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Regulation of distinct AMPA receptor phosphorylation sites during bidirectional synaptic plasticity
It is shown that LTP and LTD reversibly modify the phosphorylation of the AMPA receptor GluR1 subunit, and that identical stimulation conditions recruit different signal-transduction pathways depending on synaptic history.
PKA phosphorylation of AMPA receptor subunits controls synaptic trafficking underlying plasticity
- J. Esteban, S. Shi, Christopher L. Wilson, M. Nuriya, R. Huganir, R. Malinow
- Biology, ChemistryNature Neuroscience
- 1 February 2003
It is found that PKA phosphorylation of the AMPA receptor subunits GluR4 and GLUR1 directly controlled the synaptic incorporation of AMPA receptors in organotypic slices from rat hippocampus.
MAPK cascade signalling and synaptic plasticity
This work has reported the involvement of a 'parallel' but distinct kinase cascade leading to the activation of p38 MAPK, which might control distinct forms of synaptic plasticity in the adult brain.
GRIP: a synaptic PDZ domain-containing protein that interacts with AMPA receptors
GRIP is a new member of the PDZ domain-containing protein family which has seven PDZ domains and no catalytic domain and appears to serve as an adapter protein that links AMPA receptors to other proteins and may be critical for the clustering of AMPA receptor at excitatory synapses in the brain.
Characterization of Multiple Phosphorylation Sites on the AMPA Receptor GluR1 Subunit
Elongation Factor 2 and Fragile X Mental Retardation Protein Control the Dynamic Translation of Arc/Arg3.1 Essential for mGluR-LTD
Phosphorylation of the AMPA Receptor Subunit GluR2 Differentially Regulates Its Interaction with PDZ Domain-Containing Proteins
- H. J. Chung, J. Xia, R. Scannevin, Xiaoqun Zhang, R. Huganir
- Biology, ChemistryJournal of Neuroscience
- 1 October 2000
It is shown that PKC phosphorylation of the AMPA receptor GluR2 subunit differentially modulates its interaction with the PDZ domain-containing proteins GRIP1 and PICK1.
The cell biology of synaptic plasticity: AMPA receptor trafficking.
The life cycle of AMPARs is described, from their biogenesis, through their journey to the synapse, and ultimately through their demise, and how the modulation of this process is essential for brain function is discussed.
Arc/Arg3.1 Mediates Homeostatic Synaptic Scaling of AMPA Receptors
The C9orf72 repeat expansion disrupts nucleocytoplasmic transport
Nuclear import is impaired as a result of HRE expression in the fly model and in C9orf72 iPSC-derived neurons, and these deficits are rescued by small molecules and antisense oligonucleotides targeting the HRE G-quadruplexes.