Conservation and phylogenetic stepwise changes of aquaporin (AQP) 4 palmitoylation in vertebrate evolution

Hayashi, Takashi

doi:10.14800/nt.1608

Cited by 3 publications

(3 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Recent expansive progress in genome analyses revealed that many vertebrate species possess many neuronal receptor and ion channel orthologues (Chen et al, 2001;Chiu, DeSalle, Lam, Meisel, & Coruzzi, 1999;Okamura et al, 2005;Sprengel et al, 2001). Previous studies have shown that palmitoylation sites of AMPA receptors, NMDA receptors, KA receptors, and those of iGluRs-binding proteins, postsynaptic density-95 (PSD-95), glutamate receptor interacting protein 1b (GRIP1b), and protein interacting with C-kinase (PICK1), are extremely conserved in various species of whole vertebrates (Hayashi, 2014;Hayashi, 2015;. Generally speaking, structurally or functionally important amino acid residues are conserved during molecular evolution against mutation pressure.…”

Section: Evolution Of Iglurs Palmitoylationmentioning

confidence: 99%

Post‐translational palmitoylation of ionotropic glutamate receptors in excitatory synaptic functions

Hayashi

2020

British J Pharmacology

View full text Add to dashboard Cite

In the mammalian CNS, glutamate is the major excitatory neurotransmitter. Ionotropic glutamate receptors (iGluRs) are responsible for the glutamate‐mediated postsynaptic excitation of neurons. Regulation of glutamatergic synapses is critical for higher brain functions including neural communication, memory formation, learning, emotion, and behaviour. Many previous studies have shown that post‐translational protein S‐palmitoylation, the only reversible covalent attachment of lipid to protein, regulates synaptic expression, intracellular localization, and membrane trafficking of iGluRs and their scaffolding proteins in neurons. This modification mechanism is extremely conserved in the vertebrate lineages. The failure of appropriate palmitoylation‐dependent regulation of iGluRs leads to hyperexcitability that reduces the maintenance of network stability, resulting in brain disorders, such as epileptic seizures. This review summarizes advances in the study of palmitoylation of iGluRs, especially AMPA receptors and NMDA receptors, and describes the current understanding of palmitoylation‐dependent regulation of excitatory glutamatergic synapses. LINKED ARTICLES This article is part of a themed issue on Neurochemistry in Japan. To view the other articles in this section visit http://onlinelibrary.wiley.com/doi/10.1111/bph.v178.4/issuetoc

show abstract

Section: Evolution Of Iglurs Palmitoylationmentioning

confidence: 99%

Post‐translational palmitoylation of ionotropic glutamate receptors in excitatory synaptic functions

Hayashi

2020

British J Pharmacology

View full text Add to dashboard Cite

show abstract

“…Similarly, vertebrate-specific conservations of palmitoylation sites are also observed in other ion channels and neurotransmitter receptors (Borroni et al, 2016 ), such as HCN2 ( h yperpolarization-activated c yclic n ucleotide-gated channel 2) orthologs (Itoh et al, 2017 ), a water channel AQP4 ( aq ua p orin family protein 4) orthologs (Hayashi, 2017 ), and serotonin (chemically known as 5-hydroxytryptamine, 5-HT) receptors 5-HT 1A , 5-HT 4 , 5-HT 7 receptor orthologs (Kaizuka and Hayashi, 2018 ).…”

Section: Evolutionary Acquisition and Conservation Of Synaptic Palmitoylation In The Vertebrate Lineagementioning

confidence: 89%

Evolutionarily Established Palmitoylation-Dependent Regulatory Mechanisms of the Vertebrate Glutamatergic Synapse and Diseases Caused by Their Disruption

Hayashi

2021

Front. Mol. Neurosci.

View full text Add to dashboard Cite

Glutamate is the major excitatory neurotransmitter in the vertebrate brain and various modifications have been established in the glutamatergic synapses. Generally, many neuronal receptors and ion channels are regulated by S-palmitoylation, a reversible post-translational protein modification. Genome sequence databases show the evolutionary acquisition and conservation concerning vertebrate-specific palmitoylation of synaptic proteins including glutamate receptors. Moreover, palmitoylation of some glutamate receptor-binding proteins is subsequently acquired only in some mammalian lineages. Recent progress in genome studies has revealed that some palmitoylation-catalyzing enzymes are the causative genes of neuropsychiatric disorders. In this review, I will summarize the evolutionary development of palmitoylation-dependent regulation of glutamatergic synapses and their dysfunctions which are caused by the disruption of palmitoylation mechanism.

show abstract

“…Thus, AQP4 drives bidirectional water flow across the blood–brain barrier. Palmitoylation controls AQP4 spatial organization by inhibiting square formation and thereby impeding the constitution of a functional channel [ 43 ]. Further regulation governed by this modification is observed in sodium–calcium exchanger 1 (NCX1), playing a dual role.…”

Section: S -Palmitoylation Of Ion Channelsmentioning

confidence: 99%

Palmitoylation of Voltage-Gated Ion Channels

Cassinelli

Viñola-Renart

Benavente-Garcia

et al. 2022

IJMS

View full text Add to dashboard Cite

Protein lipidation is one of the most common forms of posttranslational modification. This alteration couples different lipids, such as fatty acids, phospho- and glycolipids and sterols, to cellular proteins. Lipidation regulates different aspects of the protein’s physiology, including structure, stability and affinity for cellular membranes and protein–protein interactions. In this scenario, palmitoylation is the addition of long saturated fatty acid chains to amino acid residues of the proteins. The enzymes responsible for this modification are acyltransferases and thioesterases, which control the protein’s behavior by performing a series of acylation and deacylation cycles. These enzymes target a broad repertoire of substrates, including ion channels. Thus, protein palmitoylation exhibits a pleiotropic role by differential modulation of the trafficking, spatial organization and electrophysiological properties of ion channels. Considering voltage-gated ion channels (VGICs), dysregulation of lipidation of both the channels and the associated ancillary subunits correlates with the development of various diseases, such as cancer or mental disorders. Therefore, a major role for protein palmitoylation is currently emerging, affecting not only the dynamism and differential regulation of a moiety of cellular proteins but also linking to human health. Therefore, palmitoylation of VGIC, as well as related enzymes, constitutes a novel pharmacological tool for drug development to target related pathologies.

show abstract

Conservation and phylogenetic stepwise changes of aquaporin (AQP) 4 palmitoylation in vertebrate evolution

Cited by 3 publications

References 31 publications

Post‐translational palmitoylation of ionotropic glutamate receptors in excitatory synaptic functions

Post‐translational palmitoylation of ionotropic glutamate receptors in excitatory synaptic functions

Evolutionarily Established Palmitoylation-Dependent Regulatory Mechanisms of the Vertebrate Glutamatergic Synapse and Diseases Caused by Their Disruption

Palmitoylation of Voltage-Gated Ion Channels

Contact Info

Product

Resources

About