Lipid Droplet–Peroxisome Connections in Plants. (February 2020)

• Record Type: Journal Article
• Authors: Esnay, Nicolas; Dyer, John M.; Mullen, Robert T.; Chapman, Kent D.
• Is Part Of: Contact. Volume 3(2020)
• Publication Date: 2020-02
• Subjects: lipid droplet -- lipid -- FFAT (FFAT-like) -- peroxisome -- vesicle-associated membrane protein-associated protein; Cell interaction -- Periodicals; Cells -- Periodicals; Cytology -- Periodicals; 571.6
• DOI: 10.1177/2515256420908765
• Languages: English
• ISSNs: 2515-2564

Abstract

Lipid droplets (LDs) are the principal subcellular sites for the storage of triacylglycerols (TAGs), and in plants, TAG degradation requires metabolism in peroxisomes. This metabolic cooperation includes TAG hydrolysis by the sugar-dependent 1 lipase located on the LD surface and the transfer of fatty acids into the peroxisome matrix by the peroxisomal membrane ATP-binding cassette transporter, PXA1. During seed germination, this process fuels heterotrophic growth and involves the retromer-dependent formation of peroxisomal membrane extensions called peroxules that interact with LDs. Similar changes in membrane architecture are also observed during interactions of peroxisomes and LDs in yeast and mammalian cells, despite differences in the molecular components required for their connections. Proteins directly involved in LD–peroxisome membrane contact site formation in plants have not yet been identified, but the connection between these two organelles is dependent upon PXA1, which contains a cytoplasmic exposed FFAT (two phenylalanines in an acidic tract)-like motif capable of interacting with vesicle-associated membrane protein-associated proteins (VAPs). Indeed, the identification of several VAPs in plant LD proteomes supports the premise that a VAP-PXA1 connection might be part of a functional tethering complex that connects these two organelles, although other types of interactions are also possible. Overall, such connections between peroxisomes and LDs would allow for efficient transfer of lipophilic substrates from LDs to the peroxisome matrix in plant cells, similar to how VAPs participate in lipid transfer reactions between other subcellular compartments in eukaryotic systems.