ArticleMolecular biology of the cell2000
Exposure at the cell surface is required for gas3/PMP22 To regulate both cell death and cell spreading: implication for the Charcot-Marie-Tooth type 1A and Dejerine-Sottas diseases.
Article in Molecular biology of the cell, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 55 citations in OpenAlex.
- Peripheral Myelin Protein-22 and Its Prominence in Charcot-Marie-Tooth Disease.Chemical reviews · 2026Review
- Charcot-Marie-Tooth disease type 1E: clinical natural history and molecular impact of PMP22 variants.Brain : a journal of neurology · 2026Article
- Charcot-Marie-Tooth disease type 1E: Clinical Natural History and Molecular Impact ofmedRxiv : the preprint server for health sciences · 2025Article
- AAV-mediated editing of PMP22 rescues Charcot-Marie-Tooth disease type 1A features in patient-derived iPS Schwann cells.Communications medicine · 2023Article
- Charcot Marie Tooth Disease. A Single Disorder?International journal of molecular sciences · 2018Article
- Elevated Peripheral Myelin Protein 22, Reduced Mitotic Potential, and Proteasome Impairment in Dermal Fibroblasts from Charcot-Marie-Tooth Disease Type 1A Patients.The American journal of pathology · 2018Article
- Clinical and Molecular Characterization of PMP22 point mutations in Taiwanese patients with Inherited Neuropathy.Scientific reports · 2017Article
- PMP22 is critical for actin-mediated cellular functions and for establishing lipid rafts.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014Article
- The PMP22 gene and its related diseases.Molecular neurobiology · 2013Review
- Physiology and function of the tight junction.Cold Spring Harbor perspectives in biology · 2009Review
- Peripheral myelin protein 22 is in complex with alpha6beta4 integrin, and its absence alters the Schwann cell basal lamina.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2006Article
- Pathomechanisms of mutant proteins in Charcot-Marie-Tooth disease.Neuromolecular medicine · 2006Review
- Molecular genetics of autosomal-dominant demyelinating Charcot-Marie-Tooth disease.Neuromolecular medicine · 2006Review
- Modulation of epithelial morphology, monolayer permeability, and cell migration by growth arrest specific 3/peripheral myelin protein 22.Molecular biology of the cell · 2005Article
- The tetraspan protein EMP2 modulates the surface expression of caveolins and glycosylphosphatidyl inositol-linked proteins.Molecular biology of the cell · 2004Article
- Peripheral myelin protein 22 is a constituent of intercellular junctions in epithelia.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Gas3/PMP22 is a tetraspan membrane protein highly expressed in myelinating Schwann cells. Point mutations in the gas3/PMP22 gene account for the dominant inherited peripheral neuropathies Charcot-Marie-Tooth type 1A disease (CMT1A) and Dejerine-Sottas syndrome (DSS). Gas3/PMP22 can regulate apoptosis and cell spreading in cultured cells. Gas3/PMP22 point mutations, which are responsible for these diseases, are defective in this respect. In this report, we demonstrate that Gas3/PMP22-WT is exposed at the cell surface, while its point-mutated derivatives are intracellularly retained, colocalizing mainly with the endoplasmic reticulum (ER). The putative retrieval motif present in the carboxyl terminus of Gas3/PMP22 is not sufficient for the intracellular sequestration of its point-mutated forms. On the contrary, the introduction of a retrieval signal at the carboxyl terminus of Gas3/PMP22-WT leads to its intracellular accumulation, which is accompanied by a failure to trigger cell death as well as by changes in cell spreading. In addition, by substituting the Asn at position 41 required for N-glycosylation, we provide evidence that N-glycosylation is required for the full effect on cell spreading, but it is not necessary for triggering cell death. In conclusion, we suggest that the DSS and the CMT1A neuropathies derived from point mutations of Gas3/PMP22 might arise, at the molecular level, from a reduced exposure of Gas3/PMP22 at the cell surface, which is required to exert its biological functions.
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