Functional Characterization of an Electromagnetic Perceptive Protein
Mitra, S.; Barnaba, C.; Schmidt, J. C.; Pelled, G.; Gilad, A. A.
Show abstract
Magnetoreception, the response to geomagnetic fields is a well described phenomenon in nature. However, it is likely that convergent evolution led to different mechanisms in different organisms. One intriguing example is the unique Electromagnetic Perceptive Gene (EPG) from the glass catfish Kryptopterus vitreolus, that can remotely control cellular function, upon magnetic stimulation in in-vitro and in-vivo. Here, we report for the first time the cellular location and orientation of the EPG protein. We utilized a differential labelling technique to determine that the EPG protein is a membrane anchored protein with an N-terminal extracellular domain. The kinetics and diffusion dynamics of the EPG protein in response to magnetic stimulation was also elucidated using single particle imaging and tracking. Pulse chase labelling and Total Internal Reflection Fluorescence (TIRF) imaging revealed an increase in EPG kinetics post magnetic activation at a single particle level. Trajectory analysis show notably different EPG protein kinetics before and after magnetic stimulation in both 2 (free vs bound particle) and 3 state (free vs intermediate vs bound particle) tracking models. This data provides additional information to support and understand the underlying biophysical mechanisms behind EPG activation by magnetic fields and provides evidence for the basis of magnetoreception in the EPG protein that will aid in future studies that seek to further understand this novel mechanism. This study is important for understanding magnetoreception as well as developing new technologies for magnetogenetics - the utilization of electromagnetic fields to remotely control cellular function. Table of Contents Graphic O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=126 SRC="FIGDIR/small/329946v2_ufig1.gif" ALT="Figure 1"> View larger version (39K): org.highwire.dtl.DTLVardef@1ce4aborg.highwire.dtl.DTLVardef@e8bb89org.highwire.dtl.DTLVardef@1705113org.highwire.dtl.DTLVardef@dadf23_HPS_FORMAT_FIGEXP M_FIG C_FIG
Matching journals
The top 7 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- Benchmarking of novel green fluorescent proteins for the quantification of protein oligomerization in living cells 93%
- Improved yellow-green split fluorescent proteins for protein labeling and signal amplification 93%
- Arachidonic acid promotes the binding of 5-lipoxygenase on nanodiscs containing 5-lipoxygenase activating protein in the absence of calcium-ions. 93%
Similar papers in this journal
Similar papers in this journal
- Network Organisation and the Dynamics of Tubules in the Endoplasmic Reticulum 94%
- Repeated FRAP of the actin-binding protein CapG in the cell nucleus - a functional assay for EGF signaling in the single live breast cancer cell 93%
- Ratiometric fluorescence nanoscopy and lifetime imaging of novel Nile Red analogs for analysis of membrane packing in living cells 93%
Similar papers in this journal
- Single molecule dynamics at a bacterial replication fork after nutritional downshift 92%
- The impact of plasma membrane lipid composition on flagella-mediated adhesion of enterohemorrhagic Escherichia coli 92%
- Photochromic fluorophores enable imaging of lowly-expressed proteins in the autofluorescent fungus Candida albicans 92%
Similar papers in this journal
- Bacteriophage uptake by Eukaryotic cell layers represents a major sink for phages during therapy 92%
- Influence of nanobody binding on fluorescence emission, mobility and organization of GFP-tagged proteins 91%
- Diffusion of small molecule drugs is affected by surface interactions and crowder proteins 91%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.