| Autor: |
Medler KF; Department of Biological Sciences, Louisiana State University, Baton Rouge 70803, USA., Bruch RC |
| Jazyk: |
angličtina |
| Zdroj: |
Chemical senses [Chem Senses] 1999 Jun; Vol. 24 (3), pp. 295-9. |
| DOI: |
10.1093/chemse/24.3.295 |
| Abstrakt: |
Recombinant protein segments from a metabotropic glutamate receptor and from an odorant receptor were used as substrates in protein kinase C phosphorylation assays. Protein kinase Cbeta and delta phosphorylated an intracellular consensus phosphorylation site in the metabotropic glutamate receptor. Only protein kinase Cdelta phosphorylated a novel extracellular consensus phosphorylation site in the odorant receptor. These results suggest differential regulation of these receptors by protein kinase C isotypes. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
|
