2,2'-Bis(monoacylglycero) PO₄ (BMP), but Not 3,1'-BMP, Increases Membrane Curvature Stress to Enhance α-Tocopherol Transfer Protein Binding to Membranes

Journal Article · Wed Jan 21 00:00:00 EST 2015 · Lipids

DOI:https://doi.org/10.1007/s11745-015-3989-9· OSTI ID:1265511

Baptist, Matilda ^[1]; Panagabko, Candace ^[1]; Nickels, Jonathan D. ^[2]; Katsaras, John ^[2]; Atkinson, Jeffrey ^[1]

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1. Brock Univ., St. Catharines, ON (Canada). Chemistry and Centre for Biotechnology
2. 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

Related Subjects

59 BASIC BIOLOGICAL SCIENCES