ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2000
Clinical mutations in the L1 neural cell adhesion molecule affect cell-surface expression.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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Who cites it
16 citing papers in PubMed, 41 citations in OpenAlex.
- The Role of the Immunoglobulin Superfamily of Cell Adhesion Molecules in Intellectual Disability.Cells · 2026Review
- Mice Mutated in the First Fibronectin Domain of Adhesion Molecule L1 Show Brain Malformations and Behavioral Abnormalities.Biomolecules · 2024Article
- L1 Syndrome Prenatal Diagnosis Supplemented by Functional Analysis of One L1CAM Gene Missense Variant.Reproductive sciences (Thousand Oaks, Calif.) · 2022Article
- Increased plasmin-mediated proteolysis of L1CAM in a mouse model of idiopathic normal pressure hydrocephalus.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
- A novel L1CAM isoform with angiogenic activity generated by NOVA2-mediated alternative splicing.eLife · 2019Article
- Pathomechanistic characterization of two exonic L1CAM variants located in trans in an obligate carrier of X-linked hydrocephalus.Neurogenetics · 2012Article
- The cell adhesion molecule L1 regulates the expression of choline acetyltransferase and the development of septal cholinergic neurons.Brain and behavior · 2011Article
- Axon initial segment dysfunction in a mouse model of genetic epilepsy with febrile seizures plus.The Journal of clinical investigation · 2010Article
- Pathogenic human L1-CAM mutations reduce the adhesion-dependent activation of EGFR.Human molecular genetics · 2009Article
- Synaptic adhesion-like molecules (SALMs) promote neurite outgrowth.Molecular and cellular neurosciences · 2008Article
- Detection of L1 CAM mutation in a male child with mental retardation.Indian journal of clinical biochemistry : IJCB · 2004Article
- The unfolded protein response in protein aggregating diseases.Neuromolecular medicine · 2003Review
- The C264Y missense mutation in the extracellular domain of L1 impairs protein trafficking in vitro and in vivo.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2003Article
- Targeted ablation of NrCAM or ankyrin-B results in disorganized lens fibers leading to cataract formation.The Journal of cell biology · 2001Article
- Cytoplasmic domain mutations of the L1 cell adhesion molecule reduce L1-ankyrin interactions.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2001Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Mutations in the L1 neural cell adhesion molecule, a transmembrane glycoprotein, cause a spectrum of congenital neurological syndromes, ranging from hydrocephalus to mental retardation. Many of these mutations are single amino acid changes that are distributed throughout the various domains of the protein. Defective herpes simplex virus vectors were used to express L1 protein with the clinical missense mutations R184Q and D598N in the Ig2 and Ig6 extracellular domains, respectively, and S1194L in the cytoplasmic domain. All three mutant proteins were expressed at similar levels in infected cells. Neurite outgrowth of cerebellar granule cells was stimulated on astrocytes expressing wild-type or S1194L L1, whereas those expressing R184Q and D598N L1 failed to increase neurite length. Live cell immunofluorescent staining of L1 demonstrated that most defective vector-infected cells did not express R184Q or D598N L1 on their cell surface. This greatly diminished cell-surface expression occurred in astrocytes, neurons, and non-neural cells. In contrast to wild-type or S1194L L1, the R184Q and D598N L1 proteins had altered apparent molecular weights and remained completely endoglycosidase H (endoH)-sensitive, suggesting incomplete post-translational processing. We propose that some missense mutations in human L1 impede correct protein trafficking, with functional consequences independent of protein activity. This provides a rationale for how expressed, full-length proteins with single amino acid changes could cause clinical phenotypes similar in severity to knock-out mutants.
Indexed as
Identifiers
10908608PMC6772530W2149183584What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.