CDase is a pan-ceramidase in Drosophila

Changqing Yuan, Raghavendra Pralhada Rao, Nahid Jesmin, Takeshi Bamba, Kunio Nagashima, Alberto Pascual, Thomas Preat, Eiichiro Fukusaki, Usha Acharya, Jairaj K. Acharya

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Ceramidases catalyze the conversion of ceramide to sphingosine. They are acylaminohydrolases that catalyze the deacylation of the amide-linked saturated fatty acid from ceramide to generate sphingosine. They also catalyze the reverse reaction of ceramide biosynthesis using sphingosine and fatty acid. In mammals, different proteins catalyze these reactions while individually exhibiting optimal activity over a narrow pH range and have been accordingly called acid, neutral, and alkaline ceramidases. Several genes encode for variants of alkaline ceramidase in mammals. Brainwashing (Bwa) is the only putative alkaline ceramidase homologue present in Drosophila. In this study we have demonstrated that BWA does not exhibit ceramidase activity and that bwa null mutants display no loss of ceramidase activity. Instead, the neutral ceramidase gene CDase encodes the protein that is responsible for all measurable ceramidase activity in Drosophila. Our studies show strong genetic interaction of Bwa with CDase and the Drosophila ceramide kinase gene (DCERK). We show that, although BWA is unlikely to be a ceramidase, it is a regulator of sphingolipid flux in Drosophila. Bwa exhibits strong genetic interaction with other genes coding for ceramide-metabolizing enzymes. This interaction might partly explain its original identification as a ceramidase.

Original languageEnglish
Pages (from-to)33-43
Number of pages11
JournalMolecular biology of the cell
Volume22
Issue number1
DOIs
Publication statusPublished - Jan 1 2011

Fingerprint

Ceramidases
Alkaline Ceramidase
Drosophila
Ceramides
Persuasive Communication
Neutral Ceramidase
Sphingosine
Genes
Acid Ceramidase
Mammals
Fatty Acids
Sphingolipids
Amides
Proteins
Enzymes

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

Cite this

Yuan, C., Rao, R. P., Jesmin, N., Bamba, T., Nagashima, K., Pascual, A., ... Acharya, J. K. (2011). CDase is a pan-ceramidase in Drosophila. Molecular biology of the cell, 22(1), 33-43. https://doi.org/10.1091/mbc.E10-05-0453

CDase is a pan-ceramidase in Drosophila. / Yuan, Changqing; Rao, Raghavendra Pralhada; Jesmin, Nahid; Bamba, Takeshi; Nagashima, Kunio; Pascual, Alberto; Preat, Thomas; Fukusaki, Eiichiro; Acharya, Usha; Acharya, Jairaj K.

In: Molecular biology of the cell, Vol. 22, No. 1, 01.01.2011, p. 33-43.

Research output: Contribution to journalArticle

Yuan, C, Rao, RP, Jesmin, N, Bamba, T, Nagashima, K, Pascual, A, Preat, T, Fukusaki, E, Acharya, U & Acharya, JK 2011, 'CDase is a pan-ceramidase in Drosophila', Molecular biology of the cell, vol. 22, no. 1, pp. 33-43. https://doi.org/10.1091/mbc.E10-05-0453
Yuan C, Rao RP, Jesmin N, Bamba T, Nagashima K, Pascual A et al. CDase is a pan-ceramidase in Drosophila. Molecular biology of the cell. 2011 Jan 1;22(1):33-43. https://doi.org/10.1091/mbc.E10-05-0453
Yuan, Changqing ; Rao, Raghavendra Pralhada ; Jesmin, Nahid ; Bamba, Takeshi ; Nagashima, Kunio ; Pascual, Alberto ; Preat, Thomas ; Fukusaki, Eiichiro ; Acharya, Usha ; Acharya, Jairaj K. / CDase is a pan-ceramidase in Drosophila. In: Molecular biology of the cell. 2011 ; Vol. 22, No. 1. pp. 33-43.
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