Phosphorylation Induces Conformational Rigidity at the C-Terminal Domain of AMPA Receptors.
Journal
The journal of physical chemistry. B
ISSN: 1520-5207
Titre abrégé: J Phys Chem B
Pays: United States
ID NLM: 101157530
Informations de publication
Date de publication:
10 01 2019
10 01 2019
Historique:
pubmed:
13
12
2018
medline:
2
6
2020
entrez:
13
12
2018
Statut:
ppublish
Résumé
The intracellular C-terminal domain (CTD) of AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor undergoes phosphorylation at specific locations during long-term potentiation. This modification enhances conductance through the AMPA receptor ion channel and thus potentially plays a crucial role in modulating receptor trafficking and signaling. However, because the CTD structure is largely unresolved, it is difficult to establish if phosphorylation induces conformational changes that might play a role in enhancing channel conductance. Herein, we utilize single-molecule Förster resonance energy transfer (smFRET) spectroscopy to probe the conformational changes of a section of the AMPA receptor CTD, under the conditions of point-mutated phosphomimicry. Multiple analysis algorithms fail to identify stable conformational states within the smFRET distributions, consistent with a lack of well-defined secondary structure. Instead, our results show that phosphomimicry induces conformational rigidity to the CTD, and such rigidity is electrostatically tunable.
Identifiants
pubmed: 30537817
doi: 10.1021/acs.jpcb.8b10749
pmc: PMC6465090
mid: NIHMS1006907
doi:
Substances chimiques
Receptors, AMPA
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
130-137Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM122528
Pays : United States
Commentaires et corrections
Type : ErratumIn
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