Regulation of Single-Channel Conductance of Voltage-Dependent Anion Channel by Mercuric Chloride in a Planar Lipid Bilayer

Malik, C. P.; Ghosh, Subhendu

doi:10.1007/s00232-020-00134-1

Cited by 6 publications

(3 citation statements)

References 62 publications

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“…It may be remembered here that VDAC1’s gating is regulated mainly by the mitochondrial membrane potential. As mentioned in the Introduction it is also influenced by various metabolites, ligands (such as Bax and Bid, , plasminogen, mercuric chloride, quinidine, and hydrogen peroxide), and post-translational modifications by enzymes − (such as Protein Kinase A , and MAP kinases). ,,, …”

Section: Discussionmentioning

confidence: 99%

“…As mentioned in the Introduction it is also influenced by various metabolites, ligands (such as Bax and Bid, 9,10 plasminogen, 11 mercuric chloride, 12 quinidine, 13 and hydrogen peroxide), 14 and post-translational modifications by enzymes 15−18 (such as Protein Kinase A 19,20 and MAP kinases). 10,17,21,22 Preliminary bioinformatics analysis suggests that VDAC1 possesses multiple binding sites for CaM.…”

Section: Discussionmentioning

confidence: 99%

“…On the contrary, recombinant hVDAC3 has been reported to form a relatively small conductance channel in the bilayer lipid membrane (BLM) . The gating properties of VDAC1 depend on the membrane potential, interaction with various metabolites, and ligands, such as Bax and Bid, , plasminogen, mercuric chloride, quinidine, and hydrogen peroxide, and post-translational modifications by enzymes, − e.g., protein kinase A , and mitogen-activated protein (MAP) kinases. ,,, Moreover, VDAC1 is one of the primary regulators of OMM permeability, mediating cytochrome c release, where critical mitochondrial Ca 2+ concentration is an essential determinant of a cell’s response to apoptotic signals …”

Section: Introductionmentioning

confidence: 99%

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Calmodulin Modulates the Gating Properties of Voltage-Dependent Anion Channel from Rat Brain Mitochondria

et al. 2022

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Calmodulin (CaM) is a key signaling protein that plays a decisive role in mitochondrial Ca2+ homeostasis and signaling and modulates the mitochondrial membrane properties. We propose that voltage-dependent anion channel 1 (VDAC1), one of the most abundant outer mitochondrial membrane (OMM) proteins, could be its possible target or site of action. VDAC1 is known to play a crucial role in the mitochondrial Ca2+ signaling mechanism. Bilayer electrophysiology experiments show that CaM significantly reduces VDAC1’s conductivity and modulates its gating as well as permeability properties. Also, spectrofluorimetric analysis indicates the possibility of binding CaM with VDAC1. Theoretical analysis of fluorescence data shows that the aforementioned protein–protein interaction is not linear, but rather it is a complex nonlinear process. In VDAC1, CaM binding site has been predicted using various bioinformatics tools. It is proposed that CaM could interact with VDAC1’s outer-loop region and regulate its gating properties. Our findings suggest that VDAC1–CaM interaction could play a crucial role in the transport of ions and metabolites through the OMM and the regulation of the mitochondrial Ca2+ signaling mechanism through alteration of VDAC1’s gating and conductive properties.

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