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. 2017 Jan 18;10:618. doi: 10.3389/fnins.2016.00618

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Copyright © 2017 Park, Ji, Kim, An and Yoon.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Increased half-life of TREM2 R47H. (A) HeLa cells transfected with wild-type TREM2 and the R47H variant were treated with cycloheximide (5 μg/μl) for the indicated times. TREM2 R47H decreased more slowly compared with wild-type. (B) The intensity of each band was measured using Image J and relative intensities are plotted. The data represent the mean ± S.E. from three independent experiments. ^*P < 0.05, ^**P < 0.01, ^***P < 0.005. (C) Protein samples from HeLa cells expressing various types of TREM2 were fractionated with digitonin. Both wild-type and TREM2 R47H were present in the membranous organelle fraction (M). This fraction was further fractionated into membrane soluble (MS) and membrane insoluble (MI) fractions. Unglycosylated bands of TREM2 (arrow) were found only in the membranous fractions and not in the cytosolic (c) fraction.