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Related Experiment Video

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The finger loop as an activation sensor in arrestin.

Sergey A Vishnivetskiy¹, Elizabeth K Huh¹, Eugenia V Gurevich¹

¹Department of Pharmacology, Vanderbilt University, Nashville, TN, USA.

Journal of Neurochemistry

|November 7, 2020

Summary

The arrestin-1 finger loop acts as a crucial sensor for activated G-protein-coupled receptors. Mutations revealed its essential role in detecting receptor activation states, impacting arrestin-1 binding dynamics.

Keywords:

GPCR arrestin protein-protein interactions receptor activation structure-function

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Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Arrestins bind to activated G-protein-coupled receptors (GPCRs) to terminate signaling.
The finger loop of arrestin is proposed to sense the activated state of GPCRs.

Purpose of the Study:

To investigate the role of the arrestin-1 finger loop in recognizing activated rhodopsin.
To determine if the finger loop functions as a sensor for GPCR activation.

Main Methods:

Comprehensive mutagenesis of the bovine visual arrestin-1 finger loop.
Generation of mutant arrestin-1 proteins using cell-free translation.
In vitro binding assays with purified light-activated rhodopsin.

Main Results:

Most finger loop mutations significantly affected arrestin-1 binding to activated rhodopsin.
Six mutations specifically impaired binding to the activated receptor conformation.
The finger loop is critical for arrestin-1's ability to sense receptor activation.

Conclusions:

The arrestin-1 finger loop is a key determinant for sensing the activated conformation of GPCRs.
Arrestin-1 exhibits differential binding to various rhodopsin functional states.