2,2'-Bis(monoacylglycero) PO4 (BMP), but Not 3,1'-BMP, increases membrane curvature stress to enhance α-tocopherol transfer protein binding to membranes

Lipids. 2015 Mar;50(3):323-8. doi: 10.1007/s11745-015-3989-9. Epub 2015 Jan 21.

Abstract

Previous work revealed that α-tocopherol transfer protein (α-TTP) co-localizes with bis(monoacylglycero)phosphate (BMP) in late endosomes. BMP is a lipid unique to late endosomes and is believed to induce membrane curvature and support the multivesicular nature of this organelle. We examined the effect of BMP on α-TTP binding to membranes using dual polarization interferometry and vesicle-binding assay. α-TTP binding to membranes is increased by the curvature-inducing lipid BMP. α-TTP binds to membranes with greater affinity when they contain the 2,2'-BMP versus 3,1'-BMP isomers.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Carrier Proteins / metabolism*
  • Cell Membrane / physiology*
  • Endosomes / metabolism
  • Humans
  • Interferometry / methods
  • Liver / cytology*
  • Liver / metabolism
  • Phosphates / metabolism*
  • Stress, Physiological

Substances

  • Carrier Proteins
  • Phosphates
  • alpha-tocopherol transfer protein