Please use this identifier to cite or link to this item: http://hdl.handle.net/2445/104026
Title: AMPAR interacting protein CPT1C enhances surface expression of GluA1-containing receptors
Author: Gratacòs i Batlle, Esther
Yefimenko Nosova, Natalia
Casco García, Helena
Soto del Cerro, David
Keywords: Sinapsi
Receptors de neurotransmissors
Neurones
Electrofisiologia
Neurobiologia
Synapses
Neurotransmitter receptors
Neurons
Electrophysiology
Neurobiology
Issue Date: 2-Feb-2015
Publisher: Frontiers Media
Abstract: AMPARs mediate the vast majority of fast excitatory synaptic transmission in the brain and their biophysical and trafficking properties depend on their subunit composition and on several posttranscriptional and posttranslational modifications. Additionally, in the brain AMPARs associate with auxiliary subunits, which modify the properties of the receptors. Despite the abundance of AMPAR partners, recent proteomic studies have revealed even more interacting proteins that could potentially be involved in AMPAR regulation. Amongst these, carnitine palmitoyltransferase 1C (CPT1C) has been demonstrated to form an integral part of native AMPAR complexes in brain tissue extracts. Thus, we aimed to investigate whether CPT1C might be able to modulate AMPAR function. Firstly, we confirmed that CPT1C is an interacting protein of AMPARs in heterologous expression systems. Secondly, CPT1C enhanced whole-cell currents of GluA1 homomeric and GluA1/GluA2 heteromeric receptors. However, CPT1C does not alter the biophysical properties of AMPARs and co-localization experiments revealed that AMPARs and CPT1C are not associated at the plasma membrane despite a strong level of co-localization at the intracellular level. We established that increased surface GluA1 receptor number was responsible for the enhanced AMPAR mediated currents in the presence of CPT1C. Additionally, we revealed that the palmitoylable residue C585 of GluA1 is important in the enhancement of AMPAR trafficking to the cell surface by CPT1C. Nevertheless, despite its potential as a depalmitoylating enzyme, CPT1C does not affect the palmitoylation state of GluA1. To sum up, this work suggests that CPT1C plays a role as a novel regulator of AMPAR surface expression in neurons. Fine modulation of AMPAR membrane trafficking is fundamental in normal synaptic activity and in plasticity processes and CPT1C is therefore a putative candidate to regulate neuronal AMPAR physiology.
Note: Reproducció del document publicat a: https://doi.org/10.3389/fncel.2014.00469
It is part of: Frontiers in Cellular Neuroscience, 2015, vol. 8, p. 469
Related resource: https://doi.org/10.3389/fncel.2014.00469
URI: http://hdl.handle.net/2445/104026
ISSN: 1662-5102
Appears in Collections:Articles publicats en revistes (Biomedicina)

Files in This Item:
File Description SizeFormat 
660295.pdf6.59 MBAdobe PDFView/Open


This item is licensed under a Creative Commons License Creative Commons