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Mechanisms of CPT1C-Dependent AMPAR Trafficking Enhancement

Overview of attention for article published in Frontiers in Molecular Neuroscience, August 2018
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Title
Mechanisms of CPT1C-Dependent AMPAR Trafficking Enhancement
Published in
Frontiers in Molecular Neuroscience, August 2018
DOI 10.3389/fnmol.2018.00275
Pubmed ID
Authors

Esther Gratacòs-Batlle, Mireia Olivella, Nuria Sánchez-Fernández, Natalia Yefimenko, Federico Miguez-Cabello, Rut Fadó, Núria Casals, Xavier Gasull, Santiago Ambrosio, David Soto

Abstract

In neurons, AMPA receptor (AMPAR) function depends essentially on their constituent components:the ion channel forming subunits and ion channel associated proteins. On the other hand, AMPAR trafficking is tightly regulated by a vast number of intracellular neuronal proteins that bind to AMPAR subunits. It has been recently shown that the interaction between the GluA1 subunit of AMPARs and carnitine palmitoyltransferase 1C (CPT1C), a novel protein partner of AMPARs, is important in modulating surface expression of these ionotropic glutamate receptors. Indeed, synaptic transmission in CPT1C knockout (KO) mice is diminished supporting a positive trafficking role for that protein. However, the molecular mechanisms of such modulation remain unknown although a putative role of CPT1C in depalmitoylating GluA1 has been hypothesized. Here, we explore that possibility and show that CPT1C effect on AMPARs is likely due to changes in the palmitoylation state of GluA1. Based on in silico analysis, Ser 252, His 470 and Asp 474 are predicted to be the catalytic triad responsible for CPT1C palmitoyl thioesterase (PTE) activity. When these residues are mutated or when PTE activity is inhibited, the CPT1C effect on AMPAR trafficking is abolished, validating the CPT1C catalytic triad as being responsible for PTE activity on AMPAR. Moreover, the histidine residue (His 470) of CPT1C is crucial for the increase in GluA1 surface expression in neurons and the H470A mutation impairs the depalmitoylating catalytic activity of CPT1C. Finally, we show that CPT1C effect seems to be specific for this CPT1 isoform and it takes place solely at endoplasmic reticulum (ER). This work adds another facet to the impressive degree of molecular mechanisms regulating AMPAR physiology.

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The data shown below were collected from the profiles of 3 tweeters who shared this research output. Click here to find out more about how the information was compiled.

Mendeley readers

The data shown below were compiled from readership statistics for 24 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 24 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 8 33%
Researcher 6 25%
Professor 1 4%
Student > Bachelor 1 4%
Student > Doctoral Student 1 4%
Other 2 8%
Unknown 5 21%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 7 29%
Neuroscience 6 25%
Medicine and Dentistry 2 8%
Agricultural and Biological Sciences 1 4%
Arts and Humanities 1 4%
Other 0 0%
Unknown 7 29%

Attention Score in Context

This research output has an Altmetric Attention Score of 2. 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 08 October 2018.
All research outputs
#10,834,901
of 17,370,809 outputs
Outputs from Frontiers in Molecular Neuroscience
#1,141
of 2,001 outputs
Outputs of similar age
#162,039
of 285,030 outputs
Outputs of similar age from Frontiers in Molecular Neuroscience
#47
of 83 outputs
Altmetric has tracked 17,370,809 research outputs across all sources so far. This one is in the 35th percentile – i.e., 35% of other outputs scored the same or lower than it.
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