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Fung, E.T.2
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48
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Yotiao: A novel protein of neuromusuclar junction and brain that interacts with specific splice variants of NMDA receptor subunit MR1
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Lin JW, Wyszynski M, Madhavan R, Sealock R, Kim JU, Sheng M. Yotiao: a novel protein of neuromusuclar junction and brain that interacts with specific splice variants of NMDA receptor subunit MR1. J Neurosci. 18:1998;2017-2027.
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Lin, J.W.1
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Sheng, M.6
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49
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Competitive binding of alpha-actinin and calmodulin to the NMDA receptor
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of outstanding interest. This paper describes the interaction of the NR1 and NR2B subunits with α-actin through their cytoplasmic tails, providing a mechanism for the anchorage of the NMDA receptor to the actin cytoskeleton. The interaction of α-actinin with the NR1 tail can also be completed off by calcium/calmodulin, thus suggesting that calcium entry through the NMDA receptor may modulate the receptor's interaction with the actin cytoskeleton. This work also offers an explanation for the dependence of NMDA receptor activity on intact cytoskeleton.
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Wyszynski M, Lin J, Rao A, Nigh E, Beggs AH, Craig AM, Sheng M. Competitive binding of alpha-actinin and calmodulin to the NMDA receptor. of outstanding interest Nature. 385:1997;439-442 This paper describes the interaction of the NR1 and NR2B subunits with α-actin through their cytoplasmic tails, providing a mechanism for the anchorage of the NMDA receptor to the actin cytoskeleton. The interaction of α-actinin with the NR1 tail can also be completed off by calcium/calmodulin, thus suggesting that calcium entry through the NMDA receptor may modulate the receptor's interaction with the actin cytoskeleton. This work also offers an explanation for the dependence of NMDA receptor activity on intact cytoskeleton.
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Nature
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Wyszynski, M.1
Lin, J.2
Rao, A.3
Nigh, E.4
Beggs, A.H.5
Craig, A.M.6
Sheng, M.7
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50
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0032519871
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Differential regional expression and ultrastructural localization of alpha-actinin-2, a putative NMDA receptor anchoring protein, in rat brain
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Wyszynski W, Kharazia V, Rao A, Beggs AH, Craig AM, Weinberg R, Sheng M. Differential regional expression and ultrastructural localization of alpha-actinin-2, a putative NMDA receptor anchoring protein, in rat brain. J Neurosci. 18:1998;1383-1392.
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Wyszynski, W.1
Kharazia, V.2
Rao, A.3
Beggs, A.H.4
Craig, A.M.5
Weinberg, R.6
Sheng, M.7
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51
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Role of actin in the organization of brain-postsynaptic densities
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Adam G, Matus A. Role of actin in the organization of brain-postsynaptic densities. Brain Res Mol Brain Res. 43:1996;246-250.
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Brain Res Mol Brain Res
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Inactivation of NMDA receptors by direct interaction of calmodulin with the NR1 subunit
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Ehlers MD, Zhang S, Bernhardt JP, Huganir RL. Inactivation of NMDA receptors by direct interaction of calmodulin with the NR1 subunit. Cell. 84:1996;745-755.
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Ehlers, M.D.1
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53
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Calcium-dependent inactivation of recombinant NMDA receptors is NR2 subunit specific
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Krupp JJ, Vissel B, Heinemann SF, Westbrook GL. Calcium-dependent inactivation of recombinant NMDA receptors is NR2 subunit specific. Mol Pharmacol. 50:1996;1680-1688.
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Krupp, J.J.1
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0030861054
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Hisatsune C, Umemori H, Inoue T, Michikawa T, Kohda K, Mikoshiba K, Yamamoto T. Phosphorylation-dependent regulation of N-methyl-D-aspartate receptors by calmodulin. J Biol Chem. 272:1997;20805-20810.
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Hisatsune, C.1
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Yamamoto, T.7
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55
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0030900558
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GRIP, a synaptic PDZ domain-containing protein that interacts with AMPA receptors [see comments]
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of outstanding interest. Using the yeast two-hybrid system, these investigators isolated a PDZ domain containing protein that interacted specifically with the carboxy-terminal tail of GluR2 and GluR3. Co-immunoprecipitation and immunohistochemistry suggested that GRIP and AMPA receptors directly interact in neurons. As a second and related observation, the investigators also found that overexpression of the GLUR2 carboxyl terminus disrupted AMPA receptor synaptic targeting.
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Dong H, O'Brien RJ, Fung ET, Lanahan AA, Worley PF, Huganir RL. GRIP, a synaptic PDZ domain-containing protein that interacts with AMPA receptors [see comments]. of outstanding interest Nature. 386:1997;279-284 Using the yeast two-hybrid system, these investigators isolated a PDZ domain containing protein that interacted specifically with the carboxy-terminal tail of GluR2 and GluR3. Co-immunoprecipitation and immunohistochemistry suggested that GRIP and AMPA receptors directly interact in neurons. As a second and related observation, the investigators also found that overexpression of the GLUR2 carboxyl terminus disrupted AMPA receptor synaptic targeting.
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(1997)
Nature
, vol.386
, pp. 279-284
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Dong, H.1
O'Brien, R.J.2
Fung, E.T.3
Lanahan, A.A.4
Worley, P.F.5
Huganir, R.L.6
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56
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0027480426
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AMPA glutamate receptor subunits are differentially distributed in rat brain
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Martin LJ, Blackstone CD, Levey AI, Huganir RL, Price DL. AMPA glutamate receptor subunits are differentially distributed in rat brain. Neuroscience. 53:1993;327-358.
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Neuroscience
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Martin, L.J.1
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Huganir, R.L.4
Price, D.L.5
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57
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0027999649
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Cellular localization and laminar distribution of AMPA receptor subunit mRNAs and proteins in the rat cerebral cortex
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Conti F, Minelli A, Brecha N. Cellular localization and laminar distribution of AMPA receptor subunit mRNAs and proteins in the rat cerebral cortex. J Comput Neurol. 350:1994;241-259.
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Conti, F.1
Minelli, A.2
Brecha, N.3
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58
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0030969931
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Glutamate receptors are selectively targeted as postsynaptic sites in neurons
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of outstanding interest. This paper reported that glutamate receptors could be sorted within a given neuron based on their subunit composition. The authors found that in neurons with two different types of dendrites, GluR4 containing AMPA receptors were sorted into one type of dendrite, whereas those without GluR4 were sorted into another. This morphologic observation explained already known physiological differences between the synapses on these dendrites.
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of outstanding interest Rubio M, Wenthold RJ. Glutamate receptors are selectively targeted as postsynaptic sites in neurons. Neuron. 18:1997;939-950 This paper reported that glutamate receptors could be sorted within a given neuron based on their subunit composition. The authors found that in neurons with two different types of dendrites, GluR4 containing AMPA receptors were sorted into one type of dendrite, whereas those without GluR4 were sorted into another. This morphologic observation explained already known physiological differences between the synapses on these dendrites.
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Neuron
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Rubio, M.1
Wenthold, R.J.2
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59
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0030970135
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Homer: A protein that selectively binds metabotropic glutamate receptors
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of outstanding interest. This paper shows that Homer, a PDZ-like domain containing protein, interacts with the cytoplasmic tails of the phospholipiase-C-linked metabotropic glutamate receptors, mGluR1a and mGluR5. Synaptic activity induces the expression of Homer and may thus regulate the targeting of the metabotropic glutamate receptor.
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Brakeman PR, Lanahan AA, O'Brien R, Roche K, Barnes CA, Huganir RL, Worley PF. Homer: a protein that selectively binds metabotropic glutamate receptors. of outstanding interest Nature. 386:1997;284-288 This paper shows that Homer, a PDZ-like domain containing protein, interacts with the cytoplasmic tails of the phospholipiase-C-linked metabotropic glutamate receptors, mGluR1a and mGluR5. Synaptic activity induces the expression of Homer and may thus regulate the targeting of the metabotropic glutamate receptor.
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(1997)
Nature
, vol.386
, pp. 284-288
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Brakeman, P.R.1
Lanahan, A.A.2
O'Brien, R.3
Roche, K.4
Barnes, C.A.5
Huganir, R.L.6
Worley, P.F.7
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