Title |
Calmodulin Enhances Cryptochrome Binding to INAD in Drosophila Photoreceptors
|
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Published in |
Frontiers in Molecular Neuroscience, August 2018
|
DOI | 10.3389/fnmol.2018.00280 |
Pubmed ID | |
Authors |
Gabriella Margherita Mazzotta, Massimo Bellanda, Giovanni Minervini, Milena Damulewicz, Paola Cusumano, Simona Aufiero, Monica Stefani, Barbara Zambelli, Stefano Mammi, Rodolfo Costa, Silvio C. E. Tosatto |
Abstract |
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 Ca2+-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. |
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