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Quaternary Structure, Protein Dynamics, and Synaptic Function of SAP97 Controlled by L27 Domain Interactions

Single-particle electron microscopy (EM) combined with biochemical measurements revealed the molecular shape of SAP97 and a monomer-dimer transition that depended on the N-terminal L27 domain. Overexpression of SAP97 drove GluR1 to synapses, potentiated AMPA receptor (AMPAR) excitatory postsynaptic... Full description

Journal Title: Neuron 2004, Vol.44 (3), p.453-467
Main Author: Nakagawa, Terunaga
Other Authors: Futai, Kensuke , Lashuel, Hilal A , Lo, Irene , Okamoto, Kenichi , Walz, Thomas , Hayashi, Yasunori , Sheng, Morgan
Format: Electronic Article Electronic Article
Language: English
Subjects:
Quelle: Alma/SFX Local Collection
Publisher: United States: Elsevier Inc
ID: ISSN: 0896-6273
Link: https://www.ncbi.nlm.nih.gov/pubmed/15504326
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title: Quaternary Structure, Protein Dynamics, and Synaptic Function of SAP97 Controlled by L27 Domain Interactions
format: Article
creator:
  • Nakagawa, Terunaga
  • Futai, Kensuke
  • Lashuel, Hilal A
  • Lo, Irene
  • Okamoto, Kenichi
  • Walz, Thomas
  • Hayashi, Yasunori
  • Sheng, Morgan
subjects:
  • Adaptor Proteins, Signal Transducing
  • Analysis of Variance
  • Animals
  • Baculoviridae - physiology
  • Biophysics - methods
  • Brain - cytology
  • Cells, Cultured
  • Chromatography, Gel - methods
  • Dendritic Spines - metabolism
  • Discs Large Homolog 1 Protein
  • Disks Large Homolog 4 Protein
  • Excitatory Amino Acid Agonists - pharmacology
  • Excitatory Amino Acid Antagonists - pharmacology
  • Excitatory Postsynaptic Potentials - genetics
  • Experiments
  • Gene Expression Regulation - physiology
  • Genetic Vectors
  • Guanylate Kinases
  • Humans
  • Immunohistochemistry - methods
  • In Vitro Techniques
  • Insecta
  • Intracellular Signaling Peptides and Proteins
  • Kinases
  • Lentivirus - genetics
  • Long-Term Potentiation - genetics
  • Medical research
  • Membrane Proteins
  • mental disorders
  • Mice
  • Microscopy, Confocal - methods
  • Microscopy, Electron, Scanning - methods
  • Microscopy, Energy-Filtering Transmission Electron - methods
  • Molecular weight
  • musculoskeletal
  • Mutagenesis
  • N-Methylaspartate - pharmacology
  • Nerve Tissue Proteins - chemistry
  • Nerve Tissue Proteins - metabolism
  • Nerve Tissue Proteins - physiology
  • Nerve Tissue Proteins - ultrastructure
  • nervous system
  • neural
  • Neurons
  • Neurons - cytology
  • Neurons - physiology
  • Neuroscience(all)
  • ocular physiology
  • Patch-Clamp Techniques - methods
  • Protein Structure, Tertiary - physiology
  • Proteins
  • Rats
  • Receptors, AMPA - metabolism
  • Receptors, AMPA - physiology
  • Recombinant Fusion Proteins - genetics
  • Recombinant Fusion Proteins - metabolism
  • RNA, Antisense - metabolism
  • RNA, Small Interfering
  • Sequence Alignment - methods
  • Synapses - physiology
  • Synaptic Transmission - physiology
  • Time Factors
  • Transfection - methods
  • Valine - analogs & derivatives
  • Valine - pharmacology
ispartof: Neuron, 2004, Vol.44 (3), p.453-467
description: Single-particle electron microscopy (EM) combined with biochemical measurements revealed the molecular shape of SAP97 and a monomer-dimer transition that depended on the N-terminal L27 domain. Overexpression of SAP97 drove GluR1 to synapses, potentiated AMPA receptor (AMPAR) excitatory postsynaptic currents (EPSCs), and occluded LTP. Synaptic potentiation and GluR1 delivery were dissociable by L27 domain mutants that inhibit multimerization of SAP97. Loss of potentiation was correlated with faster turnover of monomeric SAP97 mutants in dendritic spines. We propose that L27-mediated interactions of SAP97 with itself or other proteins regulate the synaptic delivery of AMPARs. RNAi knockdown of endogenous PSD-95 depleted surface GluR1 and impaired AMPA EPSCs. In contrast, RNAi knockdown of endogenous SAP97 reduced surface expression of both GluR1 and GluR2 and inhibited both AMPA and NMDA EPSCs. Thus SAP97 has a broader role than its close relative, PSD-95, in the maintenance of synaptic function.
language: eng
source: Alma/SFX Local Collection
identifier: ISSN: 0896-6273
fulltext: fulltext
issn:
  • 0896-6273
  • 1097-4199
url: Link


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titleQuaternary Structure, Protein Dynamics, and Synaptic Function of SAP97 Controlled by L27 Domain Interactions
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descriptionSingle-particle electron microscopy (EM) combined with biochemical measurements revealed the molecular shape of SAP97 and a monomer-dimer transition that depended on the N-terminal L27 domain. Overexpression of SAP97 drove GluR1 to synapses, potentiated AMPA receptor (AMPAR) excitatory postsynaptic currents (EPSCs), and occluded LTP. Synaptic potentiation and GluR1 delivery were dissociable by L27 domain mutants that inhibit multimerization of SAP97. Loss of potentiation was correlated with faster turnover of monomeric SAP97 mutants in dendritic spines. We propose that L27-mediated interactions of SAP97 with itself or other proteins regulate the synaptic delivery of AMPARs. RNAi knockdown of endogenous PSD-95 depleted surface GluR1 and impaired AMPA EPSCs. In contrast, RNAi knockdown of endogenous SAP97 reduced surface expression of both GluR1 and GluR2 and inhibited both AMPA and NMDA EPSCs. Thus SAP97 has a broader role than its close relative, PSD-95, in the maintenance of synaptic function.
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1EISSN: 1097-4199
2DOI: 10.1016/j.neuron.2004.10.012
3PMID: 15504326
languageeng
publisherUnited States: Elsevier Inc
subjectAdaptor Proteins, Signal Transducing ; Analysis of Variance ; Animals ; Baculoviridae - physiology ; Biophysics - methods ; Brain - cytology ; Cells, Cultured ; Chromatography, Gel - methods ; Dendritic Spines - metabolism ; Discs Large Homolog 1 Protein ; Disks Large Homolog 4 Protein ; Excitatory Amino Acid Agonists - pharmacology ; Excitatory Amino Acid Antagonists - pharmacology ; Excitatory Postsynaptic Potentials - genetics ; Experiments ; Gene Expression Regulation - physiology ; Genetic Vectors ; Guanylate Kinases ; Humans ; Immunohistochemistry - methods ; In Vitro Techniques ; Insecta ; Intracellular Signaling Peptides and Proteins ; Kinases ; Lentivirus - genetics ; Long-Term Potentiation - genetics ; Medical research ; Membrane Proteins ; mental disorders ; Mice ; Microscopy, Confocal - methods ; Microscopy, Electron, Scanning - methods ; Microscopy, Energy-Filtering Transmission Electron - methods ; Molecular weight ; musculoskeletal ; Mutagenesis ; N-Methylaspartate - pharmacology ; Nerve Tissue Proteins - chemistry ; Nerve Tissue Proteins - metabolism ; Nerve Tissue Proteins - physiology ; Nerve Tissue Proteins - ultrastructure ; nervous system ; neural ; Neurons ; Neurons - cytology ; Neurons - physiology ; Neuroscience(all) ; ocular physiology ; Patch-Clamp Techniques - methods ; Protein Structure, Tertiary - physiology ; Proteins ; Rats ; Receptors, AMPA - metabolism ; Receptors, AMPA - physiology ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; RNA, Antisense - metabolism ; RNA, Small Interfering ; Sequence Alignment - methods ; Synapses - physiology ; Synaptic Transmission - physiology ; Time Factors ; Transfection - methods ; Valine - analogs & derivatives ; Valine - pharmacology
ispartofNeuron, 2004, Vol.44 (3), p.453-467
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1Futai, Kensuke
2Lashuel, Hilal A
3Lo, Irene
4Okamoto, Kenichi
5Walz, Thomas
6Hayashi, Yasunori
7Sheng, Morgan
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descriptionSingle-particle electron microscopy (EM) combined with biochemical measurements revealed the molecular shape of SAP97 and a monomer-dimer transition that depended on the N-terminal L27 domain. Overexpression of SAP97 drove GluR1 to synapses, potentiated AMPA receptor (AMPAR) excitatory postsynaptic currents (EPSCs), and occluded LTP. Synaptic potentiation and GluR1 delivery were dissociable by L27 domain mutants that inhibit multimerization of SAP97. Loss of potentiation was correlated with faster turnover of monomeric SAP97 mutants in dendritic spines. We propose that L27-mediated interactions of SAP97 with itself or other proteins regulate the synaptic delivery of AMPARs. RNAi knockdown of endogenous PSD-95 depleted surface GluR1 and impaired AMPA EPSCs. In contrast, RNAi knockdown of endogenous SAP97 reduced surface expression of both GluR1 and GluR2 and inhibited both AMPA and NMDA EPSCs. Thus SAP97 has a broader role than its close relative, PSD-95, in the maintenance of synaptic function.
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1Analysis of Variance
2Animals
3Baculoviridae - physiology
4Biophysics - methods
5Brain - cytology
6Cells, Cultured
7Chromatography, Gel - methods
8Dendritic Spines - metabolism
9Discs Large Homolog 1 Protein
10Disks Large Homolog 4 Protein
11Excitatory Amino Acid Agonists - pharmacology
12Excitatory Amino Acid Antagonists - pharmacology
13Excitatory Postsynaptic Potentials - genetics
14Experiments
15Gene Expression Regulation - physiology
16Genetic Vectors
17Guanylate Kinases
18Humans
19Immunohistochemistry - methods
20In Vitro Techniques
21Insecta
22Intracellular Signaling Peptides and Proteins
23Kinases
24Lentivirus - genetics
25Long-Term Potentiation - genetics
26Medical research
27Membrane Proteins
28mental disorders
29Mice
30Microscopy, Confocal - methods
31Microscopy, Electron, Scanning - methods
32Microscopy, Energy-Filtering Transmission Electron - methods
33Molecular weight
34musculoskeletal
35Mutagenesis
36N-Methylaspartate - pharmacology
37Nerve Tissue Proteins - chemistry
38Nerve Tissue Proteins - metabolism
39Nerve Tissue Proteins - physiology
40Nerve Tissue Proteins - ultrastructure
41nervous system
42neural
43Neurons
44Neurons - cytology
45Neurons - physiology
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54Recombinant Fusion Proteins - genetics
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56RNA, Antisense - metabolism
57RNA, Small Interfering
58Sequence Alignment - methods
59Synapses - physiology
60Synaptic Transmission - physiology
61Time Factors
62Transfection - methods
63Valine - analogs & derivatives
64Valine - pharmacology
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titleQuaternary Structure, Protein Dynamics, and Synaptic Function of SAP97 Controlled by L27 Domain Interactions
authorNakagawa, Terunaga ; Futai, Kensuke ; Lashuel, Hilal A ; Lo, Irene ; Okamoto, Kenichi ; Walz, Thomas ; Hayashi, Yasunori ; Sheng, Morgan
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6Cells, Cultured
7Chromatography, Gel - methods
8Dendritic Spines - metabolism
9Discs Large Homolog 1 Protein
10Disks Large Homolog 4 Protein
11Excitatory Amino Acid Agonists - pharmacology
12Excitatory Amino Acid Antagonists - pharmacology
13Excitatory Postsynaptic Potentials - genetics
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15Gene Expression Regulation - physiology
16Genetic Vectors
17Guanylate Kinases
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20In Vitro Techniques
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25Long-Term Potentiation - genetics
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27Membrane Proteins
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35Mutagenesis
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54Recombinant Fusion Proteins - genetics
55Recombinant Fusion Proteins - metabolism
56RNA, Antisense - metabolism
57RNA, Small Interfering
58Sequence Alignment - methods
59Synapses - physiology
60Synaptic Transmission - physiology
61Time Factors
62Transfection - methods
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atitleQuaternary Structure, Protein Dynamics, and Synaptic Function of SAP97 Controlled by L27 Domain Interactions
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abstractSingle-particle electron microscopy (EM) combined with biochemical measurements revealed the molecular shape of SAP97 and a monomer-dimer transition that depended on the N-terminal L27 domain. Overexpression of SAP97 drove GluR1 to synapses, potentiated AMPA receptor (AMPAR) excitatory postsynaptic currents (EPSCs), and occluded LTP. Synaptic potentiation and GluR1 delivery were dissociable by L27 domain mutants that inhibit multimerization of SAP97. Loss of potentiation was correlated with faster turnover of monomeric SAP97 mutants in dendritic spines. We propose that L27-mediated interactions of SAP97 with itself or other proteins regulate the synaptic delivery of AMPARs. RNAi knockdown of endogenous PSD-95 depleted surface GluR1 and impaired AMPA EPSCs. In contrast, RNAi knockdown of endogenous SAP97 reduced surface expression of both GluR1 and GluR2 and inhibited both AMPA and NMDA EPSCs. Thus SAP97 has a broader role than its close relative, PSD-95, in the maintenance of synaptic function.
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pmid15504326
doi10.1016/j.neuron.2004.10.012
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