ArticleThe Journal of cell biology1998
Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells.
Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 129 papers.
What it found
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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
129 citing papers in PubMed.
- Clinical and genetic spectrum of CASK-related disorders in Chinese patients.Journal of neurology · 2026Article
- CASK promotes non-small cell lung cancer growth through coordinated regulation of EGFR expression, trafficking, and p21 expression.Journal of biomedical science · 2026Article
- CASK hypomorph mice display cone photoreceptor dysfunction.bioRxiv : the preprint server for biology · 2026Article
- Review
- Protein 4.1N Plays a Cell Type-Specific Role in Hippocampal Glutamatergic Synapse Regulation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023Article
- Article
- RNA in situ conformation sequencing reveals novel long-range RNA structures with impact on splicing.RNA (New York, N.Y.) · 2023Article
- Diverse Clinical Phenotypes ofGenes · 2023Review
- Adenylyl cyclase 6 plays a minor role in the mouse inner ear and retina.Scientific reports · 2023Article
- A novel missense variant in the CASK gene causes intellectual developmental disorder and microcephaly with pontine and cerebellar hypoplasia.BMC medical genomics · 2022Article
- A de novo variant in CASK gene causing intellectual disability and brain hypoplasia: a case report and literature review.Italian journal of pediatrics · 2022Article
- The Non-Linear Path from Gene Dysfunction to Genetic Disease: Lessons from the MICPCH Mouse Model.Cells · 2022Review
- The Effect of hsa-miR-451b Knockdown on Biological Functions of Gastric Cancer Stem-Like Cells.Biochemical genetics · 2021Article
- Cross-platform validation of neurotransmitter release impairments in schizophrenia patient-derivedProceedings of the National Academy of Sciences of the United States of America · 2021Article
- LIN-10 can promote LET-23 EGFR signaling and trafficking independently of LIN-2 and LIN-7.Molecular biology of the cell · 2021Article
- Golgi localization of the LIN-2/7/10 complex points to a role in basolateral secretion of LET-23 EGFR in theDevelopment (Cambridge, England) · 2021Article
- 4.1N-Mediated Interactions and Functions in Nerve System and Cancer.Frontiers in molecular biosciences · 2021Review
- Colorectal cancer patients withAging · 2020Article
- Calcium/Calmodulin-dependent Serine Protein Kinase-associated Neuro-gastrointestinal Disorder: First Report of a Patient With Hirschsprung's Disease.Journal of neurogastroenterology and motility · 2020Article
- Heparan Sulfate Proteoglycans Biosynthesis and Post Synthesis Mechanisms Combine Few Enzymes and Few Core Proteins to Generate Extensive Structural and Functional Diversity.Molecules (Basel, Switzerland) · 2020Review
69 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issuedWood DF [corrected to Woods DF]
Authors and funding
7 authors.
Funding
Abstract
In Caenorhabditis elegans, mutations in the lin-2 gene inactivate the LET-23 receptor tyrosine kinase/Ras/MAP kinase pathway required for vulval cell differentiation. One function of LIN-2 is to localize LET-23 to the basal membrane domain of vulval precursor cells. LIN-2 belongs to the membrane-associated guanylate kinase family of proteins. We have cloned and characterized the human homolog of LIN-2, termed hCASK, and Northern and Western blot analyses reveal that it is ubiquitously expressed. Indirect immunofluorescence localizes CASK to distinct lateral and/or basal plasma membrane domains in different epithelial cell types. We detect in a yeast two-hybrid screen that the PDZ domain of hCASK binds to the heparan sulfate proteoglycan syndecan-2. This interaction is confirmed using in vitro binding assays and immunofluorescent colocalization. Furthermore, we demonstrate that hCASK binds the actin-binding protein 4.1. Syndecans are known to bind extracellular matrix, and to form coreceptor complexes with receptor tyrosine kinases. We speculate that CASK mediates a link between the extracellular matrix and the actin cytoskeleton via its interaction with syndecan and with protein 4.1. Like other membrane-associated guanylate kinases, its multidomain structure enables it to act as a scaffold at the membrane, potentially recruiting multiple proteins and coordinating signal transduction.
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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.