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. 2011 Jan 1;22(1):33–43. doi: 10.1091/mbc.E10-05-0453

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© 2011 Yuan et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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FIGURE 6: — BWA overexpressor flies show no ceramidase activity. (A) Extracts from control w¹¹¹⁸, viable null cdase¹ (cdase¹ null with the suppressor mutation), and BWA overexpressors in w¹¹¹⁸ (BWA OE), and extracts from cdase¹ null lethal flies that were rescued by BWA overexpression (BWA OE; cdase¹) flies, were assayed for activity using a long-chain ceramide (d-erythro C-24 ceramide) as substrate. Control w¹¹¹⁸ and w¹¹¹⁸ overexpressing extracts show the same specific ceramidase activity against the long-chain ceramide, implying that BWA overexpression does not contribute to any observable increase in ceramidase activity at any of the three pHs indicated. Similarly, the viable allele of cdase¹ and the lethal mutant of cdase¹ rescued by overexpression of BWA show no activity when the assay is performed at the three pHs indicated. Thus BWA protein that is genetically active exhibits no biochemical ceramidase activity. All activity measurements are an average of at least six measurements, and the error bars denote SD. (B) Control extract is able to deacylate NBD-dihydroceramide, and this activity is lost in viable allele of cdase¹. The activity is not recovered in lethal mutants of cdase¹ rescued by overexpression of BWA. (C) Control extract is able to deacylate NBD-phytoceramide, and this activity is lost in viable allele of cdase¹ (suppressor, cdase¹). The activity is not recovered in lethal mutants of cdase¹ rescued by overexpression of BWA.