Topologically Diverse Human Membrane Proteins Partition to Liquid-Disordered Domains in Phase-Separated Lipid Vesicles.

Schlebach JP, Barrett PJ, Day CA, Kim JH, Kenworthy AK, Sanders CR
Biochemistry. 2016 55 (7): 985-8

PMID: 26859249 · PMCID: PMC4766968 · DOI:10.1021/acs.biochem.5b01154

The integration of membrane proteins into "lipid raft" membrane domains influences many biochemical processes. The intrinsic structural properties of membrane proteins are thought to mediate their partitioning between membrane domains. However, whether membrane topology influences the targeting of proteins to rafts remains unclear. To address this question, we examined the domain preference of three putative raft-associated membrane proteins with widely different topologies: human caveolin-3, C99 (the 99 residue C-terminal domain of the amyloid precursor protein), and peripheral myelin protein 22. We find that each of these proteins are excluded from the ordered domains of giant unilamellar vesicles containing coexisting liquid-ordered and liquid-disordered phases. Thus, the intrinsic structural properties of these three topologically distinct disease-linked proteins are insufficient to confer affinity for synthetic raft-like domains.

MeSH Terms (20)

Amyloid beta-Protein Precursor Caveolin 3 Cholesterol Fluorescent Dyes Humans Hydrophobic and Hydrophilic Interactions Membrane Microdomains Microscopy, Confocal Microscopy, Fluorescence Models, Molecular Myelin Proteins Peptide Fragments Phosphatidylcholines Phosphatidylethanolamines Protein Conformation Protein Interaction Domains and Motifs Recombinant Proteins Rhodamines Sphingomyelins Unilamellar Liposomes

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