Abstract
Growth factor receptor-bound protein 14 (Grb14) is an adaptor protein that is involved in receptor tyrosine kinase signalling. In this study, we report that Grb14 interacts with the rod photoreceptor-specific cyclic-nucleotide-gated channel alpha subunit (CNGA1) and decreases its affinity for cyclic guanosine monophosphate. Channel modulation is controlled by direct binding of the Grb14 Ras-associating domain with the carboxy-terminal region of CNGA1. We observed that the channel remains open in Grb14-mice that are exposed to light, suggesting that Grb14 is a normal physiological modulator of CNG channel function in vivo.
| Original language | English |
|---|---|
| Pages (from-to) | 861-867 |
| Number of pages | 7 |
| Journal | EMBO Reports |
| Volume | 11 |
| Issue number | 11 |
| DOIs | |
| Publication status | Published - 2010 |
| Externally published | Yes |
Keywords
- cyclic-nucleotide-gated channel
- Grb14
- photoreceptor cells
- Ras-associating domain
- tyrosine kinase signalling
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