Details

Autor(en) / Beteiligte

• Price, Ann M.
• Doner, Nathan M.
• Gidda, Satinder K.
• Jambunathan, Srikarthika
• James, Christopher N.
• Schami, Alyssa
• Yurchenko, Olga
• Mullen, Robert T.
• Dyer, John M.
• Puri, Vishwajeet
• Chapman, Kent D.

Titel

Mouse Fat-Specific Protein 27 (FSP27) expressed in plant cells localizes to lipid droplets and promotes lipid droplet accumulation and fusion

Ist Teil von

• Biochimie, 2020-02, Vol.169 (C), p.41-53

Ort / Verlag

France: Elsevier B.V

Erscheinungsjahr

2020

Quelle

Access via ScienceDirect (Elsevier)

Beschreibungen/Notizen

• Fat-Specific Protein 27 (FSP27) belongs to a small group of vertebrate proteins containing a Cell-death Inducing DNA fragmentation factor-α-like Effector (CIDE)-C domain and is involved in lipid droplet (LD) accumulation and energy homeostasis. FSP27 is predominantly expressed in white and brown adipose tissues, as well as liver, and plays a key role in mediating LD-LD fusion. No orthologs have been identified in invertebrates or plants. In this study, we tested the function of mouse FSP27 in stably-transformed Arabidopsis thaliana leaves and seeds, as well as through transient expression in Nicotiana tabacum suspension-cultured cells and N. benthamiana leaves. Confocal microscopic analysis of plant cells revealed that, similar to ectopic expression in mammalian cells, FSP27 produced in plants 1) correctly localized to LDs, 2) accumulated at LD-LD contact sites, and 3) induced an increase in the number and size of LDs and also promoted LD clustering and fusion. Furthermore, FSP27 increased oil content in transgenic A. thaliana seeds. Given that plant oils have uses in human and animal nutrition as well as industrial uses such as biofuels and bioplastics, our results suggest that ectopic expression of FSP27 in plants represents a potential strategy for increasing oil content and energy density in bioenergy or oilseed crops. [Display omitted] •The mouse Fat-Specific Protein 27 (FSP27) was ectopically expressed in three plant systems where it localized to lipid droplets (LDs), promoted an increase in the numbers and sizes of LDs, and induced LD clustering and fusion.•The functionality of FSP27 in a plant cell context was surprising given that no obvious homologs of the protein are present in plants, suggesting that no additional factors are required for its cellular activity with LDs.•The heterologous expression of mammalian FSP27 in plants provides an attractive strategy for the manipulation of LDs in plant tissues, which may find biotechnology-related applications for the enhanced storage of lipophilic molecules in plant seeds or biomass.