The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.
Mechanism of rhodopsin kinase activation
Open accessAbstract
The role of the cytoplasmic loops and C-terminal region of bovine rhodopsin (Rho) in binding and activating rhodopsin kinase was investigated. The ability of various enzymatically truncated forms of photolyzed rhodopsin (Rho*) to stimulate rhodopsin kinase activity was quantified. Following endopeptidase Asp-N cleavage of all phosphorylation sites on the C-terminal, the resulting truncated Rho* (329G-Rho*) was not phosphorylated by rhodopsin kinase. This suggests that rhodopsin kinase only phosphorylates C-terminal sites of Rho*. However 329G-Rho* could bind rhodopsin kinase and stimulate phosphorylation of exogenous peptide. Kinase stimulation was investigated for other truncated forms of Rho* in which the C-terminal region was either partially or completely eliminated, and the V-VI loop was either cleaved or left intact (339K-Rho*, 341E239E-Rho*, 329G239E-Rho*, 327P240S-Rho*). Results suggest that the V-VI loop is crucial for kinase binding (similar to the binding of GT). Mastoparan, a model peptide for G-protein-coupled receptors, was found to stimulate rhodopsin kinase in a mechanism similar to that of truncated Rho*. We conclude that rhodopsin kinase binds to the cytoplasmic loops of Rho* to cause a stimulation of its catalytic activity.
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G PROTEIN–COUPLED RECEPTOR KINASES
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Metadata
- Authors
- Palczewski, K., Buczyłko, J., Kaplan, M. W., Polans, A. S., & Crabb, J. W.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1991-07
- Volume
- 266
- Issue
- 20
- Pages
- 12949-12955
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2143071207
- Cited by
- 305
- References
- 38
- FWCI
- 5.58
- Type
- journal article
- Language
- en
- Open access
- hybrid
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