Matches in SemOpenAlex for { <https://semopenalex.org/work/W4378348749> ?p ?o ?g. }
- W4378348749 abstract "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." @default.
- W4378348749 created "2023-05-27" @default.
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- W4378348749 date "2023-05-09" @default.
- W4378348749 modified "2023-10-17" @default.
- W4378348749 title "Reversible binding of divalent cations to Ductin protein assemblies—A putative new regulatory mechanism of membrane traffic processes" @default.
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- W4378348749 doi "https://doi.org/10.3389/fmolb.2023.1195010" @default.
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