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J Biol Chem. 2017 Dec 8;292(49):19987-19988. doi: 10.1074/jbc.H117.801936.

Co-conspirators in a new mechanism for the degradation of Δ9-desaturase.

Author information

1
From the Departments of Nutritional Sciences and.
2
From the Departments of Nutritional Sciences and james.ntambi@wisc.edu.
3
Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706.

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.

PMID:
29222194
PMCID:
PMC5723987
DOI:
10.1074/jbc.H117.801936
[Indexed for MEDLINE]
Free PMC Article

Conflict of interest statement

The authors declare that they have no conflicts of interests with the contents of this article. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health, American Diabetes Association, or U.S. Department of Agriculture.

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