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. 2019 Oct 15;6:107. doi: 10.3389/fmolb.2019.00107

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Copyright © 2019 Legrand, Martinez, Grélard, Berbon, Morvan, Tawani, Loquet, Mongrand and Habenstein.

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) and the copyright owner(s) 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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Hypothetic model of a comprehensive nanodomain clustering mechanism consolidating the structural data on StREM1.3. (A) PIP mix and sterols increase lipid order over the whole membrane because of their homogeneous distribution (B) RemCA peptides could bind and cluster PIP altogether and recruit sterols in their vicinity. This would reduce the presence of sterols and PIPs in DMPC-d54-rich regions, lowering the |2*S_CD| of the latter. (C) StREM1.3 forms homo-trimers, bringing RemCA domains in vicinity. This might increase the rigidifying effect more efficiently over the whole membrane, considering the size and the stability of the associated objects.