What question did this study set out to answer?

To examine the molecular mechanisms and biochemical requirements governing the association of the 48-kDa protein with illuminated rod photoreceptor disk membranes.

October 29, 1984FEBS Letters

Light‐induced binding of 48‐kDa protein to photoreceptor membranes is highly enhanced by phosphorylation of rhodopsin

View Full Paper

Ask AI

Bookmark

Authors

HKH. KühnHoward Hughes Medical Institute SHS W HallUniversity of Reading UWUrsula WildenJeonbuk National University

Discussion

Member takes

Implication

In vitro biochemical assay demonstrates that rhodopsin phosphorylation enhances light-dependent 48-kDa protein binding, suggesting competitive regulation with GTP-binding proteins.

Key Points

To examine the molecular mechanisms and biochemical requirements governing the association of the 48-kDa protein with illuminated rod photoreceptor disk membranes.
Assayed the binding of soluble 48-kDa protein to rod disk membranes under dark and light conditions (5–10% rhodopsin activation) with or without ATP and rhodopsin kinase.
Assessed 48-kDa protein binding to pre-phosphorylated, regenerated rhodopsin and evaluated competitive displacement by adding excess GTP-binding protein.
The 48-kDa protein bound to disk membranes upon illumination of 5–10% of rhodopsin only when rhodopsin was phosphorylated by ATP and rhodopsin kinase, though pre-phosphorylated rhodopsin bound the protein in the light without requiring free ATP.
Illumination triggered GTP-binding protein association with both unphosphorylated and phosphorylated rhodopsin, and excess GTP-binding protein competitively displaced the 48-kDa protein from illuminated, phosphorylated disk membranes.

Cite This Study

Kühn et al. (1984) studied this question.

synapsesocial.com/papers/6a15fa2fbdb7c25666524c9d https://doi.org/10.1016/0014-5793(84)81221-1

View Full Paper

Ask AI

Bookmark

Implication

In vitro biochemical assay demonstrates that rhodopsin phosphorylation enhances light-dependent 48-kDa protein binding, suggesting competitive regulation with GTP-binding proteins.

Light‐induced binding of 48‐kDa protein to photoreceptor membranes is highly enhanced by phosphorylation of rhodopsin

Discussion

Member takes

Implication

Key Points

Cite This Study

Light‐induced binding of 48‐kDa protein to photoreceptor membranes is highly enhanced by phosphorylation of rhodopsin

Discussion

Member takes

Implication

Key Points

Cite This Study

Also Consider

Also Consider