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Ancient Origins of RGK Protein Function: Modulation of Voltage-Gated Calcium Channels Preceded the Protostome and Deuterostome Split
RGK proteins, Gem, Rad, Rem1, and Rem2, are members of the Ras superfamily of small GTP-binding proteins that interact with Ca(2+) channel β subunits to modify voltage-gated Ca(2+) channel function. In addition, RGK proteins affect several cellular processes such as cytoskeletal rearrangement, neuro...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Public Library of Science
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4081519/ https://www.ncbi.nlm.nih.gov/pubmed/24992013 http://dx.doi.org/10.1371/journal.pone.0100694 |
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author | Puhl, Henry L. Lu, Van B. Won, Yu-Jin Sasson, Yehezkel Hirsch, Joel A. Ono, Fumihito Ikeda, Stephen R. |
author_facet | Puhl, Henry L. Lu, Van B. Won, Yu-Jin Sasson, Yehezkel Hirsch, Joel A. Ono, Fumihito Ikeda, Stephen R. |
author_sort | Puhl, Henry L. |
collection | PubMed |
description | RGK proteins, Gem, Rad, Rem1, and Rem2, are members of the Ras superfamily of small GTP-binding proteins that interact with Ca(2+) channel β subunits to modify voltage-gated Ca(2+) channel function. In addition, RGK proteins affect several cellular processes such as cytoskeletal rearrangement, neuronal dendritic complexity, and synapse formation. To probe the phylogenetic origins of RGK protein–Ca(2+) channel interactions, we identified potential RGK-like protein homologs in genomes for genetically diverse organisms from both the deuterostome and protostome animal superphyla. RGK-like protein homologs cloned from Danio rerio (zebrafish) and Drosophila melanogaster (fruit flies) expressed in mammalian sympathetic neurons decreased Ca(2+) current density as reported for expression of mammalian RGK proteins. Sequence alignments from evolutionarily diverse organisms spanning the protostome/deuterostome divide revealed conservation of residues within the RGK G-domain involved in RGK protein – Ca(v)β subunit interaction. In addition, the C-terminal eleven residues were highly conserved and constituted a signature sequence unique to RGK proteins but of unknown function. Taken together, these data suggest that RGK proteins, and the ability to modify Ca(2+) channel function, arose from an ancestor predating the protostomes split from deuterostomes approximately 550 million years ago. |
format | Online Article Text |
id | pubmed-4081519 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-40815192014-07-10 Ancient Origins of RGK Protein Function: Modulation of Voltage-Gated Calcium Channels Preceded the Protostome and Deuterostome Split Puhl, Henry L. Lu, Van B. Won, Yu-Jin Sasson, Yehezkel Hirsch, Joel A. Ono, Fumihito Ikeda, Stephen R. PLoS One Research Article RGK proteins, Gem, Rad, Rem1, and Rem2, are members of the Ras superfamily of small GTP-binding proteins that interact with Ca(2+) channel β subunits to modify voltage-gated Ca(2+) channel function. In addition, RGK proteins affect several cellular processes such as cytoskeletal rearrangement, neuronal dendritic complexity, and synapse formation. To probe the phylogenetic origins of RGK protein–Ca(2+) channel interactions, we identified potential RGK-like protein homologs in genomes for genetically diverse organisms from both the deuterostome and protostome animal superphyla. RGK-like protein homologs cloned from Danio rerio (zebrafish) and Drosophila melanogaster (fruit flies) expressed in mammalian sympathetic neurons decreased Ca(2+) current density as reported for expression of mammalian RGK proteins. Sequence alignments from evolutionarily diverse organisms spanning the protostome/deuterostome divide revealed conservation of residues within the RGK G-domain involved in RGK protein – Ca(v)β subunit interaction. In addition, the C-terminal eleven residues were highly conserved and constituted a signature sequence unique to RGK proteins but of unknown function. Taken together, these data suggest that RGK proteins, and the ability to modify Ca(2+) channel function, arose from an ancestor predating the protostomes split from deuterostomes approximately 550 million years ago. Public Library of Science 2014-07-03 /pmc/articles/PMC4081519/ /pubmed/24992013 http://dx.doi.org/10.1371/journal.pone.0100694 Text en https://creativecommons.org/publicdomain/zero/1.0/ This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration, which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. |
spellingShingle | Research Article Puhl, Henry L. Lu, Van B. Won, Yu-Jin Sasson, Yehezkel Hirsch, Joel A. Ono, Fumihito Ikeda, Stephen R. Ancient Origins of RGK Protein Function: Modulation of Voltage-Gated Calcium Channels Preceded the Protostome and Deuterostome Split |
title | Ancient Origins of RGK Protein Function: Modulation of Voltage-Gated Calcium Channels Preceded the Protostome and Deuterostome Split |
title_full | Ancient Origins of RGK Protein Function: Modulation of Voltage-Gated Calcium Channels Preceded the Protostome and Deuterostome Split |
title_fullStr | Ancient Origins of RGK Protein Function: Modulation of Voltage-Gated Calcium Channels Preceded the Protostome and Deuterostome Split |
title_full_unstemmed | Ancient Origins of RGK Protein Function: Modulation of Voltage-Gated Calcium Channels Preceded the Protostome and Deuterostome Split |
title_short | Ancient Origins of RGK Protein Function: Modulation of Voltage-Gated Calcium Channels Preceded the Protostome and Deuterostome Split |
title_sort | ancient origins of rgk protein function: modulation of voltage-gated calcium channels preceded the protostome and deuterostome split |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4081519/ https://www.ncbi.nlm.nih.gov/pubmed/24992013 http://dx.doi.org/10.1371/journal.pone.0100694 |
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