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AMPA receptor

The α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic
acid receptor (also known as AMPA receptor, AMPAR,
or quisqualate receptor) is an ionotropic transmembrane
receptor for glutamate that mediates fast synaptic
transmission in the central nervous system (CNS). It has
been traditionally classified as a non-NMDA-type receptor,
along with the kainate receptor. Its name is derived from its
ability to be activated by the artificial glutamate analog
AMPA. The receptor was first named the "quisqualate
receptor" by Watkins and colleagues after a naturally
occurring agonist quisqualate and was only later given the
label "AMPA receptor" after the selective agonist
developed by Tage Honore and colleagues at the Royal
Danish School of Pharmacy in Copenhagen.[1] AMPARs
are found in many parts of the brain and are the most
commonly found receptor in the nervous system. The
AMPA receptor GluA2 (GluR2) tetramer was the first
glutamate receptor ion channel to becrystallized. The AMPA receptor bound to a glutamate antagonist
showing the amino terminal, ligand binding, and
transmembrane domain, PDB 3KG2

Contents
Structure and function
Subunit composition
Ion channel function
Synaptic plasticity
AMPA receptor trafficking
Molecular and signaling response to
LTP-inducing stimuli
AMPA receptor trafficking to the PSD in
response to LTP
Constitutive trafficking and changes in
subunit composition
LTD-induced endocytosis of AMPA
receptors
Role in Seizures
Molecular target for epilepsy therapy
Agonists
Positive allosteric modulators
Antagonists
Negative allosteric modulators
See also
References
External links
Structure and function

Subunit composition
AMPARs are composed of four types of subunits, designated as GluA1 (GRIA1), GluA2 (GRIA2), GluA3 (GRIA3), and GluA4,
alternatively called GluRA-D2 (GRIA4), which combine to form tetramers.[2][3][4] Most AMPARs are heterotetrameric, consisting of
symmetric 'dimer of dimers' of GluA2 and either GluA1, GluA3 or GluA4.[5][6] Dimerization starts in the endoplasmic reticulum
with the interaction of N-terminal LIVBP domains, then "zips up" through the ligand-binding domain into the transmembrane ion
pore.[6]

The conformation of the subunit protein in the plasma membrane caused controversy for some time. While the amino acid sequence
of the subunit indicated that there seemed to be four transmembrane domains (parts of the protein that pass through the plasma
membrane), proteins interacting with the subunit indicated that the N-terminus seemed to be extracellular, while the C-terminus
seemed to be intracellular. However, if each of the four transmembrane domains wentall the way through the plasma membrane, then
the two termini would have to be on the same side of the membrane. It was eventually discovered that the second "transmembrane"
domain does not in fact cross the membrane at all, but kinks back on itself within the membrane and returns to the intracellular
side.[7] When the four subunits of the tetramer come together, this second membranous domain forms the ion-permeable pore of the
receptor.

AMPAR subunits differ most in their C-terminal sequence, which determines their interactions with scaffolding proteins. All
AMPARs contain PDZ-binding domains, but which PDZ domain they bind to differs. For example, GluA1 binds to SAP97 through
SAP97's class I PDZ domain,[8] while GluA2 binds to PICK1[9] and GRIP/ABP. Of note, AMPARs cannot directly bind to the
common synaptic protein PSD-95 owing to incompatible PDZ domains, although they do interact with PSD-95 via stargazin (the
prototypical member of the TARP family of AMPAR auxiliary subunits).[10]

Phosphorylation of AMPARs can regulate channel localization, conductance, and open probability. GluA1 has four known
phosphorylation sites at serine 818 (S818), S831, threonine 840, and S845 (other subunits have similar phosphorylation sites, but
GluR1 has been the most extensively studied). S818 is phosphorylated by protein kinase C, and is necessary for long-term
potentiation (LTP; for GluA1's role in LTP, see below).[11] S831 is phosphorylated by CaMKII and PKC during LTP, which helps
deliver GluA1-containing AMPAR to the synapse,[12] and increases their single channel conductance.[13] The T840 site was more
recently discovered, and has been implicated in LTD.[14] Finally, S845 is phosphorylated by PKA which regulates its open
probability.[15]

Ion channel function


Each AMPAR has four sites to which an agonist (such as glutamate) can bind, one for each subunit.[5] The binding site is believed to
be formed by the N-terminal tail and the extracellular loop between transmembrane domains three and four.[16] When an agonist
binds, these two loops move towards each other, opening the pore. The channel opens when two sites are occupied,[17] and increases
its current as more binding sites are occupied.[18] Once open, the channel may undergo rapid desensitization, stopping the current.
The mechanism of desensitization is believed to be due to a small change in angle of one of the parts of the binding site, closing the
pore.[19] AMPARs open and close quickly (1ms), and are thus responsible for most of the fast excitatory synaptic transmission in the
central nervous system.[17] The AMPAR's permeability to calcium and other cations, such as sodium and potassium, is governed by
the GluA2 subunit. If an AMPAR lacks a GluA2 subunit, then it will be permeable to sodium, potassium, and calcium. The presence
of a GluA2 subunit will almost always render the channel impermeable to calcium. This is determined by post-transcriptional
modification — RNA editing — of the Q-to-R editing site of the GluA2 mRNA. Here, A→I editing alters the uncharged amino acid
glutamine (Q) to the positively charged arginine (R) in the receptor's ion channel. The positively charged amino acid at the critical
point makes it energetically unfavourable for calcium to enter the cell through the pore. Almost all of the GluA2 subunits in CNS are
edited to the GluA2(R) form. This means that the principal ions gated by AMPARs are sodium and potassium, distinguishing
AMPARs from NMDA receptors (the other main ionotropic glutamate receptors in the brain), which also permit calcium influx. Both
AMPA and NMDA receptors, however, have an equilibrium potential near 0 mV. The prevention of calcium entry into the cell on
activation of GluA2-containing AMPARs is proposed to guard against excitotoxicity.[20]

The subunit composition of the AMPAR is also important for the way this receptor is modulated. If an AMPAR lacks GluA2
subunits, then it is susceptible to being blocked in a voltage-dependent manner by a class of molecules called polyamines. Thus,
when the neuron is at a depolarized membrane potential, polyamines will block the AMPAR channel more strongly, preventing the
flux of potassium ions through the channel pore. GluA2-lacking AMPARs are, thus, said to have an inwardly rectifying I/V curve,
which means that they pass less outward current than inward current at equivalent distance from the reversal potential. Calcium
permeable AMPARs are found typically early during postnatal development, on some interneurons or in dopamine neurons of the
[VTA] after the exposure to an addictive drug.[21]

Alongside RNA editing, alternative splicing allows a range of functional AMPA receptor subunits beyond what is encoded in the
genome. In other words, although one gene (GRIA1–GRIA4) is encoded for each subunit (GluA1–GluA4), splicing after transcription
from DNA allows some exons to be translated interchangeably, leading to several functionally different subunits from each gene.

The flip/flop sequence is one such interchangeable exon. A 38-amino acid sequence found prior to (i.e., before the N-terminus of) the
fourth membranous domain in all four AMPAR subunits, it determines the speed of desensitisation[22] of the receptor and also the
speed at which the receptor is resensitised[23] and the rate of channel closing.[24] The flip form is present in prenatal AMPA receptors
[25]
and gives a sustained current in response to glutamate activation.

Synaptic plasticity
AMPA receptors (AMPAR) are both glutamate receptors and cation channels that are integral to plasticity and synaptic transmission
at many postsynaptic membranes. One of the most widely and thoroughly investigated forms of plasticity in the nervous system is
known as long-term potentiation, or LTP. There are two necessary components of LTP: presynaptic glutamate release and
postsynaptic depolarization. Therefore, LTP can be induced experimentally in a paired electrophysiological recording when a
presynaptic cell is stimulated to release glutamate on a postsynaptic cell that is depolarized. The typical LTP induction protocol
involves a “tetanus” stimulation, which is a 100 Hz stimulation for 1 second. When one applies this protocol to a pair of cells, one
will see a sustained increase of the amplitude of the EPSP following tetanus. This response is interesting since it is thought to be the
physiological correlate for learning and memory in the cell. In fact, it was recently shown that, following a single paired-avoidance
paradigm in mice, LTP could be recorded in somehippocampal synapses in vivo.[26]

The molecular basis for LTP has been extensively studied, and AMPARs have been shown to play an integral role in the process.
Both GluR1 and GluR2 play an important role in synaptic plasticity. It is now known that the underlying physiological correlate for
the increase in EPSP size is a postsynaptic upregulation of AMPARs at the membrane,[27] which is accomplished through the
interactions of AMPARs with many cellular proteins.

The simplest explanation for LTP is as follows (see the long-term potentiation article for a much more detailed account). Glutamate
binds to postsynaptic AMPARs and another glutamate receptor, the NMDA receptor (NMDAR). Ligand binding causes the AMPARs
to open, and Na+ flows into the postsynaptic cell, resulting in a depolarization. NMDARs, on the other hand, do not open directly
because their pores are occluded at resting membrane potential by Mg2+ ions. NMDARs can open only when a depolarization from
the AMPAR activation leads to repulsion of the Mg2+ cation out into the extracellular space, allowing the pore to pass current. Unlike
AMPARs, however, NMDARs are permeable to both Na+ and Ca2+. The Ca2+ that enters the cell triggers the upregulation of
AMPARs to the membrane, which results in a long-lasting increase in EPSP size underlying LTP. The calcium entry also
phosphorylates CaMKII, which phosphorylates AMPARs, increasing their single-channel conductance.

AMPA receptor trafficking

Molecular and signaling response to L


TP-inducing stimuli
The mechanism for LTP has long been a topic of debate, but,
recently, mechanisms have come to some consensus. AMPARs
play a key role in this process, as one of the key indicators of
LTP induction is the increase in the ratio of AMPAR to
NMDARs following high-frequency stimulation. The idea is that
AMPARs are trafficked from the dendrite into the synapse and
incorporated through some series of signaling cascades.

AMPARs are initially regulated at the transcriptional level at


their 5’ promoter regions. There is significant evidence pointing
towards the transcriptional control of AMPA receptors in longer-
term memory through cAMP response element-binding protein
(CREB) and Mitogen-activated protein kinases (MAPK).[28]
Regulation of AMPAR trafficking to the postsynaptic Messages are translated on the rough endoplasmic reticulum
density in response to LTP-inducing stimuli (rough ER) and modified there. Subunit compositions are
determined at the time of modification at the rough ER.[9] After
post-ER processing in the golgi apparatus, AMPARs are released
into the perisynaptic membrane as a reserve waiting for the T
LP process to be initiated.

The first key step in the process following glutamate binding to NMDARs is the influx of calcium through the NMDA receptors and
the resultant activation of Ca2+/calmodulin-dependent protein kinase (CaMKII).[29] Blocking either this influx or the activation of
CaMKII prevents LTP, showing that these are necessary mechanisms for LTP.[30] In addition, profusion of CaMKII into a synapse
causes LTP, showing that it is a causal and sufficient mechanism.[31]

CaMKII has multiple modes of activation to cause the incorporation of AMPA receptors into the perisynaptic membrane. CAMKII
enzyme is eventually responsible for the development of the actin cytoskeleton of neuronal cells and, eventually, for the dendrite and
axon development (synaptic plasticity).[32] The first is direct phosphorylation of synaptic-associated protein 97(SAP97).[33] First,
SAP-97 and Myosin-VI, a motor protein, are bound as a complex to the C-terminus of AMPARs. Following phosphorylation by
CaMKII, the complex moves into the perisynaptic membrane.[34] The second mode of activation is through the MAPK pathway.
CaMKII activates the Ras proteins, which go on to activate p42/44 MAPK, which drives AMPAR insertion directly into the
perisynaptic membrane.[35]

AMPA receptor trafficking to the PSD in response to LTP


Once AMPA receptors are transported to the perisynaptic region through PKA or SAP97 phosphorylation, receptors are then
trafficked to the postsynaptic density (PSD). However, this process of trafficking to the PSD still remains controversial. One
possibility is that, during LTP, there is lateral movement of AMPA receptors from perisynpatic sites directly to the PSD.[36] Another
possibility is that exocytosis of intracellular vesicles is responsible for AMPA trafficking to the PSD directly.[37] Recent evidence
suggests that both of these processes are happening after an LTP stimulus; however, only the lateral movement of AMPA receptors
from the perisynaptic region enhances the number of AMPA receptors at the PSD.[38] The exact mechanism responsible for lateral
movement of AMPA receptors to the PSD remains to be discovered; however, research has discovered several essential proteins for
AMPA receptor trafficking. For example, overexpression of SAP97 leads to increased AMPA receptor trafficking to synapses.[39] In
addition to influencing synaptic localization, SAP97 has also been found to influence AMPA receptor conductance in response to
glutamate.[40] Myosin proteins are calcium sensitive motor proteins that have also been found to be essential for AMPA receptor
trafficking. Disruption of myosin Vb interaction with Rab11 and Rab11-FIP2 blocks spine growth and AMPA receptor trafficking.[41]
Therefore, it is possible that myosin may drive the lateral movement of AMPA receptors in the perisynpatic region to the PSD.
Transmembrane AMPA receptor regulatory proteins (TARPs) are a family proteins that associate with AMPA receptors and control
their trafficking and conductance.[42] CACNG2 (Stargazin) is one such protein and is found to bind AMPA receptors in the
perisynaptic and postsynaptic regions.[43] The role of stargazin in trafficking between the perisynaptic and postsynaptic regions
remains unclear; however, stargazin is essential for immobilizing AMPA receptors in the PSD by interacting with PSD-95.[44] PSD-
[45]
95 stabilizes AMPA receptors to the synapse anddisruption of the stargazin-PSD-95 interaction suppressed synaptic transmission.
Constitutive trafficking and changes in subunit composition
AMPA receptors are continuously being trafficked (endocytosed, recycled, and reinserted) into and out of the plasma membrane.
Recycling endosomes within the dendritic spine contain pools of AMPA receptors for such synaptic reinsertion.[46] Two distinct
.[47][48]
pathways exist for the trafficking of AMPA receptors: a regulated pathway and a constitutive pathway

In the regulated pathway, GluA1-containing AMPA receptors are trafficked to the synapse in an activity-dependent manner,
stimulated by NMDA receptor activation.[12] Under basal conditions, the regulated pathway is essentially inactive, being transiently
activated only upon the induction of long-term potentiation.[46][47] This pathway is responsible for synaptic strengthening and the
initial formation of new memories.[49]

In the constitutive pathway, GluA1-lacking AMPA receptors, usually GluR2-GluR3 heteromeric receptors, replace the GluA1-
containing receptors in a one-for-one, activity-independent manner,[50][51] preserving the total number of AMPA receptors in the
synapse.[46][47] This pathway is responsible for the maintenance of new memories, sustaining the transient changes resulting from
the regulated pathway. Under basal conditions, this pathway is routinely active, as it is necessary also for the replacement of damaged
receptors.

The GluA1 and GluA4 subunits consist of a long carboxy (C)-tail, whereas the GluA2 and GluA3 subunits consist of a short carboxy-
tail. The two pathways are governed by interactions between the C termini of the AMPA receptor subunits and synaptic compounds
and proteins. Long C-tails prevent GluR1/4 receptors from being inserted directly into the postsynaptic density zone (PSDZ) in the
absence of activity, whereas the short C-tails of GluA2/3 receptors allow them to be inserted directly into the PSDZ.[36][52] The
GluA2 C terminus interacts with and binds to N-ethylmaleimide sensitive fusion protein,[53][54][55] which allows for the rapid
insertion of GluR2-containing AMPA receptors at the synapse.[56] In addition, GluR2/3 subunits are more stably tethered to the
synapse than GluR1 subunits.[57][58][59]

LTD-induced endocytosis of AMPA receptors


Long-term depression enacts mechanisms to decrease
AMPA receptor density in selected dendritic spines,
dependent on clathrin and calcineurin and distinct
from that of constitutive AMPAR trafficking. The
starting signal for AMPAR endocytosis is an
NMDAR-dependent calcium influx from low-
frequency stimulation, which in turn activates protein
phosphatases PP1 and calcineurin. However, AMPAR
endocytosis has also been activated by voltage-
dependent calcium channels, agonism of AMPA
receptors, and administration of insulin, suggesting LTD-induced endocytosis of AMPA receptors
general calcium influx as the cause of AMPAR
endocytosis.[60] Blockage of PP1 did not prevent
[61]
AMPAR endocytosis, but antagonist application ot calcineurin led to significant inhibition of this process.

Calcineurin interacts with an endocytotic complex at the postsynaptic zone, explaining its effects on LTD.[62] The complex,
consisting of a clathrin-coated pit underneath a section of AMP
AR-containing plasma membrane and interacting proteins, is the direct
mechanism for reduction of AMPARs, in particular GluR2/GluR3 subunit-containing receptors, in the synapse. Interactions from
calcineurin activate dynamin GTPase activity, allowing the clathrin pit to excise itself from the cell membrane and become a
cytoplasmic vesicle.[63] Once the clathrin coat detaches, other proteins can interact directly with the AMPARs using PDZ carboxyl
tail domains; for example, glutamate receptor-interacting protein 1 (GRIP1) has been implicated in intracellular sequestration of
AMPARs.[64] Intracellular AMPARs are subsequently sorted for degradation by lysosomes or recycling to the cell membrane.[65] For
the latter, PICK1 and PKC can displace GRIP1 to return AMPARs to the surface, reversing the effects of endocytosis and LTD. when
appropriate.[66] Nevertheless, the highlighted calcium-dependent, dynamin-mediated mechanism above has been implicated as a key
component of LTD. and as such may have applications to further behavioral research.[67]
Role in Seizures
AMPA receptors play a key role in the generation and spread of epileptic seizures.[68] Kainic acid, a convulsant that is widely used in
A receptors [69]
epilepsy research induces seizures, in part, via activation of AMP

Molecular target for epilepsy therapy


The noncompetitive AMPA receptor antagoniststalampanel and perampanel have been demonstrated to have activity in the treatment
of adults with partial seizures,[70][71] indicating that AMPA receptor antagonists represent a potential target for the treatment of
epilepsy.[72] [73] Perampanel (trade name: Fycompa) received Marketing Authorisation Approval by the European Commission for
the treatment of partial epilepsy on July 27, 2012. The drug was approved in the United States by the Food and Drug Administration
(FDA) on October 22, 2012. As has been the case for most recently developed AEDs including pregabalin, lacosamide and
ezogabine, the FDA recommended that perampanel be classified by the Drug Enforcement Administration (DEA) as a scheduled
drug. It has been designated as a Schedule 3 controlled substance.

Decanoic acid acts as a non-competitive AMPA receptor antagonist at therapeutically relevant concentrations, in a voltage- and
subunit-dependent manner, and this is sufficient to explain its antiseizure effects.[74] This direct inhibition of excitatory
neurotransmission by decanoic acid in the brain contributes to the anticonvulsant effect of the medium-chain triglyceride ketogenic
diet.[74] Decanoic acid and the AMPA receptor antagonist drug perampanel act at separate sites on the AMPA receptor, and so it is
possible that they have a cooperative effect at the AMPA receptor, suggesting that perampanel and the ketogenic diet could be
synergistic.[74]

Preclinical research suggest that several derivatives of aromatic amino acids with antiglutamatergic properties including AMPA
receptor antagonism and inhibition of glutamate release such as 3,5-dibromo-D-tyrosine and 3,5-dibromo-L-phenylalnine exhibit
[75][76]
strong anticonvulsant effect in animal models suggesting use of these compounds as a novel class of antiepileptic drugs.

Agonists
5-Fluorowillardiine – a synthetic modification ofwillardiine
AMPA – a synthetic agonist after which the receptor is named
Domoic acid – a naturally occurring agonist that causesamnesic shellfish
poisoning
Glutamic acid (glutamate) – the endogenous agonist
Ibotenic acid – a naturally occurring agonist found inAmanita muscaria
Quisqualic acid – a naturally occurring agonist found in certain species
Willardiine – a naturally occurring agonist

Glutamate, the endogenous


Positive allosteric modulators agonist of the AMPAR.

Aniracetam Farampator (CX-691, Oxiracetam


Cyclothiazide ORG-24448) PEPA
CX-516 IDRA-21 PF-04958242
CX-546 LY-404187 Piracetam
CX-614 LY-503430[77][78] Pramiracetam
CX-717 Mibampator (LY- Tulrampator (S-
451395) 47445, CX-1632)
ORG-26576

AMPA, a synthetic agonist of


Antagonists the AMPAR.

Becampanel
CNQX
Dasolampanel
DNQX
DNQX
Fanapanel (MPQX)
Kaitocephalin
Kynurenic acid – endogenous ligand
NBQX
L-phenylalanine[79]
3,5-Dibromo-L-phenylalanine, a naturally occurring halogenated derivative of
Selurampanel
Tezampanel
Zonampanel

Negative allosteric modulators


Barbiturates (e.g., pentobarbital, sodium thiopental) – non-selective
Ethanol – non-selective
Inhalational anaesthetics(e.g., cyclopropane, enflurane, halothane, isoflurane,
sevoflurane) – non-selective
GYKI-52466
Irampanel
Perampanel
Talampanel

See also Perampanel, a negative


allosteric modulator of the
Arc/Arg3.1 AMPAR used to treat
epilepsy.

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External links
AMPA receptors - pharmacology
Drosophila Glutamate receptor IIA- The Interactive Fly

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