Ion pore properties of ionotropic glutamate receptors are modulated by a transplanted potassium channel selectivity filter

Hoffmann, Jutta; Gorodetskaia, Anna; Hollmann, Michael

doi:10.1016/j.mcn.2006.08.006

Cited by 8 publications

(4 citation statements)

References 43 publications

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“…The prokaryotic GluR0 does have the TVGYG sequence and is K ϩ -selective (Chen et al, 1999a), but introduction of this sequence into mammalian glutamate receptor subunits does not confer K ϩ selectivity (Hoffmann et al, 2006a), probably because of different interactions of this region within the mammalian glutamate receptor compared with K ϩ channels. Indeed, in the membrane-spanning GluA2 structure, the extended region in the M2 loop is disordered, and this may reflect the absence of TVGYG and stabilizing interactions that underlie K ϩ selectivity in K ϩ channels.…”

Section: B Mechanisms Of Ion Permeationmentioning

confidence: 99%

Glutamate Receptor Ion Channels: Structure, Regulation, and Function

et al. 2010

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Section: B Mechanisms Of Ion Permeationmentioning

confidence: 99%

Glutamate Receptor Ion Channels: Structure, Regulation, and Function

et al. 2010

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“…However, although the iGluR6 LBD was shown to gate the sGluR0 pore, and the LBD of the NR1 NMDA receptor could gate several K + channel pore-loops (not including that of sGluR0), none of these was K + -selective39, indicating that selectivity depends on more than just the K + channel pore-loop. Furthermore, experiments showed that transplanting the GYG-motif to iGluRs did not render them K + -selective40. We therefore designed an alternative set of chimeras with the hope of obtaining coupling, while preserving K + selectivity.…”

Section: Resultsmentioning

confidence: 99%

A light-gated, potassium-selective glutamate receptor for the optical inhibition of neuronal firing

et al. 2010

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Genetically targeted light-activated ion channels and pumps make it possible to determine the role of specific neurons in neuronal circuits, information processing and behavior. Here, we describe the development of a K+-selective ionotropic glutamate receptor that reversibly inhibits neuronal activity in response to light in dissociated neurons and brain slice and reversibly suppresses behavior in zebrafish. The receptor is a chimera of the pore region of a K+-selective bacterial glutamate receptor and the ligand binding domain of the light-gated mammalian kainate receptor (iGluR6/GluK2). This hyperpolarizing light-gated channel, HyLighter, is turned on by a brief light pulse at one wavelength and turned off by a pulse at a second wavelength. The control is obtained at moderate intensity. After optical activation, the photo-current and optical silencing of activity persist in the dark for extended periods. The low light requirement and bi-stability of HyLighter represent advantages for the dissection of neural circuitry.

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“…In doing so, we exploited the modular design of iGluRs that allows for homologous domains to be interchanged between subunits from different subfamilies, conveying the properties of the donor domain to the accepting receptor. The feasibility of this domain-swapping approach has been shown before for other domains such as the pore region (Strutz-Seebohm et al, 2003; Hoffmann et al, 2006a,b; Tapken and Hollmann, 2008; Villmann et al, 2008) or the LBD (Schmid et al, 2009). …”

Section: Introductionmentioning

confidence: 81%

The Transmembrane Domain C of AMPA Receptors is Critically Involved in Receptor Function and Modulation

Terhag¹,

Gottschling²,

Hollmann³

2010

Front. Mol. Neurosci.

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Ionotropic glutamate receptors are major players in synaptic transmission and are critically involved in many cognitive events. Although receptors of different subfamilies serve different functions, they all show a conserved domain topology. For most of these domains, structure–function relationships have been established and are well understood. However, up to date the role of the transmembrane domain C in receptor function has been investigated only poorly. We have constructed a series of receptor chimeras and point mutants designed to shed light on the structural and/or functional importance of this domain. We here present evidence that the role of transmembrane domain C exceeds that of a mere scaffolding domain and that several amino acid residues located within the domain are crucial for receptor gating and desensitization. Furthermore, our data suggest that the domain may be involved in receptor interaction with transmembrane AMPA receptor regulatory proteins.

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Ion pore properties of ionotropic glutamate receptors are modulated by a transplanted potassium channel selectivity filter

Cited by 8 publications

References 43 publications

Glutamate Receptor Ion Channels: Structure, Regulation, and Function

Glutamate Receptor Ion Channels: Structure, Regulation, and Function

A light-gated, potassium-selective glutamate receptor for the optical inhibition of neuronal firing

The Transmembrane Domain C of AMPA Receptors is Critically Involved in Receptor Function and Modulation

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