StarD10, a START domain protein overexpressed in breast cancer, functions as a phospholipid transfer protein

Olayioye, MA; Vehring, S; Muller, P; Herrmann, A; Schiller, J; Thiele, C; Lindeman, GJ; Visvader, JE; Pomorski, T

Author(s): Olayioye, MA; Vehring, S; Muller, P; Herrmann, A; Schiller, J; Thiele, C; Lindeman, GJ; Visvader, JE; Pomorski, T;
Details: Publication Year 2005-07-22,Volume 280,Issue #29,Page 27436-27442
Journal Title: JOURNAL OF BIOLOGICAL CHEMISTRY
Publication Type: Journal Article
Abstract: We originally identified StarD10 as a protein overexpressed in breast cancer that cooperates with the ErbB family of receptor tyrosine kinases in cellular transformation. StarD10 contains a steroidogenic acute regulatory protein (StAR/StarD1)-related lipid transfer ( START) domain that is thought to mediate binding of lipids. We now provide evidence that StarD10 interacts with phosphatidylcholine ( PC) and phosphatidylethanolamine ( PE) by electron spin resonance measurement. Interaction with these phospholipids was verified in a fluorescence resonance energy transfer-based assay with 7-nitro-2,1,3-benzoxadiazol-4- yl-labeled lipids. Binding was not restricted to lipid analogs since StarD10 selectively extracted PC and PE from small unilamellar vesicles prepared with endogenous radiolabeled lipids from Vero monkey kidney cells. Mass spectrometry revealed that StarD10 preferentially selects lipid species containing a palmitoyl or stearoyl chain on the sn-1 and an unsaturated fatty acyl chain ( 18: 1 or 18: 2) on the sn-2 position. StarD10 was further shown to bind lipids in vivo by cross-linking of protein expressed in transfected HEK-293T cells with photoactivable phosphatidylcholine. In addition to a lipid binding function, StarD10 transferred PC and PE between membranes. Interestingly, these lipid binding and transfer specificities distinguish StarD10 from the related START domain proteins Pctp and CERT, suggesting a distinct biological function.
Publisher: AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Keywords: PHOSPHATIDYLCHOLINE TRANSFER PROTEIN; PHOSPHATIDYLINOSITOL TRANSFER PROTEIN; ASSISTED LASER-DESORPTION; MASS-SPECTROMETRY; INTRACELLULAR TRAFFICKING; BOVINE LIVER; CHOLESTEROL; MEMBRANES; BINDING; LIPIDS
Publisher's Version: https://doi.org/10.1074/jbc.M413330200
Terms of Use/Rights Notice: Refer to copyright notice on published article.

Creation Date: 2005-07-22 12:00:00