期刊
BIOCHEMISTRY
卷 50, 期 17, 页码 3408-3410出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi2003247
关键词
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资金
- Arnold and Mabel Beckman Foundation
- NYSTAR
- National Institutes of Health [R01CA097061, R01GM085081, RC2CA148308, R01GM88724]
Voltage-dependent anion channels (VDACs) are critical regulators of outer mitochondrial membrane permeability in eukaryotic cells. VDACs have also been postulated to regulate cell death mechanisms. Erastin, a small molecule quinazolinone that is selectively lethal to tumor cells exopressing mutant RAS, has previously been reported as a ligant for hVDAC2. While significant efforts have been made to elucidate the structure and function of hVDAC1, structural and functional characterization of hVDAC2 remains lacking. Here, we present an in vitro system that provides a platform for both functional and structural investigation of hVDAC2 and its Small molecule modulator,erastin. Using this system, we found that erastin increases permeability,of VDAC2 liposomes to NADH in a manner that requires the amino-terminal 'region Of VDAC2. Furthermore, We-confirmed that this VDAC2-lipsome sample, is folded:using soli-state NMR.
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