TAILIEUCHUNG - Báo cáo khoa học: Cholesterol interaction with the related steroidogenic acute regulatory lipid-transfer (START) domains of StAR (STARD1) and MLN64 (STARD3)

The steroidogenic acute regulatory (StAR)-related lipid transfer (START) domains are found in a wide range of proteins involved in intracellular trafficking of cholesterol and other lipids. Among the START proteins are the StAR protein itself (STARD1) and the closely related MLN64 protein (STARD3), which both function in cholesterol movement. | ễFEBS Journal Cholesterol interaction with the related steroidogenic acute regulatory lipid-transfer START domains of StAR STARD1 and MlN64 STARD3 Julian Reitz1 Katja Gehrig-Burger1 Jerome F. Strauss III2 and Gerald Gimpl1 1 Institute of Biochemistry Gutenberg-University Mainz Germany 2 Department of Obstetrics Gynecology Virginia Commonwealth University Richmond VA USA Keywords cholesterol MLN64 STARD1 STARD3 START proteins Correspondence G. Gimpl Institute of Biochemistry Gutenberg-University Mainz Becherweg 30 55128 Mainz Germany Fax 49 6131 3925348 Tel 49 6131 3923829 E-mail gimpl@ Received 14 January 2008 revised 5 February 2008 accepted 14 February 2008 doi The steroidogenic acute regulatory StAR -related lipid transfer START domains are found in a wide range of proteins involved in intracellular trafficking of cholesterol and other lipids. Among the START proteins are the StAR protein itself STARD1 and the closely related MLN64 protein STARD3 which both function in cholesterol movement. We compared the cholesterol-binding properties of these two START domain proteins. Cholesterol stabilized STARD3-START against trypsin-catalyzed degradation whereas cholesterol had no protective effect on STARD1-START. 3H Azocholestanol predominantly labeled a kDa fragment of STARD1-START comprising amino acids 83-140 which contains residues proposed to interact with cholesterol in a hydrophobic cavity. Photoaffinity labeling studies suggest that cholesterol preferentially interacts with one side wall of this cavity. In contrast 3H azocholestanol was distributed more or less equally among the polypeptides of STARD3-START. Overall our results provide evidence for differential cholesterol binding of the two most closely related START domain proteins STARD1 and STARD3. Cholesterol is an essential multifunctional lipid in most eukaryotic cells. It exerts a strong influence on the physical state of the plasma membrane forms .

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