Abstract
Background: Phosphatidylinositol 3-Kinases (PI3Ks) are a family of lipid kinases that phosphorylate the D3-hydroxyls of the inositol ring of phosphoinositides, and are responsible for coordinating a diverse range of cellular functions. A canonical pathway of activation of PI3Ks through the interaction of RA-domain with Ras proteins has been well established. In retinal photoreceptors, we have identified a non-canonical pathway of PI3Kγ activation through the interaction of its RA-domain with a putative Ras-like domain (RLD) in alpha subunit of cyclic nucleotide-gated channel (CNGA1) in retinal rod photoreceptors.
Results: The interaction between PI3Kγ and CNGA1 does not appear to play a role in regulation of CNG channel activity, but PI3Kγ uses CNGA1 as an anchoring module to achieve close proximity to its substrate to generate D3-phosphoinositides.
Conclusions: Our studies suggest a functional non-canonical PI3Kγ activation in retinal rod photoreceptor cells.
| Original language | English |
|---|---|
| Article number | 7 |
| Pages (from-to) | 1-11 |
| Number of pages | 11 |
| Journal | Cell Communication and Signaling |
| Volume | 13 |
| DOIs | |
| Publication status | Published - 2015 |
| Externally published | Yes |
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