLR-1 glutamate receptors in the ventral nerve cord of C. elegans. Curr. Biol. 14, 2057-2062
    • (2004) Curr. Biol. , vol.14 , pp. 2057-2062
    • Juo, P.1    Kaplan, J.M.2
  • 14
    • 59349099346 scopus 로고    scopus 로고
    • The ubiquitin ligase rpm-1 and the p38 mapk pmk-3 regulate ampa receptor trafficking
    • Park, E. C., Glodowski, D. R., and Rongo, C. (2009) The ubiquitin ligase RPM-1 and the p38 MAPK PMK-3 regulate AMPA receptor trafficking. PloS ONE 4, e4284
    • (2009) PloS ONE , vol.4
    • Park, E.C.1    Glodowski, D.R.2    Rongo, C.3
  • 15
    • 8844276742 scopus 로고    scopus 로고
    • Independent regulation of synaptic size and activity by the anaphase-promoting complex
    • van Roessel, P., Elliott, D. A., Robinson, I. M., Prokop, A., and Brand, A. H. (2004) Independent regulation of synaptic size and activity by the anaphase-promoting complex. Cell 119, 707-718
    • (2004) Cell , vol.119 , pp. 707-718
    • Van Roessel, P.1    Elliott, D.A.2    Robinson, I.M.3    Prokop, A.4    Brand, A.H.5
  • 16
    • 33644866769 scopus 로고    scopus 로고
    • Kel-8 is a substrate receptor for cul3-dependent ubiquitin ligase that regulates synaptic glutamate receptor turnover
    • Schaefer, H., and Rongo, C. (2006) KEL-8 is a substrate receptor for CUL3-dependent ubiquitin ligase that regulates synaptic glutamate receptor turnover. Mol. Biol. Cell 17, 1250-1260
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1250-1260
    • Schaefer, H.1    Rongo, C.2
  • 17
    • 79251584863 scopus 로고    scopus 로고
    • Apc(cdh1) mediates epha4-dependent downregulation of ampa receptors in homeostatic plasticity
    • Fu, A. K., Hung, K. W., Fu, W. Y., Shen, C., Chen, Y., Xia, J., Lai, K. O., and Ip, N. Y. (2011) APC(Cdh1) mediates EphA4-dependent downregulation of AMPA receptors in homeostatic plasticity. Nat. Neurosci. 14, 181-189
    • (2011) Nat. Neurosci. , vol.14 , pp. 181-189
    • Fu, A.K.1    Hung, K.W.2    Fu, W.Y.3    Shen, C.4    Chen, Y.5    Xia, J.6    Lai, K.O.7    Ip, N.Y.8
  • 18
    • 80052690758 scopus 로고    scopus 로고
    • Nedd4-mediated ampa receptor ubiquitination regulates receptor turnover and trafficking
    • Lin, A., Hou, Q., Jarzylo, L., Amato, S., Gilbert, J., Shang, F., and Man, H. Y. (2011) Nedd4-mediated AMPA receptor ubiquitination regulates receptor turnover and trafficking. J. Neurochem. 119, 27-39
    • (2011) J. Neurochem. , vol.119 , pp. 27-39
    • Lin, A.1    Hou, Q.2    Jarzylo, L.3    Amato, S.4    Gilbert, J.5    Shang, F.6    Man, H.Y.7
  • 20
    • 78650070867 scopus 로고    scopus 로고
    • Activity-dependent ubiquitination of glua1 mediates a distinct ampa receptor endocytosis and sorting pathway
    • Schwarz, L. A., Hall, B. J., and Patrick, G. N. (2010) Activity-dependent ubiquitination of GluA1 mediates a distinct AMPA receptor endocytosis and sorting pathway. J. Neurosci. 30, 16718-16729
    • (2010) J. Neurosci. , vol.30 , pp. 16718-16729
    • Schwarz, L.A.1    Hall, B.J.2    Patrick, G.N.3
  • 21
    • 79251554350 scopus 로고    scopus 로고
    • The deubiquitinating enzyme usp-46 negatively regulates the degradation of glutamate receptors to control their abundance in the ventral nerve cord of caenorhabditis elegans
    • Kowalski, J. R., Dahlberg, C. L., and Juo, P. (2011) The deubiquitinating enzyme USP-46 negatively regulates the degradation of glutamate receptors to control their abundance in the ventral nerve cord of Caenorhabditis elegans. J. Neurosci. 31, 1341-1354
    • (2011) J. Neurosci. , vol.31 , pp. 1341-1354
    • Kowalski, J.R.1    Dahlberg, C.L.2    Juo, P.3
  • 24
    • 77957893483 scopus 로고    scopus 로고
    • A global census of fission yeast deubiquitinating enzyme localization and interaction networks reveals distinct compartmentalization profiles and overlapping functions in endocytosis and polarity
    • Kouranti, I., McLean, J. R., Feoktistova, A., Liang, P., Johnson, A. E., Roberts-Galbraith, R. H., and Gould, K. L. (2010) A global census of fission yeast deubiquitinating enzyme localization and interaction networks reveals distinct compartmentalization profiles and overlapping functions in endocytosis and polarity. PLoS Biol. 8, e1000471
    • (2010) PLoS Biol. , vol.8
    • Kouranti, I.1    McLean, J.R.2    Feoktistova, A.3    Liang, P.4    Johnson, A.E.5    Roberts-Galbraith, R.H.6    Gould, K.L.7
  • 25
    • 84873055250 scopus 로고    scopus 로고
    • The deubiquitination enzyme usp46 functions as a tumor suppressor by controlling phlpp-dependent attenuation of akt signaling in colon cancer
    • Li, X., Stevens, P. D., Yang, H., Gulhati, P., Wang, W., Evers, B. M., and Gao, T. (2013) The deubiquitination enzyme USP46 functions as a tumor suppressor by controlling PHLPP-dependent attenuation of Akt signaling in colon cancer. Oncogene 32, 471-478
    • (2013) Oncogene , vol.32 , pp. 471-478
    • Li, X.1    Stevens, P.D.2    Yang, H.3    Gulhati, P.4    Wang, W.5    Evers, B.M.6    Gao, T.7
  • 26
    • 84870685075 scopus 로고    scopus 로고
    • Deubiquitylation machinery is required for embryonic polarity in caenorhabditis elegans
    • McCloskey, R. J., and Kemphues, K. J. (2012) Deubiquitylation machinery is required for embryonic polarity in Caenorhabditis elegans. PLoS Genet. 8, e1003092
    • (2012) PLoS Genet. , vol.8
    • McCloskey, R.J.1    Kemphues, K.J.2
  • 27
    • 84865455417 scopus 로고    scopus 로고
    • The ubiquitin-specific protease 12 (usp12) is a negative regulator of notch signaling acting on notch receptor trafficking toward degradation
    • Moretti, J., Chastagner, P., Liang, C. C., Cohn, M. A., Israël, A., and Brou, C. (2012) The ubiquitin-specific protease 12 (USP12) is a negative regulator of Notch signaling acting on Notch receptor trafficking toward degradation. J. Biol. Chem. 287, 29429-29441
    • (2012) J. Biol. Chem. , vol.287 , pp. 29429-29441
    • Moretti, J.1    Chastagner, P.2    Liang, C.C.3    Cohn, M.A.4    Israël, A.5    Brou, C.6
  • 28
    • 84862263954 scopus 로고    scopus 로고
    • Ubiquitin-specific peptidase 46 (usp46) regulates mouse immobile behavior in the tail suspension test through the gabaergic system
    • Imai, S., Mamiya, T., Tsukada, A., Sakai, Y., Mouri, A., Nabeshima, T., and Ebihara, S. (2012) Ubiquitin-specific peptidase 46 (Usp46) regulates mouse immobile behavior in the tail suspension test through the GABAergic system. PloS ONE 7, e39084
    • (2012) PloS ONE , vol.7
    • Imai, S.1    Mamiya, T.2    Tsukada, A.3    Sakai, Y.4    Mouri, A.5    Nabeshima, T.6    Ebihara, S.7
  • 30
    • 64149129169 scopus 로고    scopus 로고
    • Uaf1 is a subunit of multiple deubiquitinating enzyme complexes
    • Cohn, M. A., Kee, Y., Haas, W., Gygi, S. P., and D'Andrea, A. D. (2009) UAF1 is a subunit of multiple deubiquitinating enzyme complexes. J. Biol. Chem. 284, 5343-5351
    • (2009) J. Biol. Chem. , vol.284 , pp. 5343-5351
    • Cohn, M.A.1    Kee, Y.2    Haas, W.3    Gygi, S.P.4    D'Andrea, A.D.5
  • 32
    • 77951247308 scopus 로고    scopus 로고
    • Wdr20 regulates activity of the usp12 x uaf1 deubiquitinating enzyme complex
    • Kee, Y., Yang, K., Cohn, M. A., Haas, W., Gygi, S. P., and D'Andrea, A. D. (2010) WDR20 regulates activity of the USP12 x UAF1 deubiquitinating enzyme complex. J. Biol. Chem. 285, 11252-11257
    • (2010) J. Biol. Chem. , vol.285 , pp. 11252-11257
    • Kee, Y.1    Yang, K.2    Cohn, M.A.3    Haas, W.4    Gygi, S.P.5    D'Andrea, A.D.6
  • 33
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • Sowa, M. E., Bennett, E. J., Gygi, S. P., and Harper, J. W. (2009) Defining the human deubiquitinating enzyme interaction landscape. Cell 138, 389-403
    • (2009) Cell , vol.138 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4
  • 34
    • 0016063911 scopus 로고
    • The genetics of caenorhabditis elegans
    • Brenner, S. (1974) The genetics of Caenorhabditis elegans. Genetics 77, 71-94
    • (1974) Genetics , vol.77 , pp. 71-94
    • Brenner, S.1
  • 35
    • 0032544612 scopus 로고
    • Lin-10 is a shared component of the polarized protein localization path-ways in neurons and epithelia
    • Rongo, C., Whitfield, C. W., Rodal, A., Kim, S. K., and Kaplan, J. M. (1998) LIN-10 is a shared component of the polarized protein localization path-ways in neurons and epithelia. Cell 94, 751-759
    • (1988) Cell , vol.94 , pp. 751-759
    • Rongo, C.1    Whitfield, C.W.2    Rodal, A.3    Kim, S.K.4    Kaplan, J.M.5
  • 36
    • 34248529792 scopus 로고    scopus 로고
    • Primary culture of caenorhabditis elegans developing embryo cells for electrophysiological, cell biological and molecular studies
    • Strange, K., Christensen, M., and Morrison, R. (2007) Primary culture of Caenorhabditis elegans developing embryo cells for electrophysiological, cell biological and molecular studies. Nat. Prot. 2, 1003-1012
    • (2007) Nat. Prot. , vol.2 , pp. 1003-1012
    • Strange, K.1    Christensen, M.2    Morrison, R.3
  • 37
    • 34948862147 scopus 로고    scopus 로고
    • Cdk-5 regulates the abundance of glr-1 glutamate receptors in the ventral cord of caenorhabditis elegans
    • Juo, P., Harbaugh, T., Garriga, G., and Kaplan, J. M. (2007) CDK-5 regulates the abundance of GLR-1 glutamate receptors in the ventral cord of Caenorhabditis elegans. Mol. Biol. Cell 18, 3883-3893
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3883-3893
    • Juo, P.1    Harbaugh, T.2    Garriga, G.3    Kaplan, J.M.4
  • 38
    • 26944490411 scopus 로고    scopus 로고
    • A combined approach for the localization and tandem affinity purification of protein complexes from metazoans
    • pl1
    • Cheeseman, I. M., and Desai, A. (2005) A combined approach for the localization and tandem affinity purification of protein complexes from metazoans. Sci. STKE 2005, pl1
    • (2005) Sci. STKE , vol.2005
    • Cheeseman, I.M.1    Desai, A.2
  • 39
    • 1442355024 scopus 로고    scopus 로고
    • Activity-based ubiquitin-specific protease (usp) profiling of virus-infected and malignant human cells
    • Ovaa, H., Kessler, B. M., Rolén, U., Galardy, P. J., Ploegh, H. L., and Masucci, M. G. (2004) Activity-based ubiquitin-specific protease (USP) profiling of virus-infected and malignant human cells. Proc. Natl. Acad. Sci. U.S.A. 101, 2253-2258
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 2253-2258
    • Ovaa, H.1    Kessler, B.M.2    Rolén, U.3    Galardy, P.J.4    Ploegh, H.L.5    Masucci, M.G.6
  • 40
    • 0035282944 scopus 로고    scopus 로고
    • Differential expression of glutamate receptor subunits in the nervous system of caenorhabditis elegans and their regulation by the homeodomain protein unc-42
    • Brockie, P. J., Madsen, D. M., Zheng, Y., Mellem, J., and Maricq, A. V. (2001) Differential expression of glutamate receptor subunits in the nervous system of Caenorhabditis elegans and their regulation by the homeodomain protein UNC-42. J. Neurosci. 21, 1510-1522
    • (2001) J. Neurosci. , vol.21 , pp. 1510-1522
    • Brockie, P.J.1    Madsen, D.M.2    Zheng, Y.3    Mellem, J.4    Maricq, A.V.5
  • 41
    • 0028867824 scopus 로고
    • Synaptic code for sensory modalities revealed by c. Elegans glr-1 glutamate receptor
    • Hart, A. C., Sims, S., and Kaplan, J. M. (1995) Synaptic code for sensory modalities revealed by C. elegans GLR-1 glutamate receptor. Nature 378, 82-85
    • (1995) Nature , vol.378 , pp. 82-85
    • Hart, A.C.1    Sims, S.2    Kaplan, J.M.3
  • 42
    • 0028837546 scopus 로고
    • Mechanosensory signalling in c. Elegans mediated by the glr-1 glutamate receptor
    • Maricq, A. V., Peckol, E., Driscoll, M., and Bargmann, C. I. (1995) Mechanosensory signalling in C. elegans mediated by the GLR-1 glutamate receptor. Nature 378, 78-81
    • (1995) Nature , vol.378 , pp. 78-81
    • Maricq, A.V.1    Peckol, E.2    Driscoll, M.3    Bargmann, C.I.4
  • 44
    • 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., Brockie, P. J., Mellem, J. E., Madsen, D. M., and Maricq, A. V. (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
    • (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
  • 45
    • 84864286265 scopus 로고    scopus 로고
    • Magi-1 modulates ampareceptor synaptic localization and behavioral plasticity in response to prior experience
    • Emtage, L., Chang, H., Tiver, R., and Rongo, C. (2009) MAGI-1 modulates AMPAreceptor synaptic localization and behavioral plasticity in response to prior experience. PloS ONE 4, e4613
    • (2009) PloS ONE , vol.4
    • Emtage, L.1    Chang, H.2    Tiver, R.3    Rongo, C.4
  • 46
    • 0842307484 scopus 로고    scopus 로고
    • Sol-1 is a cub-domain protein required for glr-1 glutamate receptor function in c. Elegans
    • Zheng, Y., Mellem, J. E., Brockie, P. J., Madsen, D. M., and Maricq, A. V. (2004) SOL-1 is a CUB-domain protein required for GLR-1 glutamate receptor function in C. elegans. Nature 427, 451-457
    • (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
  • 47
    • 0035974849 scopus 로고    scopus 로고
    • The c. Elegans glutamate receptor subunit nmr-1 is required for slow nmda-Activated currents that regulate reversal frequency during locomotion
    • Brockie, P. J., Mellem, J. E., Hills, T., Madsen, D. M., and Maricq, A. V. (2001) The C. elegans glutamate receptor subunit NMR-1 is required for slow NMDA-Activated currents that regulate reversal frequency during locomotion. Neuron 31, 617-630
    • (2001) Neuron , vol.31 , pp. 617-630
    • Brockie, P.J.1    Mellem, J.E.2    Hills, T.3    Madsen, D.M.4    Maricq, A.V.5
  • 48
    • 78650962524 scopus 로고    scopus 로고
    • Deconstruction for reconstruction. The role of proteolysis in neural plasticity and disease
    • Bingol, B., and Sheng, M. (2011) Deconstruction for reconstruction. The role of proteolysis in neural plasticity and disease. Neuron 69, 22-32
    • (2011) Neuron , vol.69 , pp. 22-32
    • Bingol, B.1    Sheng, M.2
  • 49
    • 54249158324 scopus 로고    scopus 로고
    • Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction
    • Tai, H. C., and Schuman, E. M. (2008) Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction. Nat. Rev. Neurosci. 9, 826-838
    • (2008) Nat. Rev. Neurosci. , vol.9 , pp. 826-838
    • Tai, H.C.1    Schuman, E.M.2
  • 50
    • 33847410541 scopus 로고    scopus 로고
    • Emerging roles for ubiquitin and protein degradation in neuronal function
    • Yi, J. J., and Ehlers, M. D. (2007) Emerging roles for ubiquitin and protein degradation in neuronal function. Pharmacol. Rev. 59, 14-39
    • (2007) Pharmacol. Rev. , vol.59 , pp. 14-39
    • Yi, J.J.1    Ehlers, M.D.2
  • 51
    • 79959906646 scopus 로고    scopus 로고
    • Balancing act. Deubiquitinating enzymes in the nervous system
    • Todi, S. V., and Paulson, H. L. (2011) Balancing act. Deubiquitinating enzymes in the nervous system. Trends Neurosci. 34, 370-382
    • (2011) Trends Neurosci. , vol.34 , pp. 370-382
    • Todi, S.V.1    Paulson, H.L.2
  • 52
    • 36749082959 scopus 로고    scopus 로고
    • Auaf1-containing multisubunit protein complex regulates the fanconi anemia pathway
    • Cohn, M. A., Kowal, P., Yang, K., Haas, W., Huang, T. T., Gygi, S. P., and D'Andrea, A. D. (2007)AUAF1-containing multisubunit protein complex regulates the Fanconi anemia pathway. Mol. Cell 28, 786-797
    • (2007) Mol. Cell , vol.28 , pp. 786-797
    • Cohn, M.A.1    Kowal, P.2    Yang, K.3    Haas, W.4    Huang, T.T.5    Gygi, S.P.6    D'Andrea, A.D.7
  • 53
    • 0033639083 scopus 로고    scopus 로고
    • Reinsertion or degradation of ampa receptors determined by activity-dependent endocytic sorting
    • Ehlers, M. D. (2000) Reinsertion or degradation of AMPA receptors determined by activity-dependent endocytic sorting. Neuron 28, 511-525
    • (2000) Neuron , vol.28 , pp. 511-525
    • Ehlers, M.D.1
  • 54
    • 0033695663 scopus 로고    scopus 로고
    • Distinct molecular mechanisms and divergent endocytotic pathways of ampa receptor internalization
    • Lin, J. W., Ju, W., Foster, K., Lee, S. H., Ahmadian, G., Wyszynski, M., Wang, Y. T., and Sheng, M. (2000) Distinct molecular mechanisms and divergent endocytotic pathways of AMPA receptor internalization. Nat. Neurosci. 3, 1282-1290
    • (2000) Nat. Neurosci. , vol.3 , pp. 1282-1290
    • Lin, J.W.1    Ju, W.2    Foster, K.3    Lee, S.H.4    Ahmadian, G.5    Wyszynski, M.6    Wang, Y.T.7    Sheng, M.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.