TY  - JOUR
A1  - Wang, Songyu
A1  - Powers, Robert
A1  - Gold, Vicki A. M.
A1  - Rapoport, Tom A.
T1  - The ER morphology-regulating lunapark protein induces the formation of stacked bilayer discs
T2  - Life science alliance
N2  - Lunapark (Lnp) is a conserved membrane protein that localizes to and stabilizes three-way junctions of the tubular ER network. In higher eukaryotes, phosphorylation of Lnp may contribute to the conversion of the ER from tubules to sheets during mitosis. Here, we report on the reconstitution of purified Lnp with phospholipids. Surprisingly, Lnp induces the formation of stacked membrane discs. Each disc is a bicelle, with Lnp sitting in the bilayer facing both directions. The interaction between bicelles is mediated by the cytosolic domains of Lnp, resulting in a constant distance between the discs. A phosphomimetic Lnp mutant shows reduced bicelle stacking. Based on these results, we propose that Lnp tethers ER membranes in vivo in a cell cycle–dependent manner. Lnp appears to be the first membrane protein that induces the formation of stacked bicelles.
Y1  - 2018
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/48493
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-484930
SN  - 2575-1077
N1  - © 2018 Wang et al https://creativecommons.org/licenses/by/4.0/
This article is available under a Creative Commons License (Attribution 4.0 International, as described at https://creativecommons.org/licenses/by/4.0/).
VL  - 1
IS  - 1, e201700014
SP  - 1
EP  - 11
PB  - EMBO Press
CY  - Heidelberg
ER  -