Journal
PLANT PHYSIOLOGY
Volume 170, Issue 4, Pages 2052-2071Publisher
AMER SOC PLANT BIOLOGISTS
DOI: 10.1104/pp.15.01977
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Funding
- U.S. Department of Energy, Division of Biological and Environmental Research [DE-FG02-09ER64812/DE-SC0000797]
- Natural Sciences and Engineering Research Council of Canada [217291]
- University of Guelph (Research Chair)
- U.S. Department of Agriculture Agricultural Research Service [2020-21000-012-00D]
- Canadian Institutes of Health Research [10490]
- National Science Foundation [1126205]
- Direct For Biological Sciences
- Div Of Biological Infrastructure [1126205] Funding Source: National Science Foundation
- ARS [ARS-0424563, 813424] Funding Source: Federal RePORTER
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Eukaryotic cells compartmentalize neutral lipids into organelles called lipid droplets (LDs), and while much is known about the role of LDs in storing triacylglycerols in seeds, their biogenesis and function in nonseed tissues are poorly understood. Recently, we identified a class of plant-specific, lipid droplet-associated proteins (LDAPs) that are abundant components of LDs in nonseed cell types. Here, we characterized the three LDAPs in Arabidopsis (Arabidopsis thaliana) to gain insight to their targeting, assembly, and influence on LD function and dynamics. While all three LDAPs targeted specifically to the LD surface, truncation analysis of LDAP3 revealed that essentially the entire protein was required for LD localization. The association of LDAP3 with LDs was detergent sensitive, but the protein bound with similar affinity to synthetic liposomes of various phospholipid compositions, suggesting that other factors contributed to targeting specificity. Investigation of LD dynamics in leaves revealed that LD abundance was modulated during the diurnal cycle, and characterization of LDAP misexpression mutants indicated that all three LDAPs were important for this process. LD abundance was increased significantly during abiotic stress, and characterization of mutant lines revealed that LDAP1 and LDAP3 were required for the proper induction of LDs during heat and cold temperature stress, respectively. Furthermore, LDAP1 was required for proper neutral lipid compartmentalization and triacylglycerol degradation during postgerminative growth. Taken together, these studies reveal that LDAPs are required for the maintenance and regulation of LDs in plant cells and perform nonredundant functions in various physiological contexts, including stress response and postgerminative growth.
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