Transducin

For example, the cAMP receptor of the colonial amoeba Dictyostelium, the non-rhodopsin closest in structure to the channel opsins such as the one used to restore vision in mice (Gehring 2004), binds to a transducin family adaptor protein, but also initiates ion influx in an adaptor protein-independent manner (Brzostowski & Kimmel 2001). ❋ Unknown (2006)

Modern vertebrate cilliary opsin binds to the adaptor protein transducin. ❋ Unknown (2006)

To make their discovery, scientists isolated rhodopsin / transducin directly from bovine retinas. ❋ Unknown (2009)

After light exposure, any contaminating proteins were removed, and the remaining rhodopsin and transducin "locked" in their chemical communication were removed using a centrifuge. ❋ Unknown (2009)

At the center of the discovery is the signaling of rhodopsin to transducin. ❋ Unknown (2009)

The researchers were able to "freeze frame" the chemical communication between rhodopsin and transducin to study how this takes place and what goes wrong at the molecular level in certain disorders. ❋ Unknown (2009)

This freezing involved "isolating rhodopsin / transducin directly from bovine retinas" and exposing it to light to activate the chemical signaling process. ❋ Unknown (2009)

Researchers say they were able to "freeze frame" interactions between rhodopsin and transducin to study it and find out what goes "wrong at the molecular level in certain [vision] disorders." ❋ Unknown (2009)

Here's Rachelle at Yale lindy hopping to the topic of "Structural analysis of phosducin and its phosphorylation-regulated interaction with transducin beta-gamma." ❋ Unknown (2008)

"At the center of the discovery is the signaling of rhodopsin to transducin. ❋ Unknown (2009)