Journal
NATURE COMMUNICATIONS
Volume 6, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms7826
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Funding
- NIH/NIGMS under NSF [DMR-1332208]
- NIH/NIGMS [GM-103485]
- NSF MRSEC programme [DMR-1120296]
- University of Michigan Nutrition Obesity Center (NORC) core services
- NIH [DK089503, R21DA031409-01, R01GM086596]
- NSF [CBET 1159581, CBET 1264701]
- Div Of Chem, Bioeng, Env, & Transp Sys
- Directorate For Engineering [1159581] Funding Source: National Science Foundation
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Integral membrane proteins (IMPs) play crucial roles in all cells and represent attractive pharmacological targets. However, functional and structural studies of IMPs are hindered by their hydrophobic nature and the fact that they are generally unstable following extraction from their native membrane environment using detergents. Here we devise a general strategy for in vivo solubilization of IMPs in structurally relevant conformations without the need for detergents or mutations to the IMP itself, as an alternative to extraction and in vitro solubilization. This technique, called SIMPLEx (solubilization of IMPs with high levels of expression), allows the direct expression of soluble products in living cells by simply fusing an IMP target with truncated apolipoprotein A-I, which serves as an amphipathic proteic 'shield' that sequesters the IMP from water and promotes its solubilization.
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