ArticleThe Journal of biological chemistry2005
The alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionate receptor trafficking regulator "stargazin" is related to the claudin family of proteins by Its ability to mediate cell-cell adhesion.
Article in The Journal of biological chemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 48 citations in OpenAlex.
- Claudin 24-A novel enhancer of AMPA receptor fidelity.Science advances · 2026Article
- Identification of Expression Quantitative Trait Loci (eQTL) for Adipose-Specific Regulatory Mechanisms in Hanwoo (Korean Cattle).Animals : an open access journal from MDPI · 2025Article
- Intracellular Spermine Is a Key Player in GSG1L's Regulation of Calcium-Permeable AMPAR Channel Conductance and Recovery from Desensitization.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025Article
- Exploring the impact of the stargazin V143L mutation on the dynamics of the AMPA receptor: stargazin complex.Frontiers in cellular neuroscience · 2024Article
- AMPA receptor auxiliary subunits emerged during early vertebrate evolution by neo/subfunctionalization of unrelated proteins.Open biology · 2020Article
- Trafficking of neuronal calcium channels.Neuronal signaling · 2017Review
- A rare schizophrenia risk variant of CACNA1I disrupts CaScientific reports · 2016Article
- Systems Proteomics View of the Endogenous Human Claudin Protein Family.Journal of proteome research · 2016Review
- Transplantation of GABAergic Interneurons into the Neonatal Primary Visual Cortex Reduces Absence Seizures in Stargazer Mice.Cerebral cortex (New York, N.Y. : 1991) · 2015Article
- Claudin-20 promotes an aggressive phenotype in human breast cancer cells.Tissue barriers · 2013Article
- Claudins reign: The claudin/EMP/PMP22/γ channel protein family in C. elegans.Tissue barriers · 2013Review
- Claudins and the modulation of tight junction permeability.Physiological reviews · 2013Review
- Two modes of interaction between the membrane-embedded TARP stargazin's C-terminal domain and the bilayer visualized by electron crystallography.Journal of structural biology · 2011Article
- Regulation of ionotropic glutamate receptors by their auxiliary subunits.Physiology (Bethesda, Md.) · 2010Review
- Transmembrane AMPA receptor regulatory proteins and AMPA receptor function in the cerebellum.Neuroscience · 2009Review
- Physiology and function of the tight junction.Cold Spring Harbor perspectives in biology · 2009Review
- A critical GxxxA motif in the gamma6 calcium channel subunit mediates its inhibitory effect on Cav3.1 calcium current.The Journal of physiology · 2008Article
- Inhibition of recombinant N-type Ca(V) channels by the gamma 2 subunit involves unfolded protein response (UPR)-dependent and UPR-independent mechanisms.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2007Article
- Proteomic and bioinformatic analysis of epithelial tight junction reveals an unexpected cluster of synaptic molecules.Biology direct · 2006Article
- Stargazin and other transmembrane AMPA receptor regulating proteins interact with synaptic scaffolding protein MAGI-2 in brain.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2006Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Mutations in the Cacng2 gene encoding the neuronal transmembrane protein stargazin result in recessively inherited epilepsy and ataxia in "stargazer" mice. Functional studies suggest a dual role for stargazin, both as a modulatory gamma subunit for voltage-dependent calcium channels and as a regulator of post-synaptic membrane targeting for alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionate (AMPA)-type glutamate receptors. Co-immunoprecipitation experiments demonstrate that stargazin can bind proteins of either complex in vivo, but it remains unclear whether it can associate with both complexes simultaneously. Cacng2 is one of eight closely related genes (Cacng1-8) encoding proteins with four transmembrane segments, cytoplasmic termini, and molecular masses between 25 and 44 kDa. This group of Cacng genes constitutes only one branch of a larger monophyletic assembly dominated by over 20 genes encoding proteins known as claudins. Claudins regulate cell adhesion and paracellular permeability as fundamental components of non-neuronal tight junctions. Because stargazin is structurally similar to claudins, we hypothesized that it might also have retained claudin-like functions inherited from a common ancestor. Here, we report that expression of stargazin in mouse L-fibroblasts results in cell aggregation comparable with that produced by claudins, and present evidence that the interaction is heterotypic and calcium dependent. The data suggest that the cell adhesion function of stargazin preceded its current role in neurons as a regulator of either voltage-dependent calcium channels or AMPA receptors. We speculate these complexes may have co-opted the established presence of stargazin at sites of close cell-cell contact to facilitate their own evolving intercellular signaling functions.
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