Regulation of lipid droplet dynamics and lipid homeostasis by hydroxysteroid dehydrogenase proteins.

Trends Cell Biol

Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China; University of the Chinese Academy of Sciences, Beijing 100049, China. Electronic address:

Published: November 2024

AI Article Synopsis

  • The superfamily of hydroxysteroid dehydrogenases (HSDs) includes enzymes crucial for lipid and steroid hormone metabolism across various organisms.
  • Recent studies have identified a subset of these enzymes, like 3β-HSD, 11β-HSD, and 17β-HSD, as proteins associated with lipid droplets (LDs) that play roles in LD dynamics beyond their typical functions.
  • The review explored these LD-associated HSDs, detailing their regulation of different neutral lipids, the preservation of lipids by 17β-HSDs, and the potential for targeting these enzymes in treating metabolic diseases and viral infections.

Article Abstract

The superfamily of hydroxysteroid dehydrogenases (HSDs) has been well-characterized as enzymes in lipid metabolism, and especially in steroid hormone metabolism from bacteria to mammals. Recently, a subset of HSDs members, including 3β-HSD, 11β-HSD, and 17β-HSD, have been shown to be lipid droplet (LD)-associated proteins that are involved in LD dynamics beyond their canonical functions. This review summarizes current understanding of these LD-associated HSD proteins, focusing on how they regulate different LDs with respect to distinct neutral lipids including triacylglycerols (TAGs), cholesterol esters (CEs), and retinyl esters (REs), the evolutionally conserved role of some LD-associated 17β-HSDs in preventing lipolysis, and specific targeting of HSDs for the treatment of metabolic diseases and viral infections.

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Source
http://dx.doi.org/10.1016/j.tcb.2024.10.010DOI Listing

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