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J. Biol. Chem., Vol. 280, Issue 29, 27436-27442, July 22, 2005

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StarD10, a START Domain Protein Overexpressed in Breast Cancer, Functions as a Phospholipid Transfer Protein^*

Monilola A. Olayioye, Stefanie Vehring¶, Peter Müller¶, Andreas Herrmann¶, Jürgen Schiller||, Christoph Thiele**, Geoffrey J. Lindeman, Jane E. Visvader, and Thomas Pomorski¶

From the The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Victoria 3050, Australia, ^¶Humboldt University of Berlin, Institute of Biology, Invalidenstrasse 42, 10115 Berlin, Germany, ^||University of Leipzig, Medical Faculty, Institute of Medical Physics and Biophysics, 04103 Leipzig, Germany, ^**Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany, and University of Stuttgart, Institute of Cell Biology and Immunology, Allmandring 31, 70569 Stuttgart, Germany

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.

Received for publication, November 26, 2004 , and in revised form, May 20, 2005.

^* This work was supported by the Deutsche Forschungsgemeinschaft (to T. P. and P. M.; Mu 1017/2), Interdisziplinäre Zentrum für Klinische Forschung, Leipzig at the Faculty of Medicine of the University of Leipzig (to J. S.), and European Molecular Biology Organization and Human Frontier Science Program Organization fellowships (to M. A. O.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains Supplemental Fig. 1 and Table 1.

To whom correspondence should be addressed: Humboldt University of Berlin, Institute of Biology, Dept. of Cell Biophysics, Invalidenstrasse 42, 10115 Berlin, Germany. Tel.: 49-30-2093-8326; Fax: 49-30-2093-8585; E-mail: thomas.pomorski{at}rz.hu-berlin.de.

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