Carnitine/acylcarnitine translocase and carnitine palmitoyltransferase 2 form a complex in the inner mitochondrial membrane

被引：22
作者：
Console, Lara [1 ,2 ]
Giangregorio, Nicola [2 ,3 ]
Indiveri, Cesare [1 ]
Tonazzi, Annamaria [2 ,3 ]
机构：
[1] Univ Calabria, Dept BEST, Unit Biochem & Mol Biotechnol, I-87036 Cosenza, Italy
[2] Univ Bari, Dept Biosci Biotechnol & Pharmacol Sci, Bari, Italy
[3] CNR, Inst Biomembranes & Bioenerget, I-70126 Bari, Italy
来源：
MOLECULAR AND CELLULAR BIOCHEMISTRY | 2014年 / 394卷 / 1-2期
关键词：
Protein-protein interaction; beta-oxidation; Carnitine; Mitochondria; Channeling; SITE-DIRECTED MUTAGENESIS; RESPIRATORY-CHAIN; NATIVE ELECTROPHORESIS; PROTEIN COMPLEXES; CARRIER; LIVER; IDENTIFICATION; PURIFICATION; CARDIOLIPIN; ASSOCIATION;
D O I：
10.1007/s11010-014-2098-z
中图分类号：
Q2 [细胞生物学];
学科分类号：
071009 ; 090102 ;
摘要：
Carnitine/acylcarnitine translocase and carnitine palmitoyltransferase 2 are members of the carnitine system, which are responsible of the regulation of the mitochondrial CoA/acyl-CoA ratio and of supplying substrates for the -oxidation to mitochondria. This study, using cross-Linking reagent, Blue native electrophoresis and immunoprecipitation followed by detection with immunoblotting, shows conclusive evidence about the interaction between carnitine palmitoyltransferase 2 and carnitine/acylcarnitine translocase supporting the channeling of acylcarnitines and carnitine at level of the inner mitochondrial membrane.
引用
收藏
页码：307 / 314
页数：8
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