Phosphorylation of the Drosophila transient receptor potential ion channel is regulated by the phototransduction cascade and involves several protein kinases and phosphatases
| Autor: | Armin Huber, Claudia Oberegelsbacher, Olaf Voolstra, Jens Pfannstiel, Jonas-Peter Bartels |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2013 |
| Předmět: |
Threonine
Light Phosphatase Blotting Western Molecular Sequence Data lcsh:Medicine Mass Spectrometry Phosphorylation cascade TRPC1 Transient receptor potential channel Transient Receptor Potential Channels Serine Animals Drosophila Proteins Protein phosphorylation Amino Acid Sequence Phosphorylation lcsh:Science Protein Kinase C Multidisciplinary Binding Sites biology Kinase lcsh:R Tryptophan Phosphoric Monoester Hydrolases Cell biology Drosophila melanogaster Biochemistry Mitogen-activated protein kinase Mutation biology.protein Photoreceptor Cells Invertebrate lcsh:Q Protein Kinases Research Article |
| Zdroj: | PLoS ONE, Vol 8, Iss 9, p e73787 (2013) PLoS ONE |
| ISSN: | 1932-6203 |
| Popis: | Protein phosphorylation plays a cardinal role in regulating cellular processes in eukaryotes. Phosphorylation of proteins is controlled by protein kinases and phosphatases. We previously reported the light-dependent phosphorylation of the Drosophila transient receptor potential (TRP) ion channel at multiple sites. TRP generates the receptor potential upon stimulation of the photoreceptor cell by light. An eye-enriched protein kinase C (eye-PKC) has been implicated in the phosphorylation of TRP by in vitro studies. Other kinases and phosphatases of TRP are elusive. Using phosphospecific antibodies and mass spectrometry, we here show that phosphorylation of most TRP sites depends on the phototransduction cascade and the activity of the TRP ion channel. A candidate screen to identify kinases and phosphatases provided in vivo evidence for an involvement of eye-PKC as well as other kinases and phosphatases in TRP phosphorylation. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|