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Article

Glycosylation limits forward trafficking of the tetraspan membrane protein PMP22.

The Journal of biological chemistry - 1 Jan 2000

Marinko Justin T, Wright Madison T, Schlebach Jonathan P, Clowes Katherine R, Heintzman Darren R, Plate Lars, Sanders Charles R

Abstract excerpt

Peripheral myelin protein 22 (PMP22) folds and trafficks inefficiently, with only 20% of newly expressed protein trafficking to the cell surface. This behavior is exacerbated in many of the mutants associated with Charcot-Marie-Tooth disease, motivating further study. Here we characterized the role of N-glycosylation in limiting PMP22 trafficking. We first eliminated N-glycosylation using an N41Q mutation, which...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 33933451
DOI: 10.1016/j.jbc.2021.100719
PMCID: PMC8191293

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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