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Proposed three-phenylalanine motif involved in magnetoreception signalling of an Actinopterygii protein expressed in mammalian cells
Studies at the cellular and molecular level of magnetoreception—sensing and responding to magnetic fields—are a relatively new research area. It appears that different mechanisms of magnetoreception in animals evolved from different origins, and, therefore, many questions about its mechanisms remain...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10688439/ https://www.ncbi.nlm.nih.gov/pubmed/37989224 http://dx.doi.org/10.1098/rsob.230019 |
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author | Ricker, Brianna Mitra, Sunayana Castellanos, E. Alejandro Grady, Connor J. Woldring, Daniel Pelled, Galit Gilad, Assaf A. |
author_facet | Ricker, Brianna Mitra, Sunayana Castellanos, E. Alejandro Grady, Connor J. Woldring, Daniel Pelled, Galit Gilad, Assaf A. |
author_sort | Ricker, Brianna |
collection | PubMed |
description | Studies at the cellular and molecular level of magnetoreception—sensing and responding to magnetic fields—are a relatively new research area. It appears that different mechanisms of magnetoreception in animals evolved from different origins, and, therefore, many questions about its mechanisms remain left open. Here we present new information regarding the Electromagnetic Perceptive Gene (EPG) from Kryptopterus vitreolus that may serve as part of the foundation to understanding and applying magnetoreception. Using HaloTag coupled with fluorescent ligands and phosphatidylinositol specific phospholipase C we show that EPG is associated with the membrane via glycosylphosphatidylinositol anchor. EPG's function of increasing intracellular calcium was also used to generate an assay using GCaMP6m to observe the function of EPG and to compare its function with that of homologous proteins. It was also revealed that EPG relies on a motif of three phenylalanine residues to function—stably swapping these residues using site directed mutagenesis resulted in a loss of function in EPG. This information not only expands upon our current understanding of magnetoreception but may provide a foundation and template to continue characterizing and discovering more within the emerging field. |
format | Online Article Text |
id | pubmed-10688439 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | The Royal Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-106884392023-11-30 Proposed three-phenylalanine motif involved in magnetoreception signalling of an Actinopterygii protein expressed in mammalian cells Ricker, Brianna Mitra, Sunayana Castellanos, E. Alejandro Grady, Connor J. Woldring, Daniel Pelled, Galit Gilad, Assaf A. Open Biol Research Studies at the cellular and molecular level of magnetoreception—sensing and responding to magnetic fields—are a relatively new research area. It appears that different mechanisms of magnetoreception in animals evolved from different origins, and, therefore, many questions about its mechanisms remain left open. Here we present new information regarding the Electromagnetic Perceptive Gene (EPG) from Kryptopterus vitreolus that may serve as part of the foundation to understanding and applying magnetoreception. Using HaloTag coupled with fluorescent ligands and phosphatidylinositol specific phospholipase C we show that EPG is associated with the membrane via glycosylphosphatidylinositol anchor. EPG's function of increasing intracellular calcium was also used to generate an assay using GCaMP6m to observe the function of EPG and to compare its function with that of homologous proteins. It was also revealed that EPG relies on a motif of three phenylalanine residues to function—stably swapping these residues using site directed mutagenesis resulted in a loss of function in EPG. This information not only expands upon our current understanding of magnetoreception but may provide a foundation and template to continue characterizing and discovering more within the emerging field. The Royal Society 2023-11-22 /pmc/articles/PMC10688439/ /pubmed/37989224 http://dx.doi.org/10.1098/rsob.230019 Text en © 2023 The Authors. https://creativecommons.org/licenses/by/4.0/Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, provided the original author and source are credited. |
spellingShingle | Research Ricker, Brianna Mitra, Sunayana Castellanos, E. Alejandro Grady, Connor J. Woldring, Daniel Pelled, Galit Gilad, Assaf A. Proposed three-phenylalanine motif involved in magnetoreception signalling of an Actinopterygii protein expressed in mammalian cells |
title | Proposed three-phenylalanine motif involved in magnetoreception signalling of an Actinopterygii protein expressed in mammalian cells |
title_full | Proposed three-phenylalanine motif involved in magnetoreception signalling of an Actinopterygii protein expressed in mammalian cells |
title_fullStr | Proposed three-phenylalanine motif involved in magnetoreception signalling of an Actinopterygii protein expressed in mammalian cells |
title_full_unstemmed | Proposed three-phenylalanine motif involved in magnetoreception signalling of an Actinopterygii protein expressed in mammalian cells |
title_short | Proposed three-phenylalanine motif involved in magnetoreception signalling of an Actinopterygii protein expressed in mammalian cells |
title_sort | proposed three-phenylalanine motif involved in magnetoreception signalling of an actinopterygii protein expressed in mammalian cells |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10688439/ https://www.ncbi.nlm.nih.gov/pubmed/37989224 http://dx.doi.org/10.1098/rsob.230019 |
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