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Membrane palmitoylated protein 2 is a synaptic scaffold protein required for synaptic SK2-containing channel function

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TLDR
Kim et al. as mentioned in this paper showed that SK2 physically interacts with a scaffold protein called MPP2, and this allows SK2-containing channels to contribute to long-term potentiation and synaptic strengthening.
Abstract
The neurons in the brain communicate with each other by releasing chemical messengers across structures called synapses. This signaling always occurs in the same direction: at a given synapse, one neuron sends signals that bind to receptor proteins on the surface of the receiving neuron. Repeatedly signaling across a synapse strengthens it, making it easier to communicate across, and sometimes such stimulation can cause a persistent strengthening of the synapse: this is known as long-term potentiation. Changes in synaptic strength are important for learning and memory. In the synapses formed between a type of brain cell called CA1 neurons, a protein called SK2 forms part of an ion channel in the membrane of the receiving neuron and is important for synaptic strengthening and long-term potentiation. To work correctly, the SK2 channels must be precisely positioned at the synapse, but the mechanisms responsible for this positioning were not clear. Now, by experimenting with purified proteins taken from the CA1 neurons of mice, Kim et al. show that SK2 physically interacts with a scaffold protein called MPP2. Further experiments revealed that MPP2 is responsible for positioning SK2 at the synapses, and this allows SK2-containing channels to contribute to long-term potentiation and synaptic strengthening. During synaptic strengthening, it is possible that SK2 disengages from MPP2, which influences learning. The next step is to understand the processes that dictate this behavior.

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Journal ArticleDOI

AMPA receptors and their minions: auxiliary proteins in AMPA receptor trafficking

TL;DR: The current knowledge about the roles of key partners in regulating AMPA receptor trafficking is discussed and the movement between the intracellular, extrasynaptic, and synaptic pools is examined, focusing on their involvement not only in basal synaptic function, but also in Hebbian and homeostatic plasticity.
Journal ArticleDOI

Mechanisms of MAGUK-mediated cellular junctional complex organization

TL;DR: The mechanistic basis governing target recognition and regulations of this binding by the PDZ-SH3-GK tandem of various MAGUKs are summarized.

Synaptic Trafficking of Glutamate Receptors by MAGUK Scaffolding Proteins in the Mammalian Hippocampus

TL;DR: These studies highlight the remarkable orchestration of AMPA-type glutamate receptor synaptic trafficking by multiple MAGUKs at different synapses within the same neuron and at different developmental stages.
Journal ArticleDOI

MPP2 is a postsynaptic MAGUK scaffold protein that links SynCAM1 cell adhesion molecules to core components of the postsynaptic density

TL;DR: A novel role for the membrane-associated guanylate kinase (MAGUK) protein MPP2 ( MAGUK p55 subfamily member 2) at synapses of rat central neurons is described as a scaffold that links SynCAM1 cell adhesion molecules to core proteins of the postsynaptic density.
Journal ArticleDOI

SK2 channel regulation of neuronal excitability, synaptic transmission, and brain rhythmic activity in health and diseases

TL;DR: This review highlights recent advances in the understanding of the regulation of SK2 channels and of their roles in normal brain functions, including synaptic plasticity, learning and memory, and rhythmic activities and discusses how alterations in their expression and regulation might contribute to various brain disorders.
References
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Journal ArticleDOI

Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95

TL;DR: The yeast two-hybrid system was used to show that the cytoplasmic tails of NMDA receptor subunits interact with a prominent postsynaptic density protein PSD-95, which may affect the plasticity of excitatory synapses.
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Subunit-specific rules governing AMPA receptor trafficking to synapses in hippocampal pyramidal neurons.

TL;DR: The combination of regulated addition and continuous replacement of synaptic receptors can stabilize long-term changes in synaptic efficacy and may serve as a general model for how surface receptor number is established and maintained.
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Perisynaptic Location of Metabotropic Glutamate Receptors mGluR1 and mGluR5 on Dendrites and Dendritic Spines in the Rat Hippocampus

TL;DR: It is proposed that glutamatergic synapses with an irregular edge develop in order to increase the circumference of synaptic junctions leading to an increase in the metabotropic to ionotropic glutamate receptor ratio at glutamate release sites.
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Direct interactions between PSD-95 and stargazin control synaptic AMPA receptor number

TL;DR: It is shown that AMPARs are localized to synapses through direct binding of the first two PDZ domains of synaptic PSD-95 (postsynaptic density protein of 95 kDa) to the AMPAR-associated protein, stargazin, and the central role of direct interactions between them in determining the number of synaptic AM PARs is demonstrated.
Journal ArticleDOI

The Shank family of scaffold proteins

TL;DR: The specific localization of Shank proteins at postsynaptic sites of brain excitatory synapses suggests a role for this family of proteins in the organization of cytoskeletal/ signaling complexes at specialized cell junctions.
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