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Biology subjects

Benster, T.

Publications and source records attributed to Benster, T..

2 recordsLinked to original sources

Reconstruction of visual images from mouse retinal ganglion cell spiking activity using convolutional neural networks

All visual information in mammals is encoded in the aggregate pattern of retinal ganglion cell (RGC) firing. How this information is decoded to yield percepts remains incompletely understood. We have trained convolutional neural networks with multielectrode array-recorded murine RGC responses to projected images. The trained model accurately reconstructed novel facial images solely from RGC firing data. In this model, subpopulations of cells with faster firing rates are largely sufficient for accurate reconstruction, and ON- and OFF-cells contribute complementary and overlapping information to image reconstruction. Information content for reconstruction correlates with overall firing rate, and locality of information contributing to reconstruction varies substantially across the image and retina. This model demonstrates that artificial neural networks are capable of learning multicellular sensory neural encoding, and provides a viable model for understanding visual information encoding. Significance StatementConvolutional neural networks can be trained on high-density neuronal firing data from the optic nerve to reconstruct complicated images within a defined image space.

neuroscience↗

Structural basis for channel conduction in the pump-like channelrhodopsin ChRmine

ChRmine1, a recently-discovered bacteriorhodopsin-like cation-conducting channelrhodopsin1, 2, exhibits puzzling properties (unusually-large photocurrents, exceptional red-shift in action spectrum, and extreme light-sensitivity) that have opened up new opportunities in optogenetics1, 3-5. ChRmine and its homologs function as light-gated ion channels, but by primary sequence more closely resemble ion pump rhodopsins; the molecular mechanisms for passive channel conduction in this family of proteins, as well as the unusual properties of ChRmine itself, have remained mysterious. Here we present the cryo-electron microscopy structure of ChRmine at 2.0 [A] resolution. The structure reveals striking architectural features never seen before in channelrhodopsins including trimeric assembly, a short transmembrane-helix 3 unwound in the middle of the membrane, a prominently-twisting extracellular-loop 1, remarkably-large intracellular cavities and extracellular vestibule, and an unprecedented hydrophilic pore that extends through the center of the trimer, separate from the three individual monomer pores. Electrophysiological, spectroscopic, and computational analyses provide insight into conduction and gating of light-gated channels with these distinct design features, and point the way toward structure-guided creation of novel channelrhodopsins for optogenetic applications in biology.

biophysics↗