scholarly journals Corrigendum to: The human Bcl-2 family member Bcl-rambo and voltage-dependent anion channels manifest a genetic interaction in Drosophila and cooperatively promote the activation of effector caspases in human cultured cells

2021 ◽  
pp. 112711
Author(s):  
Hisanori Matsubara ◽  
Reiji Tanaka ◽  
Tatsuya Tateishi ◽  
Hideki Yoshida ◽  
Masamitsu Yamaguchi ◽  
...  
2007 ◽  
Vol 9 (5) ◽  
pp. 550-555 ◽  
Author(s):  
Christopher P. Baines ◽  
Robert A. Kaiser ◽  
Tatiana Sheiko ◽  
William J. Craigen ◽  
Jeffery D. Molkentin

1998 ◽  
Vol 275 (3) ◽  
pp. C646-C652 ◽  
Author(s):  
Guy Droogmans ◽  
Jean Prenen ◽  
Jan Eggermont ◽  
Thomas Voets ◽  
Bernd Nilius

We have studied the effects of calix[4]arenes on the volume-regulated anion channel (VRAC) currents in cultured calf pulmonary artery endothelial cells. TS- and TS-TM-calix[4]arenes induced a fast inhibition at positive potentials but were ineffective at negative potentials. Maximal block occurred at potentials between 30 and 50 mV. Lowering extracellular pH enhanced the block and shifted the maximum inhibition to more negative potentials. Current inhibition was also accompanied by an increased current noise. From the analysis of the calix[4]arene-induced noise, we obtained a single-channel conductance of 9.3 ± 2.1 pS ( n = 9) at +30 mV. The voltage- and time-dependent block were described using a model in which calix[4]arenes bind to a site at an electrical distance of 0.25 inside the channel with an affinity of 220 μM at 0 mV. Binding occludes VRAC at moderately positive potentials, but calix[4]arenes permeate the channel at more positive potentials. In conclusion, our data suggest an open-channel block of VRAC by calix[4]arenes that also depends on the protonation of the binding site within the pore.


2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Antal Nyeste ◽  
Claudia Stincardini ◽  
Petra Bencsura ◽  
Milica Cerovic ◽  
Emiliano Biasini ◽  
...  

Cells ◽  
2020 ◽  
Vol 9 (4) ◽  
pp. 1023 ◽  
Author(s):  
Mickaële Hemono ◽  
Élodie Ubrig ◽  
Kevin Azeredo ◽  
Thalia Salinas-Giegé ◽  
Laurence Drouard ◽  
...  

Voltage-dependent anion channels (VDACs) are essential components of the mitochondrial outer membrane. VDACs are involved in the exchange of numerous ions and molecules, from ATP to larger molecules such as tRNAs, and are supposed to adjust exchanges in response to cell signals and stresses. Four major VDACs have been identified in Arabidopsis thaliana. The goal of this study was to explore the specific functions of these proteins, in particular, in tRNA import into mitochondria and stress response. The main results were: (i) VDACs appeared to differentially interact with tRNAs, and VDAC4 could be the major tRNA channel on the outer membrane, (ii) a VDAC3 mRNA isoform was found induced by different stresses, suggesting that VDAC3 might be specifically involved in early steps of stress response and (iii) an analysis of vdac3 and vdac1 mutant lines showed that VDAC3 and VDAC1 shared some, but not all functions. In conclusion, this work brings new knowledge on VDACs, which do not appear as interchangeable pores of the outer membrane and each VDAC has its own specificity.


PLoS ONE ◽  
2010 ◽  
Vol 5 (12) ◽  
pp. e15192 ◽  
Author(s):  
Eunkuk Park ◽  
Gi-Ja Lee ◽  
Samjin Choi ◽  
Seok-Keun Choi ◽  
Su-Jin Chae ◽  
...  

2009 ◽  
Vol 28 (9) ◽  
pp. 1301-1308 ◽  
Author(s):  
Tomonobu Kusano ◽  
Chika Tateda ◽  
Thomas Berberich ◽  
Yoshihiro Takahashi

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