Neuman, Sarah D;
Levine, Tim P;
Bashirullah, Arash;
(2022)
A novel superfamily of bridge-like lipid transfer proteins.
Trends in Cell Biology
, 32
(11)
pp. 962-974.
10.1016/j.tcb.2022.03.011.
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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.
| Type: | Article |
|---|---|
| Title: | A novel superfamily of bridge-like lipid transfer proteins |
| Location: | England |
| Open access status: | An open access version is available from UCL Discovery |
| DOI: | 10.1016/j.tcb.2022.03.011 |
| Publisher version: | https://doi.org/10.1016/j.tcb.2022.03.011 |
| Language: | English |
| Additional information: | This version is the author accepted manuscript. For information on re-use, please refer to the publisher's terms and conditions. |
| Keywords: | AlphaFold, Vps13, autophagy, lipid transfer proteins, lipids, membrane contact sites |
| UCL classification: | UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences > Institute of Ophthalmology UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences UCL |
| URI: | https://discovery.ucl.ac.uk/id/eprint/10150146 |
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