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Biology subjects

Vivaudou, M.

Publications and source records attributed to Vivaudou, M..

2 recordsLinked to original sources

Hijacking of internal calcium dynamics by intracellularly residing rhodopsins

Rhodopsins are ubiquitous light-driven membrane proteins with diverse functions, including ion transport. Widely distributed, they are also coded in the genomes of giant viruses infecting phytoplankton where their function is not settled. We examined the properties of three type 1 viral channelrhodopsins (VCR1s), and, unexpectedly, found that VCR1s accumulate exclusively intracellularly, and, upon illumination, induced calcium release from intracellular IP3-dependent stores. In vivo, this light-induced calcium release was sufficient to remote control muscle contraction and behavior in VCR1-expressing tadpoles. VCR1s are the first rhodopsins shown to natively confer light-induced Ca2+ release, suggesting an original mechanism for reshaping the response to light of virus-infected algae. The ability of VCR1s to photorelease calcium without altering plasma membrane electrical properties marks them as precursors for novel optogenetics tools, with potential applications in basic research and medicine.

physiology↗

Viral channelrhodopsins: calcium-dependent Na+/K+ selective light-gated channels

Phytoplankton is the base of the marine food chain, oxygen, carbon cycle playing a global role in climate and ecology. Nucleocytoplasmic Large DNA Viruses regulating the dynamics of phytoplankton comprise genes of rhodopsins of two distinct families. We present a function-structure characterization of two homologous proteins representatives of family 1 of viral rhodopsins, OLPVR1 and VirChR1. VirChR1 is a highly selective, Ca2+-dependent, Na+/K+- conducting channel and, in contrast to known cation channelrhodopsins (ChRs), is impermeable to Ca2+ ions. In human neuroblastoma cells, upon illumination, VirChR1 depolarizes the cell membrane to a level sufficient to fire neurons. It suggests its unique optogenetic potential. 1.4 [A] resolution structure of OLPVR1 reveals their remarkable difference from the known channelrhodopsins and a unique ion-conducting pathway. The data suggest that viral channelrhodopsins mediate phototaxis of algae enhancing the host anabolic processes to support virus reproduction, and therefore, their key role in global phytoplankton dynamics.

biophysics↗