2,2'-Bis(monoacylglycero) PO4 (BMP), but Not 3,1'-BMP, Increases Membrane Curvature Stress to Enhance α-Tocopherol Transfer Protein Binding to Membranes
- Brock Univ., St. Catharines, ON (Canada). Chemistry and Centre for Biotechnology
- Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
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. In this paper, 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. Finally, α-TTP binds to membranes with greater affinity when they contain the 2,2'-BMP versus 3,1'-BMP isomers.
- Research Organization:
- Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC), Basic Energy Sciences (BES)
- DOE Contract Number:
- AC05-00OR2275; FG02-08ER46528
- OSTI ID:
- 1265511
- Journal Information:
- Lipids, Vol. 50, Issue 3; ISSN 0024-4201
- Publisher:
- Springer
- Country of Publication:
- United States
- Language:
- English
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