FB2026_03 , released September 17, 2026
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Citation
Dumas, S., Ntambi, J.M. (2017). Co-conspirators in a new mechanism for the degradation of Δ9-desaturase.  J. Biol. Chem. 292(49): 19987--19988.
FlyBase ID
FBrf0237561
Publication Type
Note
Abstract
Δ9-Desaturases are central enzymes in unsaturated fatty acid synthesis regulated at the transcriptional and mRNA levels and by proteasomal degradation. A new study by Murakami et al. uncovers a novel regulatory pathway in which an N-terminal di-proline motif in the Drosophila Δ9-desaturase mediates protein degradation by a calcium-dependent cysteine protease in response to unsaturated fatty acids. This study provides new details of desaturase regulation with therapeutic implications for the treatment of metabolic syndrome.
PubMed ID
PubMed Central ID
PMC5723987 (PMC) (EuropePMC)
Related Publication(s)
Research paper

An N-terminal di-proline motif is essential for fatty acid-dependent degradation of Δ9-desaturase in Drosophila.
Murakami et al., 2017, J. Biol. Chem. 292(49): 19976--19986 [FBrf0237449]

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Secondary IDs
    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    J. Biol. Chem.
    Title
    Journal of Biological Chemistry
    Publication Year
    1905-
    ISBN/ISSN
    0021-9258
    Data From Reference