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Phosphorylation Induces Conformational Rigidity at the C-Terminal Domain of AMPA Receptors.


ABSTRACT: The intracellular C-terminal domain (CTD) of AMPA (?-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.

SUBMITTER: Chatterjee S 

PROVIDER: S-EPMC6465090 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature

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Phosphorylation Induces Conformational Rigidity at the C-Terminal Domain of AMPA Receptors.

Chatterjee Sudeshna S   Ade Carina C   Nurik Caitlin E CE   Carrejo Nicole C NC   Dutta Chayan C   Jayaraman Vasanthi V   Landes Christy F CF  

The journal of physical chemistry. B 20181227 1


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 t  ...[more]

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