NDLI: An Interaction between $Bcl-x_{L}$ and the Voltage-dependent Anion Channel (VDAC) Promotes Mitochondrial $Ca^{2+}$ Uptake

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An Interaction between $Bcl-x_{L}$ and the Voltage-dependent Anion Channel (VDAC) Promotes Mitochondrial $Ca^{2+}$ Uptake

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An Interaction between $Bcl-x_{L}$ and the Voltage-dependent Anion Channel (VDAC) Promotes Mitochondrial $Ca^{2+}$ Uptake

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Huang, Huiya Hu, Xiangxin Li, Chi White, Carl Eno, Colins O. Zhao, Guoping
Description	Author Affiliation: Huang H ( Department of Physiology and Biophysics, Rosalind Franklin University of Medicine and Science, North Chicago, Illinois 60064, USA.)
Abstract	The role of the antiapoptotic protein Bcl-xL in regulating mitochondrial Ca(2+) ([Ca(2+)]mito) handling was examined in wild-type (WT) and Bcl-xL knock-out (Bcl-xL-KO) mouse embryonic fibroblast cells. Inositol 1,4,5-trisphosphate-generating agonist evoked cytosolic Ca(2+) transients that produced a larger [Ca(2+)]mito uptake in WT cells compared with Bcl-xL-KO. In permeabilized cells, stepping external [Ca(2+)] from 0 to 3 µm also produced a larger [Ca(2+)]mito uptake in WT; moreover, the [Ca(2+)]mito uptake capacity of Bcl-xL-KO cells was restored by re-expression of mitochondrially targeted Bcl-xL. Bcl-xL enhancement of [Ca(2+)]mito uptake persisted after dissipation of the mitochondrial membrane potential but was absent in mitoplasts lacking an outer mitochondrial membrane. The outer membrane-localized voltage-dependent anion channel (VDAC) is a known Ca(2+) permeability pathway that directly interacts with Bcl-xL. Bcl-xL interacted with VDAC1 and -3 isoforms, and peptides based on the VDAC sequence disrupted Bcl-xL binding. Peptides reduced [Ca(2+)]mito uptake in WT but were without effect in Bcl-xL-KO cells. In addition, peptides reduced [Ca(2+)]mito uptake in VDAC1 and VDAC3 knock-out but not VDAC1 and -3 double knock-out mouse embryonic fibroblast cells, confirming that Bcl-xL interacts functionally with VDAC1 and -3 but not VDAC2. Thus, an interaction between Bcl-xL and VDAC promotes matrix Ca(2+) accumulation by increasing Ca(2+) transfer across the outer mitochondrial membrane.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	27
Volume Number	288
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2013-07-05
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Calcium Metabolism Embryo, Mammalian Fibroblasts Mitochondria Mitochondrial Membranes Mitochondrial Proteins Voltage-Dependent Anion Channels Bcl-X Protein Animals Cells, Cultured Cytology Mice Mice, Knockout Genetics Protein Binding Protein Isoforms Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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