Touché! STARD3 and STARD3NL tether the ER to endosomes

Biochem Soc Trans. 2016 Apr 15;44(2):493-8. doi: 10.1042/BST20150269.

Abstract

Membrane contact sites (MCSs) are subcellular regions where the membranes of distinct organelles come into close apposition. These specialized areas of the cell, which are involved in inter-organelle metabolite exchange, are scaffolded by specific complexes. STARD3 [StAR (steroidogenic acute regulatory protein)-related lipid transfer domain-3] and its close paralogue STARD3NL (STARD3 N-terminal like) are involved in the formation of contacts between late-endosomes and the endoplasmic reticulum (ER). The lipid transfer protein (LTP) STARD3 and STARD3NL, which are both anchored on the limiting membrane of late endosomes (LEs), interact with ER-anchored VAP [VAMP (vesicle-associated membrane protein)-associated protein] (VAP-A and VAP-B) proteins. This direct interaction allows ER-endosome contact formation. STARD3 or STARD3NL-mediated ER-endosome contacts, which affect endosome dynamics, are believed to be involved in cholesterol transport.

Keywords: cholesterol; endoplasmic reticulum; endosome; lipid transfer protein; membrane contact site.

Publication types

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

MeSH terms

  • Binding Sites
  • Biological Transport
  • Carrier Proteins / metabolism*
  • Cholesterol / metabolism
  • Endoplasmic Reticulum / metabolism*
  • Endosomes / metabolism*
  • Humans
  • Membrane Proteins / metabolism*
  • Protein Binding

Substances

  • Carrier Proteins
  • Membrane Proteins
  • STARD3 protein, human
  • STARD3NL protein, human
  • Cholesterol