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The C-terminal domains of the NMDA receptor: How intrinsically disordered tails affect signalling, plasticity and disease

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The C-terminal domains of the NMDA receptor : How intrinsically disordered tails affect signalling, plasticity and disease. / Warnet, Xavier L.; Bakke Krog, Helle; Sevillano-Quispe, Oscar G.; Poulsen, Hanne; Kjaergaard, Magnus.

In: European Journal of Neuroscience, 05.2020.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperReviewResearchpeer-review

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@article{825a46167b0a437aaff67886c2169b40,
title = "The C-terminal domains of the NMDA receptor: How intrinsically disordered tails affect signalling, plasticity and disease",
abstract = "NMDA receptors are part of the ionotropic glutamate receptor family, and are crucial for neurotransmission and memory. At the cellular level, the effects of activating these receptors include long-term potentiation (LTP) or depression (LTD). The NMDA receptor is a stringently gated cation channel permeable to Ca2+, and it shares the molecular architecture of a tetrameric ligand-gated ion channel with the other family members. Its subunits, however, have uniquely long cytoplasmic C-terminal domains (CTDs). While the molecular gymnastics of the extracellular domains have been described in exquisite detail, much less is known about the structure and function of these CTDs. The CTDs vary dramatically in length and sequence between receptor subunits, but they all have a composition characteristic of intrinsically disordered proteins. The CTDs affect channel properties, trafficking and downstream signalling output from the receptor, and these functions are regulated by alternative splicing, protein–protein interactions, and post-translational modifications such as phosphorylation and palmitoylation. Here, we review the roles of the CTDs in synaptic plasticity with a focus on biochemical mechanisms. In total, the CTDs play a multifaceted role as a modifier of channel function, a regulator of cellular location and abundance, and signalling scaffold control the downstream signalling output.",
keywords = "calcium signalling, glutamate receptor, postsynaptic density, signalling scaffold, synaptic plasticity",
author = "Warnet, {Xavier L.} and {Bakke Krog}, Helle and Sevillano-Quispe, {Oscar G.} and Hanne Poulsen and Magnus Kjaergaard",
year = "2020",
month = may,
doi = "10.1111/ejn.14842",
language = "English",
journal = "European Journal of Neuroscience",
issn = "0953-816X",
publisher = "Wiley-Blackwell Publishing Ltd.",

}

RIS

TY - JOUR

T1 - The C-terminal domains of the NMDA receptor

T2 - How intrinsically disordered tails affect signalling, plasticity and disease

AU - Warnet, Xavier L.

AU - Bakke Krog, Helle

AU - Sevillano-Quispe, Oscar G.

AU - Poulsen, Hanne

AU - Kjaergaard, Magnus

PY - 2020/5

Y1 - 2020/5

N2 - NMDA receptors are part of the ionotropic glutamate receptor family, and are crucial for neurotransmission and memory. At the cellular level, the effects of activating these receptors include long-term potentiation (LTP) or depression (LTD). The NMDA receptor is a stringently gated cation channel permeable to Ca2+, and it shares the molecular architecture of a tetrameric ligand-gated ion channel with the other family members. Its subunits, however, have uniquely long cytoplasmic C-terminal domains (CTDs). While the molecular gymnastics of the extracellular domains have been described in exquisite detail, much less is known about the structure and function of these CTDs. The CTDs vary dramatically in length and sequence between receptor subunits, but they all have a composition characteristic of intrinsically disordered proteins. The CTDs affect channel properties, trafficking and downstream signalling output from the receptor, and these functions are regulated by alternative splicing, protein–protein interactions, and post-translational modifications such as phosphorylation and palmitoylation. Here, we review the roles of the CTDs in synaptic plasticity with a focus on biochemical mechanisms. In total, the CTDs play a multifaceted role as a modifier of channel function, a regulator of cellular location and abundance, and signalling scaffold control the downstream signalling output.

AB - NMDA receptors are part of the ionotropic glutamate receptor family, and are crucial for neurotransmission and memory. At the cellular level, the effects of activating these receptors include long-term potentiation (LTP) or depression (LTD). The NMDA receptor is a stringently gated cation channel permeable to Ca2+, and it shares the molecular architecture of a tetrameric ligand-gated ion channel with the other family members. Its subunits, however, have uniquely long cytoplasmic C-terminal domains (CTDs). While the molecular gymnastics of the extracellular domains have been described in exquisite detail, much less is known about the structure and function of these CTDs. The CTDs vary dramatically in length and sequence between receptor subunits, but they all have a composition characteristic of intrinsically disordered proteins. The CTDs affect channel properties, trafficking and downstream signalling output from the receptor, and these functions are regulated by alternative splicing, protein–protein interactions, and post-translational modifications such as phosphorylation and palmitoylation. Here, we review the roles of the CTDs in synaptic plasticity with a focus on biochemical mechanisms. In total, the CTDs play a multifaceted role as a modifier of channel function, a regulator of cellular location and abundance, and signalling scaffold control the downstream signalling output.

KW - calcium signalling

KW - glutamate receptor

KW - postsynaptic density

KW - signalling scaffold

KW - synaptic plasticity

UR - http://www.scopus.com/inward/record.url?scp=85088024142&partnerID=8YFLogxK

U2 - 10.1111/ejn.14842

DO - 10.1111/ejn.14842

M3 - Review

C2 - 32464691

AN - SCOPUS:85088024142

JO - European Journal of Neuroscience

JF - European Journal of Neuroscience

SN - 0953-816X

ER -