Arabidopsis SEIPIN Proteins Modulate Triacylglycerol Accumulation and Influence Lipid Droplet Proliferation
Abstract
The lipodystrophy protein SEIPIN is important for lipid droplet (LD) biogenesis in human and yeast cells. In contrast with the single SEIPIN genes in humans and yeast, there are three SEIPIN homologs in Arabidopsis thaliana, designated SEIPIN1, SEIPIN2, and SEIPIN3. Essentially nothing is known about the functions of SEIPIN homologs in plants. Here, a yeast (Saccharomyces cerevisiae) SEIPIN deletion mutant strain and a plant (Nicotiana benthamiana) transient expression system were used to test the ability of Arabidopsis SEIPINs to influence LD morphology. In both species, expression of SEIPIN1 promoted accumulation of large-sized lipid droplets, while expression of SEIPIN2 and especially SEIPIN3 promoted small LDs. Arabidopsis SEIPINs increased triacylglycerol levels and altered composition. In tobacco, endoplasmic reticulum (ER)-localized SEIPINs reorganized the normal, reticulated ER structure into discrete ER domains that colocalized with LDs. N-terminal deletions and swapping experiments of SEIPIN1 and 3 revealed that this region of SEIPIN determines LD size. Ectopic overexpression of SEIPIN1 in Arabidopsis resulted in increased numbers of large LDs in leaves, as well as in seeds, and increased seed oil content by up to 10% over wild-type seeds. By contrast, RNAi suppression of SEIPIN1 resulted in smaller seeds and, as a consequence, a reduction in themore »
- Authors:
-
- Univ. of North Texas, Denton, TX (United States). Dept. of Biological Sciences, Center for Plant Lipid Research
- Univ. of Texas Southwestern Medical Center, Dallas, TX (United States). Dept. of Pharmacology
- Univ. of Guelph, ON (Canada). Dept. of Molecular and Cellular Biology
- US Dept. of Agriculture (USDA)., Ames, IA (United States). U.S. Arid-Land Agricultural Research Center, Maricopa, Arizona (United States)
- Publication Date:
- Research Org.:
- Univ. of North Texas, Denton, TX (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Biological and Environmental Research (BER)
- OSTI Identifier:
- 1441354
- Grant/Contract Number:
- SC0000797; FG02-09ER64812; 1126205
- Resource Type:
- Accepted Manuscript
- Journal Name:
- The Plant Cell
- Additional Journal Information:
- Journal Volume: 27; Journal Issue: 9; Journal ID: ISSN 1040-4651
- Publisher:
- American Society of Plant Biologists
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES
Citation Formats
Cai, Yingqi, Goodman, Joel M., Pyc, Michal, Mullen, Robert T., Dyer, John M., and Chapman, Kent D. Arabidopsis SEIPIN Proteins Modulate Triacylglycerol Accumulation and Influence Lipid Droplet Proliferation. United States: N. p., 2015.
Web. doi:10.1105/tpc.15.00588.
Cai, Yingqi, Goodman, Joel M., Pyc, Michal, Mullen, Robert T., Dyer, John M., & Chapman, Kent D. Arabidopsis SEIPIN Proteins Modulate Triacylglycerol Accumulation and Influence Lipid Droplet Proliferation. United States. https://doi.org/10.1105/tpc.15.00588
Cai, Yingqi, Goodman, Joel M., Pyc, Michal, Mullen, Robert T., Dyer, John M., and Chapman, Kent D. Tue .
"Arabidopsis SEIPIN Proteins Modulate Triacylglycerol Accumulation and Influence Lipid Droplet Proliferation". United States. https://doi.org/10.1105/tpc.15.00588. https://www.osti.gov/servlets/purl/1441354.
@article{osti_1441354,
title = {Arabidopsis SEIPIN Proteins Modulate Triacylglycerol Accumulation and Influence Lipid Droplet Proliferation},
author = {Cai, Yingqi and Goodman, Joel M. and Pyc, Michal and Mullen, Robert T. and Dyer, John M. and Chapman, Kent D.},
abstractNote = {The lipodystrophy protein SEIPIN is important for lipid droplet (LD) biogenesis in human and yeast cells. In contrast with the single SEIPIN genes in humans and yeast, there are three SEIPIN homologs in Arabidopsis thaliana, designated SEIPIN1, SEIPIN2, and SEIPIN3. Essentially nothing is known about the functions of SEIPIN homologs in plants. Here, a yeast (Saccharomyces cerevisiae) SEIPIN deletion mutant strain and a plant (Nicotiana benthamiana) transient expression system were used to test the ability of Arabidopsis SEIPINs to influence LD morphology. In both species, expression of SEIPIN1 promoted accumulation of large-sized lipid droplets, while expression of SEIPIN2 and especially SEIPIN3 promoted small LDs. Arabidopsis SEIPINs increased triacylglycerol levels and altered composition. In tobacco, endoplasmic reticulum (ER)-localized SEIPINs reorganized the normal, reticulated ER structure into discrete ER domains that colocalized with LDs. N-terminal deletions and swapping experiments of SEIPIN1 and 3 revealed that this region of SEIPIN determines LD size. Ectopic overexpression of SEIPIN1 in Arabidopsis resulted in increased numbers of large LDs in leaves, as well as in seeds, and increased seed oil content by up to 10% over wild-type seeds. By contrast, RNAi suppression of SEIPIN1 resulted in smaller seeds and, as a consequence, a reduction in the amount of oil per seed compared with the wild type. Finally, overall, our results indicate that Arabidopsis SEIPINs are part of a conserved LD biogenesis machinery in eukaryotes and that in plants these proteins may have evolved specialized roles in the storage of neutral lipids by differentially modulating the number and sizes of lipid droplets.},
doi = {10.1105/tpc.15.00588},
journal = {The Plant Cell},
number = 9,
volume = 27,
place = {United States},
year = {Tue Sep 01 00:00:00 EDT 2015},
month = {Tue Sep 01 00:00:00 EDT 2015}
}
Web of Science
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