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Reversible binding of divalent cations to Ductin protein assemblies—A putative new regulatory mechanism of membrane traffic processes

Ductins are a family of homologous and structurally similar membrane proteins with 2 or 4 trans-membrane alpha-helices. The active forms of the Ductins are membranous ring- or star-shaped oligomeric assemblies and they provide various pore, channel, gap-junction functions, assist in membrane fusion...

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Autores principales: Sebők-Nagy, Krisztina, Blastyák, András, Juhász, Gábor, Páli, Tibor
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10203432/
https://www.ncbi.nlm.nih.gov/pubmed/37228584
http://dx.doi.org/10.3389/fmolb.2023.1195010
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author Sebők-Nagy, Krisztina
Blastyák, András
Juhász, Gábor
Páli, Tibor
author_facet Sebők-Nagy, Krisztina
Blastyák, András
Juhász, Gábor
Páli, Tibor
author_sort Sebők-Nagy, Krisztina
collection PubMed
description Ductins are a family of homologous and structurally similar membrane proteins with 2 or 4 trans-membrane alpha-helices. The active forms of the Ductins are membranous ring- or star-shaped oligomeric assemblies and they provide various pore, channel, gap-junction functions, assist in membrane fusion processes and also serve as the rotor c-ring domain of V-and F-ATPases. All functions of the Ductins have been reported to be sensitive to the presence of certain divalent metal cations (Me(2+)), most frequently Cu(2+) or Ca(2+) ions, for most of the better known members of the family, and the mechanism of this effect is not yet known. Given that we have earlier found a prominent Me(2+) binding site in a well-characterised Ductin protein, we hypothesise that certain divalent cations can structurally modulate the various functions of Ductin assemblies via affecting their stability by reversible non-covalent binding to them. A fine control of the stability of the assembly ranging from separated monomers through a loosely/weakly to tightly/strongly assembled ring might render precise regulation of Ductin functions possible. The putative role of direct binding of Me(2+) to the c-ring subunit of active ATP hydrolase in autophagy and the mechanism of Ca(2+)-dependent formation of the mitochondrial permeability transition pore are also discussed.
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spelling pubmed-102034322023-05-24 Reversible binding of divalent cations to Ductin protein assemblies—A putative new regulatory mechanism of membrane traffic processes Sebők-Nagy, Krisztina Blastyák, András Juhász, Gábor Páli, Tibor Front Mol Biosci Molecular Biosciences Ductins are a family of homologous and structurally similar membrane proteins with 2 or 4 trans-membrane alpha-helices. The active forms of the Ductins are membranous ring- or star-shaped oligomeric assemblies and they provide various pore, channel, gap-junction functions, assist in membrane fusion processes and also serve as the rotor c-ring domain of V-and F-ATPases. All functions of the Ductins have been reported to be sensitive to the presence of certain divalent metal cations (Me(2+)), most frequently Cu(2+) or Ca(2+) ions, for most of the better known members of the family, and the mechanism of this effect is not yet known. Given that we have earlier found a prominent Me(2+) binding site in a well-characterised Ductin protein, we hypothesise that certain divalent cations can structurally modulate the various functions of Ductin assemblies via affecting their stability by reversible non-covalent binding to them. A fine control of the stability of the assembly ranging from separated monomers through a loosely/weakly to tightly/strongly assembled ring might render precise regulation of Ductin functions possible. The putative role of direct binding of Me(2+) to the c-ring subunit of active ATP hydrolase in autophagy and the mechanism of Ca(2+)-dependent formation of the mitochondrial permeability transition pore are also discussed. Frontiers Media S.A. 2023-05-09 /pmc/articles/PMC10203432/ /pubmed/37228584 http://dx.doi.org/10.3389/fmolb.2023.1195010 Text en Copyright © 2023 Sebők-Nagy, Blastyák, Juhász and Páli. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Molecular Biosciences
Sebők-Nagy, Krisztina
Blastyák, András
Juhász, Gábor
Páli, Tibor
Reversible binding of divalent cations to Ductin protein assemblies—A putative new regulatory mechanism of membrane traffic processes
title Reversible binding of divalent cations to Ductin protein assemblies—A putative new regulatory mechanism of membrane traffic processes
title_full Reversible binding of divalent cations to Ductin protein assemblies—A putative new regulatory mechanism of membrane traffic processes
title_fullStr Reversible binding of divalent cations to Ductin protein assemblies—A putative new regulatory mechanism of membrane traffic processes
title_full_unstemmed Reversible binding of divalent cations to Ductin protein assemblies—A putative new regulatory mechanism of membrane traffic processes
title_short Reversible binding of divalent cations to Ductin protein assemblies—A putative new regulatory mechanism of membrane traffic processes
title_sort reversible binding of divalent cations to ductin protein assemblies—a putative new regulatory mechanism of membrane traffic processes
topic Molecular Biosciences
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10203432/
https://www.ncbi.nlm.nih.gov/pubmed/37228584
http://dx.doi.org/10.3389/fmolb.2023.1195010
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