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AMPAR interacting protein CPT1C enhances surface expression of GluA1-containing receptors

Overview of attention for article published in Frontiers in Cellular Neuroscience, February 2015
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Title
AMPAR interacting protein CPT1C enhances surface expression of GluA1-containing receptors
Published in
Frontiers in Cellular Neuroscience, February 2015
DOI 10.3389/fncel.2014.00469
Pubmed ID
Authors

Esther Gratacòs-Batlle, Natalia Yefimenko, Helena Cascos-García, David Soto

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.

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Mendeley readers

The data shown below were compiled from readership statistics for 51 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 51 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 13 25%
Researcher 11 22%
Student > Master 6 12%
Student > Bachelor 4 8%
Professor 4 8%
Other 7 14%
Unknown 6 12%
Readers by discipline Count As %
Agricultural and Biological Sciences 14 27%
Biochemistry, Genetics and Molecular Biology 12 24%
Neuroscience 12 24%
Psychology 1 2%
Medicine and Dentistry 1 2%
Other 3 6%
Unknown 8 16%

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 24 February 2015.
All research outputs
#2,548,584
of 4,800,224 outputs
Outputs from Frontiers in Cellular Neuroscience
#544
of 946 outputs
Outputs of similar age
#81,113
of 146,009 outputs
Outputs of similar age from Frontiers in Cellular Neuroscience
#25
of 33 outputs
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So far Altmetric has tracked 946 research outputs from this source. They receive a mean Attention Score of 2.8. This one is in the 31st percentile – i.e., 31% of its peers scored the same or lower than it.
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