α/β hydrolase domain-containing protein 1 acts as a lysolipid lipase and is involved in lipid droplet formation
Lipid droplets (LDs) are the major sites of lipid and energy homeostasis. However, few LD biogenesis proteins have been identified. Using model microalga <i>Chlamydomonas</i>, we show that ABHD1, an α/β-hydrolase domain-containing protein, is localized to the LD surface and stimulates LD formation through two actions: one enzymatic and one structural. The knockout mutants contained similar amounts of triacylglycerols (TAG) but their LDs showed a higher content of lyso-derivatives of betaine lipid diacylglyceryl-<i>N,N,N</i>-trimethylhomoserine (DGTS). Over-expression of <i>ABHD1</i> increased LD abundance and boosted TAG content. Purified recombinant ABHD1 hydrolyzed lyso-DGTS, producing a free fatty acid and a glyceryltrimethylhomoserine. <i>In vitro</i> droplet-embedded vesicles showed that ABHD1 promoted LD emergence. Taken together, these results identify ABHD1 as a new player in LD formation by its lipase activity on lyso-DGTS and by its distinct biophysical property. This study further suggests that lipases targeted to LDs and able to act on their polar lipid coat may be interesting tools to promote LD assembly in eukaryotic cells.
Authors
- Damien Sorigue
- Fred Beisson (ORCID: https://orcid.org/0000-0001-9995-7387)
- Ismael Torres-Romero (ORCID: https://orcid.org/0000-0003-1367-8913)
- Florian Veillet (ORCID: https://orcid.org/0000-0002-6892-6825)
- Philip D. Bates (ORCID: https://orcid.org/0000-0002-1291-3363)
- Abdou Rachid Thiam (ORCID: https://orcid.org/0000-0001-7488-4724)
- Stéphan Cuiné (ORCID: https://orcid.org/0000-0002-3000-3355)
- Carla Blot (ORCID: https://orcid.org/0009-0001-9581-8598)
- Alicia Damm (ORCID: https://orcid.org/0000-0001-9291-8545)
- Hari Kiran Kotapati
- Matthew G. Garneau (ORCID: https://orcid.org/0000-0001-6113-1360)
- Sabine Brugière (ORCID: https://orcid.org/0000-0002-0757-0968)
- Bertrand Légeret (ORCID: https://orcid.org/0000-0002-0957-4700)
- Jian Xu (ORCID: https://orcid.org/0000-0002-0548-8477)
- Yohann Couté (ORCID: https://orcid.org/0000-0003-3896-6196)
- Xin Yi (ORCID: https://orcid.org/0000-0002-5686-2967)
- Marie Bertrand (ORCID: https://orcid.org/0000-0001-5098-1554)
- Yonghua Li‐Beisson (ORCID: https://orcid.org/0000-0003-1064-1816)
Institutions
- Centre National de la Recherche Scientifique (FR)
- Inserm (FR)
- Chinese Academy of Sciences (CN)
- Université Paris Cité (FR)
- Commissariat à l'Énergie Atomique et aux Énergies Alternatives (FR)
- Université Paris Sciences et Lettres (FR)
- École Normale Supérieure - PSL (FR)
- CEA Grenoble (FR)
- Sorbonne Université (FR)
- École Normale Supérieure (BI)
- CEA Cadarache (FR)
- Institut de Biosciences et Biotechnologies (FR)
- Qingdao Institute of Bioenergy and Bioprocess Technology (CN)
- Washington State University (US)
- Université Grenoble Alpes (FR)
Publication Details
- Journal
- National Science Review
- Published
- 2024-11-07
- DOI
- https://doi.org/10.1093/nsr/nwae398
- Citations
- 5
- Primary Topic
- Lipid metabolism and biosynthesis
- Type
- article
- Field-Weighted Citation Impact
- 1.47
Funders
- National Science Foundation
- University of Minnesota
- California Earthquake Authority
- European Commission
- Agence Nationale de la Recherche
- Chinese Academy of Sciences
- Commissariat à l'Énergie Atomique et aux Énergies Alternatives
- European Regional Development Fund