ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2003
The C264Y missense mutation in the extracellular domain of L1 impairs protein trafficking in vitro and in vivo.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
15 citing papers in PubMed, 32 citations in OpenAlex.
- Mice Mutated in the First Fibronectin Domain of Adhesion Molecule L1 Show Brain Malformations and Behavioral Abnormalities.Biomolecules · 2024Article
- Mice Mutated in the Third Fibronectin Domain of L1 Show Enhanced Hippocampal Neuronal Cell Death, Astrogliosis and Alterations in Behavior.Biomolecules · 2023Article
- Functional Diversity of Neuronal Cell Adhesion and Recognition Molecule L1CAM through Proteolytic Cleavage.Cells · 2022Review
- X-linked partial corpus callosum agenesis with mild intellectual disability: identification of a novel L1CAM pathogenic variant.Neurogenetics · 2021Article
- Impaired neural differentiation and glymphatic CSF flow in theDisease models & mechanisms · 2019Article
- L1CAM and its cell-surface mutants: new mechanisms and effects relevant to the physiology and pathology of neural cells.Journal of neurochemistry · 2013Article
- Differential effects of human L1CAM mutations on complementing guidance and synaptic defects in Drosophila melanogaster.PloS one · 2013Article
- Pathomechanistic characterization of two exonic L1CAM variants located in trans in an obligate carrier of X-linked hydrocephalus.Neurogenetics · 2012Article
- L1 and CHL1 Cooperate in Thalamocortical Axon Targeting.Cerebral cortex (New York, N.Y. : 1991) · 2011Article
- Bioinformatic analysis of pathogenic missense mutations of activin receptor like kinase 1 ectodomain.PloS one · 2011Article
- Role of the cytoplasmic domain of the L1 cell adhesion molecule in brain development.The Journal of comparative neurology · 2010Article
- Pathogenic human L1-CAM mutations reduce the adhesion-dependent activation of EGFR.Human molecular genetics · 2009Article
- Semaphorin-6A controls guidance of corticospinal tract axons at multiple choice points.Neural development · 2008Article
- Brain development in mice lacking L1-L1 homophilic adhesion.The Journal of cell biology · 2004Article
- The unfolded protein response in protein aggregating diseases.Neuromolecular medicine · 2003Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The neural cell adhesion molecule L1, a member of the immunoglobulin superfamily, performs important functions in the developing and adult nervous system and is implicated in neuronal migration and survival, elongation, fasciculation and pathfinding of axons, and synaptic plasticity. This view is in line with the fact that mutations in the L1 gene result in severe neurological syndromes in humans. Patients with missense mutations in the extracellular domain of L1 often develop severe phenotypes. Here, we characterized in vitro and in vivo the missense mutation C264Y, which is located in the extracellular domain of L1 and causes a severe phenotype in humans. Transfection studies in vitro demonstrate that L1 carrying this missense mutation is not expressed at the cell surface but instead is located intracellularly, most likely within the endoplasmic reticulum. Lack of cell surface expression of L1 with a C264Y mutation was confirmed in a transgenic mouse line expressing the C264Y mutation under the control of the L1 promoter in an L1-deficient background. Analysis of these transgenic mice indicates that they represent functional null mutants, phenotypically indistinguishable from L1-deficient mice. These observations corroborate the view that impaired cell surface expression of mutated variants of L1 is a potential explanation for the high number of severe pathogenic mutations identified within the human L1 gene.
Indexed as
Identifiers
12514225PMC6742132W1801672677What 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.