Growth factor receptor-bound protein 14 (Grb14) belongs to the Grb7 family. It is an adapter molecule, lacking any intrinsic enzyme activity, but mediates protein-protein and protein-lipid interactions. In photoreceptors, Grb14 undergoes a rhodopsin-dependent translocation from the inner segments to the outer segments. In photoreceptors, Grb14 undergoes a light-dependent tyrosine phosphorylation and protects the insulin receptor (IR) phosphorylation, which is neuroprotective. Outersegment- localized Grb14 also modulates the activity of the cyclic nucleotide gated (CNG) chancel. Thus, Grb14 plays a key role in receiving signals from rhodopsin, and translocating to outer segments, where it regulates IR and CNG channel activities. The present study supports the idea that rhodopsin regulates non-canonical signaling pathways in photoreceptor cells.