2. Academic Validation
  3. A novel superfamily of bridge-like lipid transfer proteins

A novel superfamily of bridge-like lipid transfer proteins

  • Trends Cell Biol. 2022 Nov;32(11):962-974. doi: 10.1016/j.tcb.2022.03.011.
Sarah D Neuman 1,  Tim P Levine 2,  Arash Bashirullah 3
Affiliations

Affiliations

  • 1 Division of Pharmaceutical Sciences, University of Wisconsin-Madison, Madison, WI 53705-2222, USA.
  • 2 UCL Institute of Ophthalmology, University College London, 11-43 Bath Street, London, EC1V 9EL, UK. Electronic address: tim.levine@ucl.ac.uk.
  • 3 Division of Pharmaceutical Sciences, University of Wisconsin-Madison, Madison, WI 53705-2222, USA. Electronic address: bashirullah@wisc.edu.
PMID: 35491307 DOI: 10.1016/j.tcb.2022.03.011
Abstract

Lipid transfer proteins mediate nonvesicular transport of lipids at membrane contact sites to regulate the lipid composition of organelle membranes. Recently, a new type of bridge-like lipid transfer protein has emerged; these proteins contain a long hydrophobic groove and can mediate bulk transport of lipids between organelles. Here, we review recent insights into the structure of these proteins and identify a repeating modular unit that we propose to name the repeating β-groove (RBG) domain. This new structural understanding conceptually unifies all the RBG domain-containing lipid transfer proteins as members of an RBG protein superfamily. We also examine the biological functions of these lipid transporters in normal physiology and disease and speculate on the evolutionary origins of RBG proteins in bacteria.

Keywords

AlphaFold; Vps13; autophagy; lipid transfer proteins; lipids; membrane contact sites.

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