| |
| Specific Observation(s) |
Source of Data |
| CamL bait peptide showed multiple positive interactions with Ryanodine receptor I |
Y2H Data
|
| CamL bait peptide showed positive interaction with CaMKII |
Y2H Data
|
| Abstract |
| Calcium-modulating cyclophilin ligand (CAML) has been shown to participate in calcium signaling by promoting the release of intracellular Ca2+ stores. An important role in T lymphocytes has been described where CAML is activated via the TNF receptor family member, TACI. Overexpression of CAML in Jurkat T cells results in increased calcium release, and the protein colocalizes with calreticulin and SERCA at cytosolic vesicles. The mechanism of action for CAML is unknown. Yeast two-hybrid data from the AfCS reveals possible interactions of CAML with the Ryanodine Receptor type I and CaMKII alpha using the same bait peptide. These data uncover the possibility that CAML regulates the release of calcium through direct interaction with Ryanodine receptors and the recruitment of CaMKII, which positively regulate Ryanodine receptors. |
| Suggested Future Experiments |
| Verify interaction between these proteins by immunoprecipitation. |
| Test the ability of CAML to promote intracellular calcium release in cells where Ryanodine receptor or CaMKII is (or is not) perturbed. |
| Discussion |
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