The 2.8 Angstrom crystal structure of visual arrestin: a model for arrestin's regulation

Article Abstract:

G proteins play a key role in the signaling pathway used by eukaryotes to communicate information from the extracellular environment. These signals activate receptors embedded in the cell membrane by triggering off a change in the conformation of G proteins, which then instruct effector molecules on the cell's physiological response. In this pathway, termination of the signal requires the presence of arrestins, which are known to bind with G protein-coupled receptors. A description of the molecular mechanism by which these arrestins are regulated is provided.

Eukaryotic cells, Cells (Biology), Eukaryotes

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Arrestin binding determines the rate of inactivation of the G protein-coupled receptor rhodopsin in vivo

Article Abstract:

Electrophysiological measurements of the Drosophila photoreceptors show that the inactivation of G protein-coupled receptor rhodopsin is due to the binding of arrestin to metarhodopsin and a bimolecular model describes the mechanism accurately. Arrestin is produced by the genes arr1 and arr2 which are found in all the photoreceptors of the eyes. Arrestin prevents the interaction of the receptor and G protein and phosphorylation of metarhodopsin and dissociation of G protein are not necessary for the inactivation of the receptor.

Drosophila

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Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1

Article Abstract:

A yeast two-hybrid system was studied to identify proteins that interact with rhodopsin's carboxy-terminal cytoplasmic tail. Results indicate that t complex testis expressed 1 (Tctex-1) interacts with the C-terminus of rhodopsin directly and with high specifity. It was observed that rhodopsin-containing vesicles biochemically and fuctionally link with microtubules using the cytoplasmic dynein in a Tctex-1-dependent manner, hence, acting as the membrane receptor fo cytoplasmic dynein.

Yeast, Yeast (Food product), Microtubules, Dynein, Cytoplasm

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