Auxiliary proteins promote modal gating of AMPA‐ and kainate‐type glutamate receptors. (April 2014)
- Record Type:
- Journal Article
- Title:
- Auxiliary proteins promote modal gating of AMPA‐ and kainate‐type glutamate receptors. (April 2014)
- Main Title:
- Auxiliary proteins promote modal gating of AMPA‐ and kainate‐type glutamate receptors
- Authors:
- Zhang, Wei
Devi, Suma Priya Sudarsana
Tomita, Susumu
Howe, James R. - Abstract:
- <abstract abstract-type="main" id="ejn12519-abs-0001"> <title>Abstract</title> <p>The gating behavior of α‐amino‐3‐hydroxy‐5‐methyl‐4‐isoxazolepropionic acid (AMPA) and kainate receptors is modulated by association with the auxiliary proteins: transmembrane AMPA receptor regulatory proteins (TARPs) and neuropilin tolloid‐like (Netos), respectively. Although the mechanisms underlying receptor modulation differ for both AMPA and kainate receptors, association with these auxiliary subunits results in the appearance of a slow component in the decay of ensemble responses to rapid applications of saturating concentrations of glutamate. We show here that these components arise from distinct gating behaviors, characterized by substantially higher open probability (<italic>P</italic><sub>open</sub>), which we only observe when core subunits are associated with their respective auxiliary partners. We refer to these behaviors as gating modes, because individual receptors switch between the low‐ and high‐<italic>P</italic><sub>open</sub> gating on a time‐scale of seconds. At any given time, association of AMPA and kainate receptors with their auxiliary subunits results in a heterogeneous receptor population, some of which are in the high‐<italic>P</italic><sub>open</sub> mode and others that display gating behavior similar to that seen for receptors formed from core subunits alone. While the switching between modes is infrequent, the presence of receptors displaying both types of gating<abstract abstract-type="main" id="ejn12519-abs-0001"> <title>Abstract</title> <p>The gating behavior of α‐amino‐3‐hydroxy‐5‐methyl‐4‐isoxazolepropionic acid (AMPA) and kainate receptors is modulated by association with the auxiliary proteins: transmembrane AMPA receptor regulatory proteins (TARPs) and neuropilin tolloid‐like (Netos), respectively. Although the mechanisms underlying receptor modulation differ for both AMPA and kainate receptors, association with these auxiliary subunits results in the appearance of a slow component in the decay of ensemble responses to rapid applications of saturating concentrations of glutamate. We show here that these components arise from distinct gating behaviors, characterized by substantially higher open probability (<italic>P</italic><sub>open</sub>), which we only observe when core subunits are associated with their respective auxiliary partners. We refer to these behaviors as gating modes, because individual receptors switch between the low‐ and high‐<italic>P</italic><sub>open</sub> gating on a time‐scale of seconds. At any given time, association of AMPA and kainate receptors with their auxiliary subunits results in a heterogeneous receptor population, some of which are in the high‐<italic>P</italic><sub>open</sub> mode and others that display gating behavior similar to that seen for receptors formed from core subunits alone. While the switching between modes is infrequent, the presence of receptors displaying both types of gating has a large impact on both the kinetics and amplitude of ensemble currents similar to those seen at synapses.</p> </abstract> … (more)
- Is Part Of:
- European journal of neuroscience. Volume 39:Number 7(2014:Apr.)
- Journal:
- European journal of neuroscience
- Issue:
- Volume 39:Number 7(2014:Apr.)
- Issue Display:
- Volume 39, Issue 7 (2014)
- Year:
- 2014
- Volume:
- 39
- Issue:
- 7
- Issue Sort Value:
- 2014-0039-0007-0000
- Page Start:
- 1138
- Page End:
- 1147
- Publication Date:
- 2014-04
- Subjects:
- Nervous system -- Periodicals
612.8 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1460-9568 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/ejn.12519 ↗
- Languages:
- English
- ISSNs:
- 0953-816X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3829.731700
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 4268.xml