Human Brown Fat Inducible Thioesterase Variant 2 Cellular Localization and Catalytic Function
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- 作者：Danqi Chen ; John Latham ; Hong Zhao ; Marco Bisoffi ; Jeremiah Farelli ; Debra Dunaway-Mariano
- 刊名：Biochemistry
- 出版年：2012
- 出版时间：September 4, 2012
- 年：2012
- 卷：51
- 期：35
- 页码：6990-6999
- 全文大小：463K
- 年卷期：v.51,no.35(September 4, 2012)
- ISSN：1520-4995
文摘
The mammalian brown fat inducible thioesterase variant 2 (BFIT2), also known as ACOT11, is a multimodular protein containing two consecutive hotdog-fold domains and a C-terminal steroidogenic acute regulatory protein-related lipid transfer domain (StarD14). In this study, we demonstrate that the N-terminal region of human BFIT2 (hBFIT2) constitutes a mitochondrial location signal sequence, which undergoes mitochondrion-dependent posttranslational cleavage. The mature hBFIT2 is shown to be located in the mitochondrial matrix, whereas the paralog 鈥渃ytoplasmic acetyl-CoA hydrolase鈥?(CACH, also known as ACOT12) was found in the cytoplasm. In vitro activity analysis of full-length hBFIT2 isolated from stably transfected HEK293 cells demonstrates selective thioesterase activity directed toward long chain fatty acyl-CoA thioesters, thus distinguishing the catalytic function of BFIT2 from that of CACH. The results from a protein鈥搇ipid overlay test indicate that the hBFIT2 StarD14 domain binds phosphatidylinositol 4-phosphate.