Caveolin-1 as a regulator of neuronal calcium sensor proteins in phototransduction systemстатья Тезисы

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[1] Caveolin-1 as a regulator of neuronal calcium sensor proteins in phototransduction system / V. Vladimirov, E. Zernii, K. Koch et al. // FEBS open bio. — 2018. — Vol. 8, no. 1. — P. 355. Caveolin­1 is the major regulatory protein of detergent resistant membranes (DRM), which associating with regulation of signaling activity in different organism systems. Rod cell membranes contain cholesterol­rich DRM, which accumulate visual cascade proteins. In this study, photoreceptor Ca2+ ­binding proteins recoverin, NCS1, GCAP1, and GCAP2, belonging to neuronal calcium sensor (NCS) family, were recognized as novel caveolin­1 interacting partners. We demonstrated that all studied proteins co­precipitate with caveolin­1 from rod outer segment membranes, and can directly interact with caveolin­1. Pull­down assay, surface plasmon resonance spectroscopy and isothermal titration calorimetry data indicate that there is interaction with full­length caveolin­1 N­terminal domain (1­101) and caveolin­1 scaffolding domain (81­101). Interestingly that this interaction occurs only in absence of calcium ions, what is supported by surface localization of caveolin­1 interaction site in Ca2+ ­free NCS proteins state. Caveolin­1 increase Ca2+ ­sensitivity of recoverin, and as a consequence, makes its inhibitory activity to rhodopsinkinase more pronounced, but not interfere with recoverin­rhodopsin kinase interaction. Amount of free Ca2+, required for this process, consider caveolin­1 influence, become in good agreement with physiological conditions of photoreceptor cell. GCAP­2 is upregulated by caveolin­1 in Ca2+ ­free state, which increase guanylate cyclase activity. It seems that there is a common mechanism of interaction between caveolin­1 and NCS proteins in Ca2+ ­free state. For recoverin increasing of Ca2+ ­sensitivity is due to the stabilization of the open conformation of its second Ca2+ ­binding domain EF2. Obtained data suggest that at low calcium NCS proteins are compartmentalized in photoreceptor rafts via binding to caveolin­1, what enhances their activity or ensures their faster responses on Ca 2+ ­signals. The study was supported by RFBR (grant # 15­-04­-07963). [ DOI ]

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