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. 2021 Sep 16;11:18435. doi: 10.1038/s41598-021-97777-4

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© The Author(s) 2021

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Cell adhesion molecule (CAM) can act as a chaperone-like molecule to regulate proteostasis and endocytosis. GlialCAM functions as a chaperone-like molecule in the ER by ensuring the conformational maturation of the regulatory membrane protein MLC1 and consequently protects MLC1 against ERAD. As a result, GlialCAM enhances the ER-exit, the PM targeting and the tethering of MLC1 variants. At the PM, GlialCAM regulates the diffusional phase separation of the PM proximity adhesion module, which links GlialCAM to early endocytosis dynamics of at least cluster members MLC1 and chloride channel ClC-2. Misaligned adhesion cluster, probably partly due to the inappropriate stoichiometry upon MLC1 or GlialCAM misfolding/mislocation or lack of expression leads to loss of proteostasis health at the late endosomal/lysosomal compartment. Hence, CAM can shape the dynamics of membrane protein folding QC, the diffusional phase separation at the PM and endocytosis of the proximity adhesion cluster.