Come a little bit closer! Lipid droplet-ER contact sites are getting crowded

Biochim Biophys Acta Mol Cell Res. 2020 Feb;1867(2):118603. doi: 10.1016/j.bbamcr.2019.118603. Epub 2019 Nov 13.


Not so long ago, contact sites between the endoplasmic reticulum (ER) and lipid droplets (LDs) were largely unexplored on a molecular level. In recent years however, numerous proteins have been identified that are enriched or exclusively located at the interfaces between LDs and the ER. These comprise members of protein classes typically found in diverse types of contacts, such as organelle tethers and lipid transfer proteins, but also proteins that have no similarities to known contact site machineries. This structurally heterogeneous group of contact site residents might be required to fulfill unique aspects of LD-ER contact biology, such as de novo LD biogenesis, and maintenance of lipidic connections between LDs and ER. Here, we summarize the current knowledge on the molecular components of this special organelle contact site, and discuss their features and functions.

Keywords: FIT2; Mdm1; Rab18; Seipin; Snx14; VPS13.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Endoplasmic Reticulum / metabolism*
  • GTP-Binding Protein gamma Subunits / chemistry
  • GTP-Binding Protein gamma Subunits / metabolism
  • Humans
  • Lipid Droplets / metabolism*
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism
  • Nuclear Proteins / chemistry
  • Nuclear Proteins / metabolism
  • Receptors, Steroid / chemistry
  • Receptors, Steroid / metabolism
  • Sorting Nexins / chemistry
  • Sorting Nexins / metabolism
  • Vesicular Transport Proteins / chemistry
  • Vesicular Transport Proteins / metabolism
  • rab GTP-Binding Proteins / chemistry
  • rab GTP-Binding Proteins / metabolism


  • BSCL2 protein, human
  • GTP-Binding Protein gamma Subunits
  • Membrane Proteins
  • Nuclear Proteins
  • Receptors, Steroid
  • Sorting Nexins
  • Vesicular Transport Proteins
  • rab GTP-Binding Proteins