Please use this identifier to cite or link to this item: http://hdl.handle.net/2445/180331
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dc.contributor.authorXu, Haijin-
dc.contributor.authorIsenmann, Sandra-
dc.contributor.authorLópez Hernández, Tania-
dc.contributor.authorEstévez, Raúl-
dc.contributor.authorLukacs, Gergely L.-
dc.contributor.authorApaja, Pirjo M.-
dc.date.accessioned2021-10-04T09:38:17Z-
dc.date.available2021-10-04T09:38:17Z-
dc.date.issued2021-09-16-
dc.identifier.issn2045-2322-
dc.identifier.urihttp://hdl.handle.net/2445/180331-
dc.description.abstractThe significance of crosstalks among constituents of plasma membrane protein clusters/complexes in cellular proteostasis and protein quality control (PQC) remains incompletely understood. Examining the glial (enriched) cell adhesion molecule (CAM), we demonstrate its chaperone-like role in the biosynthetic processing of the megalencephalic leukoencephalopathy with subcortical cyst 1 (MLC1)-heteromeric regulatory membrane protein complex, as well as the function of the GlialCAM/MLC1 signalling complex. We show that in the absence of GlialCAM, newly synthesized MLC1 molecules remain unfolded and are susceptible to polyubiquitination-dependent proteasomal degradation at the endoplasmic reticulum. At the plasma membrane, GlialCAM regulates the diffusional partitioning and endocytic dynamics of cluster members, including the ClC-2 chloride channel and MLC1. Impaired folding and/or expression of GlialCAM or MLC1 in the presence of diseases causing mutations, as well as plasma membrane tethering compromise the functional expression of the cluster, leading to compromised endo-lysosomal organellar identity. In addition, the enlarged endo-lysosomal compartments display accelerated acidification, ubiquitinated cargo-sorting and impaired endosomal recycling. Jointly, these observations indicate an essential and previously unrecognized role for CAM, where GliaCAM functions as a PQC factor for the MLC1 signalling complex biogenesis and possess a permissive role in the membrane dynamic and cargo sorting functions with implications in modulations of receptor signalling.-
dc.format.extent17 p.-
dc.format.mimetypeapplication/pdf-
dc.language.isoeng-
dc.publisherSpringer Science and Business Media LLC-
dc.relation.isformatofReproducció del document publicat a: https://doi.org/10.1038/s41598-021-97777-4-
dc.relation.ispartofScientific Reports, 2021, vol. 11, num. 1-
dc.relation.urihttps://doi.org/10.1038/s41598-021-97777-4-
dc.rightscc by (c) Xu, Haijin et al, 2021-
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/es/*
dc.subject.classificationHomeòstasi-
dc.subject.classificationNeuròglia-
dc.subject.otherHomeostasis-
dc.subject.otherNeuroglia-
dc.titleControl of membrane protein homeostasis by a chaperone-like glial cell adhesion molecule at multiple subcellular locations-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/publishedVersion-
dc.identifier.idgrec721291-
dc.date.updated2021-10-01T10:46:52Z-
dc.rights.accessRightsinfo:eu-repo/semantics/openAccess-
dc.identifier.pmid34531445-
Appears in Collections:Articles publicats en revistes (Ciències Fisiològiques)
Articles publicats en revistes (Institut d'lnvestigació Biomèdica de Bellvitge (IDIBELL))

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