May 25, 2005

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

The Journal of Biological Chemistry
Monilola A OlayioyeThomas Pomorski

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 t...Continue Reading

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Mentioned in this Paper

STARD10 protein, human
Tissue Membrane
Analog
COL4A3BP gene
Phospholipid scramblase
Lipid Binding
Phosphatidylethanolamine
Plasma Protein Binding Capacity
Mass Spectrometry
Staphylococcal Protein A

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