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Modulation of voltage-gated Ca(V)2.2 Ca(2+) channels by newly identified interaction partners

Voltage-gated Ca(2+) channels are typically integrated in a complex network of protein-protein-interactions, also referred to as Ca(2+) channel nanodomains. Amongst the neuronal Ca(V)2 channel family, Ca(V)2.2 is of particular importance due to its general role for signal transmission from the perip...

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Autores principales: Lacinova, Lubica, Mallmann, Robert Theodor, Jurkovičová-Tarabová, Bohumila, Klugbauer, Norbert
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7567506/
https://www.ncbi.nlm.nih.gov/pubmed/33006503
http://dx.doi.org/10.1080/19336950.2020.1831328
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author Lacinova, Lubica
Mallmann, Robert Theodor
Jurkovičová-Tarabová, Bohumila
Klugbauer, Norbert
author_facet Lacinova, Lubica
Mallmann, Robert Theodor
Jurkovičová-Tarabová, Bohumila
Klugbauer, Norbert
author_sort Lacinova, Lubica
collection PubMed
description Voltage-gated Ca(2+) channels are typically integrated in a complex network of protein-protein-interactions, also referred to as Ca(2+) channel nanodomains. Amongst the neuronal Ca(V)2 channel family, Ca(V)2.2 is of particular importance due to its general role for signal transmission from the periphery to the central nervous system, but also due to its significance for pain perception. Thus, Ca(V)2.2 is an ideal target candidate to search for pharmacological inhibitors but also for novel modulatory interactors. In this review we summarize the last years findings of our intense screenings and characterization of the six Ca(V)2.2 interaction partners, tetraspanin-13 (TSPAN-13), reticulon 1 (RTN1), member 1 of solute carrier family 38 (SLC38), prostaglandin D2 synthase (PTGDS), transmembrane protein 223 (TMEM223), and transmembrane BAX inhibitor motif 3 (Grina/TMBIM3) containing protein. Each protein shows a unique way of channel modulation as shown by extensive electrophysiological studies. Amongst the newly identified interactors, Grina/TMBIM3 is most striking due to its modulatory effect which is rather comparable to G-protein regulation.
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spelling pubmed-75675062020-10-26 Modulation of voltage-gated Ca(V)2.2 Ca(2+) channels by newly identified interaction partners Lacinova, Lubica Mallmann, Robert Theodor Jurkovičová-Tarabová, Bohumila Klugbauer, Norbert Channels (Austin) Review Voltage-gated Ca(2+) channels are typically integrated in a complex network of protein-protein-interactions, also referred to as Ca(2+) channel nanodomains. Amongst the neuronal Ca(V)2 channel family, Ca(V)2.2 is of particular importance due to its general role for signal transmission from the periphery to the central nervous system, but also due to its significance for pain perception. Thus, Ca(V)2.2 is an ideal target candidate to search for pharmacological inhibitors but also for novel modulatory interactors. In this review we summarize the last years findings of our intense screenings and characterization of the six Ca(V)2.2 interaction partners, tetraspanin-13 (TSPAN-13), reticulon 1 (RTN1), member 1 of solute carrier family 38 (SLC38), prostaglandin D2 synthase (PTGDS), transmembrane protein 223 (TMEM223), and transmembrane BAX inhibitor motif 3 (Grina/TMBIM3) containing protein. Each protein shows a unique way of channel modulation as shown by extensive electrophysiological studies. Amongst the newly identified interactors, Grina/TMBIM3 is most striking due to its modulatory effect which is rather comparable to G-protein regulation. Taylor & Francis 2020-10-15 /pmc/articles/PMC7567506/ /pubmed/33006503 http://dx.doi.org/10.1080/19336950.2020.1831328 Text en © 2020 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed 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, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review
Lacinova, Lubica
Mallmann, Robert Theodor
Jurkovičová-Tarabová, Bohumila
Klugbauer, Norbert
Modulation of voltage-gated Ca(V)2.2 Ca(2+) channels by newly identified interaction partners
title Modulation of voltage-gated Ca(V)2.2 Ca(2+) channels by newly identified interaction partners
title_full Modulation of voltage-gated Ca(V)2.2 Ca(2+) channels by newly identified interaction partners
title_fullStr Modulation of voltage-gated Ca(V)2.2 Ca(2+) channels by newly identified interaction partners
title_full_unstemmed Modulation of voltage-gated Ca(V)2.2 Ca(2+) channels by newly identified interaction partners
title_short Modulation of voltage-gated Ca(V)2.2 Ca(2+) channels by newly identified interaction partners
title_sort modulation of voltage-gated ca(v)2.2 ca(2+) channels by newly identified interaction partners
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7567506/
https://www.ncbi.nlm.nih.gov/pubmed/33006503
http://dx.doi.org/10.1080/19336950.2020.1831328
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