VDAC1 selectively transfers apoptotic Ca2+ signals to mitochondria

被引：252

作者：

De Stefani, D. ^{[1
,2
]}

Bononi, A. ^{[3
]}

Romagnoli, A. ^{[1
,2
]}

Messina, A. ^{[4
,5
]}

De Pinto, V. ^{[4
,5
]}

Pinton, P. ^{[3
]}

Rizzuto, R. ^{[1
,2
]}

机构：

[1] Univ Padua, Dept Biomed Sci, I-35131 Padua, Italy

[2] CNR Neurosci Inst, I-35131 Padua, Italy

[3] Univ Ferrara, Dept Expt & Diagnost Med, Interdisciplinary Ctr Study Inflammat & BioPharma, I-44100 Ferrara, Italy

[4] Univ Catania, Mol Biol Sect, Dept Biol, Catania, Italy

[5] Natl Inst Biostruct & Biosyst, Catania, Italy

来源：

CELL DEATH AND DIFFERENTIATION | 2012年 / 19卷 / 02期

关键词：

mitochondria; calcium; apoptosis; VDAC1; DEPENDENT ANION CHANNEL; INOSITOL 1,4,5-TRISPHOSPHATE RECEPTOR; OUTER-MEMBRANE PERMEABILITY; ENDOPLASMIC-RETICULUM; CELL-DEATH; CALCIUM; BAK; TRANSITION; ER; ACTIVATION;

D O I：

10.1038/cdd.2011.92

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Voltage-dependent anion channels (VDACs) are expressed in three isoforms, with common channeling properties and different roles in cell survival. We show that VDAC1 silencing potentiates apoptotic challenges, whereas VDAC2 has the opposite effect. Although all three VDAC isoforms are equivalent in allowing mitochondrial Ca2+ loading upon agonist stimulation, VDAC1 silencing selectively impairs the transfer of the low-amplitude apoptotic Ca2+ signals. Co-immunoprecipitation experiments show that VDAC1, but not VDAC2 and VDAC3, forms complexes with IP3 receptors, an interaction that is further strengthened by apoptotic stimuli. These data highlight a non-redundant molecular route for transferring Ca2+ signals to mitochondria in apoptosis. Cell Death and Differentiation (2012) 19, 267-273; doi:10.1038/cdd.2011.92; published online 1 July 2011

引用

页码：267 / 273

页数：7

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