Calmodulin Enhances Cryptochrome Binding to INAD in Drosophila Photoreceptors
| العنوان: | Calmodulin Enhances Cryptochrome Binding to INAD in Drosophila Photoreceptors |
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| المؤلفون: | 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 |
| المساهمون: | G.M.Mazzotta, M. Bellanda, G. Minervini, M. Damulewicz, P. Cusumano, S. Aufiero, M. Stefani, B. Zambelli, S. Mammi, R. Costa, S.C.E. Tosatto |
| المصدر: | Frontiers in Molecular Neuroscience, Vol 11 (2018) Frontiers in Molecular Neuroscience |
| بيانات النشر: | Frontiers Media SA, 2018. |
| سنة النشر: | 2018 |
| مصطلحات موضوعية: | 0301 basic medicine, Scaffold protein, calmodulin, photoreception, Multiprotein complex, Calmodulin, Two-hybrid screening, lcsh:RC321-571, 03 medical and health sciences, Cellular and Molecular Neuroscience, peptide-protein interaction, Cryptochrome, lcsh:Neurosciences. Biological psychiatry. Neuropsychiatry, Molecular Biology, Ternary complex, Original Research, yeast two hybrid, biology, Chemistry, INAD, biology.organism_classification, NMR, isothermal titration calorimetry, Cell biology, Light intensity, Drosophila melanogaster, 030104 developmental biology, biology.protein, cryptochrome, coimmunoprecipitation, Photoreception, Neuroscience |
| الوصف: | 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. |
| وصف الملف: | ELETTRONICO |
| تدمد: | 1662-5099 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::625e2b48aea5044993e7a9e7d597a394Test https://doi.org/10.3389/fnmol.2018.00280Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....625e2b48aea5044993e7a9e7d597a394 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 16625099 |
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