10.3389/fnmol.2018.00280.s001 Gabriella Margherita Mazzotta Gabriella Margherita Mazzotta Massimo Bellanda Massimo Bellanda Giovanni Minervini Giovanni Minervini Milena Damulewicz Milena Damulewicz Paola Cusumano Paola Cusumano Simona Aufiero Simona Aufiero Monica Stefani Monica Stefani Barbara Zambelli Barbara Zambelli Stefano Mammi Stefano Mammi Rodolfo Costa Rodolfo Costa Silvio C. E. Tosatto Silvio C. E. Tosatto Image_1_Calmodulin Enhances Cryptochrome Binding to INAD in Drosophila Photoreceptors.TIFF Frontiers 2018 Drosophila melanogaster calmodulin INAD cryptochrome photoreception 2018-08-20 04:14:33 Figure https://frontiersin.figshare.com/articles/figure/Image_1_Calmodulin_Enhances_Cryptochrome_Binding_to_INAD_in_Drosophila_Photoreceptors_TIFF/6983609 <p>Light is the main environmental stimulus that synchronizes the endogenous timekeeping systems in most terrestrial organisms. Drosophila cryptochrome (dCRY) is a light-responsive flavoprotein that detects changes in light intensity and wavelength around dawn and dusk. We have previously shown that dCRY acts through Inactivation No Afterpotential D (INAD) in a light-dependent manner on the Signalplex, a multiprotein complex that includes visual-signaling molecules, suggesting a role for dCRY in fly vision. Here, we predict and demonstrate a novel Ca<sup>2+</sup>-dependent interaction between dCRY and calmodulin (CaM). Through yeast two hybrid, coimmunoprecipitation (Co-IP), nuclear magnetic resonance (NMR) and calorimetric analyses we were able to identify and characterize a CaM binding motif in the dCRY C-terminus. Similarly, we also detailed the CaM binding site of the scaffold protein INAD and demonstrated that CaM bridges dCRY and INAD to form a ternary complex in vivo. Our results suggest a process whereby a rapid dCRY light response stimulates an interaction with INAD, which can be further consolidated by a novel mechanism regulated by CaM.</p>