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Hydroxysteroid dehydrogenase family proteins on lipid droplets through bacteria, C. elegans, and mammals
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Liu, Yangli, Xu, Shimeng, Zhang, Congyan, Zhu, Xiaotong, Hammad, Mirza Ahmed, Zhang, Xuelin, Christian, Mark, Zhang, Hong and Liu, Pingsheng (2018) Hydroxysteroid dehydrogenase family proteins on lipid droplets through bacteria, C. elegans, and mammals. Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 1863 (8). pp. 881-894. doi:10.1016/j.bbalip.2018.04.018 ISSN 1388-1981.
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WRAP-hydrozysteroid-dehydrogenase-proteins-lipid-bacteria-Christian-2018.pdf - Accepted Version - Requires a PDF viewer. Download (8Mb) | Preview |
Official URL: http://dx.doi.org/10.1016/j.bbalip.2018.04.018
Abstract
Lipid droplets (LDs) are the main fat storing sites in almost all species from bacteria to humans. The perilipin family has been found as LD proteins in mammals, Drosophila, and a couple of slime molds, but no bacterial LD proteins containing sequence conservation were identified. In this study, we reported that the hydroxysteroid dehydrogenase (HSD) family was found on LDs across all organisms by LD proteomic analysis. Imaging experiments confirmed LD targeting of three representative HSD proteins including ro01416 in RHA1, DHS-3 in C. elegans, and 17β-HSD11 in human cells. In C. elegans, 17β-HSD11 family proteins (DHS-3, DHS-4 and DHS-19) were localized on LDs in distinct tissues. In intestinal cells of C. elegans, DHS-3 targeted to cytoplasmic LDs, while DHS-9 labeled nuclear LDs. Furthermore, the N-terminal hydrophobic domains of 17β-HSD11 family were necessary for their targeting to LDs. Last, 17β-HSD11 family proteins induced LD aggregation, and deletion of DHS-3 in C. elegans caused lipid decrease. Independent of their presumptive catalytic sites, 17β-HSD11 family proteins regulated LD dynamics and lipid metabolism through affecting the LD-associated ATGL, which was conserved between C. elegans and humans. Together, these findings for HSDs provide a new insight not only into the mechanistic studies of the dynamics and functions of LDs in multiple organisms, but also into understanding the evolutionary history of the organelle.
| Item Type: | Journal Article | |||||||||||||||||||||||||||
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| Subjects: | Q Science > QP Physiology | |||||||||||||||||||||||||||
| Divisions: | Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School > Biomedical Sciences > Cell & Developmental Biology Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School |
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| Library of Congress Subject Headings (LCSH): | Lipids, Dehydrogenases, Caenorhabditis elegans, Proteomics | |||||||||||||||||||||||||||
| Journal or Publication Title: | Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids | |||||||||||||||||||||||||||
| Publisher: | Elsevier | |||||||||||||||||||||||||||
| ISSN: | 1388-1981 | |||||||||||||||||||||||||||
| Official Date: | August 2018 | |||||||||||||||||||||||||||
| Dates: |
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| Volume: | 1863 | |||||||||||||||||||||||||||
| Number: | 8 | |||||||||||||||||||||||||||
| Page Range: | pp. 881-894 | |||||||||||||||||||||||||||
| DOI: | 10.1016/j.bbalip.2018.04.018 | |||||||||||||||||||||||||||
| Status: | Peer Reviewed | |||||||||||||||||||||||||||
| Publication Status: | Published | |||||||||||||||||||||||||||
| Access rights to Published version: | Open Access (Creative Commons) | |||||||||||||||||||||||||||
| Date of first compliant deposit: | 3 May 2018 | |||||||||||||||||||||||||||
| Date of first compliant Open Access: | 24 April 2019 | |||||||||||||||||||||||||||
| RIOXX Funder/Project Grant: |
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