ArticleThe Journal of cell biology2003
The COOH-terminal domain of agrin signals via a synaptic receptor in central nervous system neurons.
Article in The Journal of cell biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 32 citations in OpenAlex.
- Mice deficient in synaptic protease neurotrypsin show impaired spaced long-term potentiation and blunted learning-induced modulation of dendritic spines.Cellular and molecular life sciences : CMLS · 2023Article
- Dynamic light scattering: a practical guide and applications in biomedical sciences.Biophysical reviews · 2016Review
- The role of agrin in synaptic development, plasticity and signaling in the central nervous system.Neurochemistry international · 2012Review
- T-shaped arrangement of the recombinant agrin G3-IgG Fc protein.Protein science : a publication of the Protein Society · 2011Article
- Agrin downregulation induced by nerve injury contributes to neuropathic pain.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010Article
- Agrin regulation of alpha3 sodium-potassium ATPase activity modulates cardiac myocyte contraction.The Journal of biological chemistry · 2009Article
- Na+/K+ ATPase regulates the expression and localization of acetylcholine receptors in a pump activity-independent manner.Molecular and cellular neurosciences · 2008Article
- HIV-1-infected blood mononuclear cells form an integrin- and agrin-dependent viral synapse to induce efficient HIV-1 transcytosis across epithelial cell monolayer.Molecular biology of the cell · 2005Article
- Agrin mediates a rapid switch from electrical coupling to chemical neurotransmission during synaptogenesis.The Journal of cell biology · 2005Article
- A single pulse of agrin triggers a pathway that acts to cluster acetylcholine receptors.Molecular and cellular biology · 2004Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Agrin is a motor neuron-derived factor that directs formation of the postsynaptic apparatus of the neuromuscular junction. Agrin is also expressed in the brain, raising the possibility that it might serve a related function at neuron-neuron synapses. Previously, we identified an agrin signaling pathway in central nervous system (CNS) neurons, establishing the existence of a neural receptor that mediates responses to agrin. As a step toward identifying this agrin receptor, we have characterized the minimal domains in agrin that bind and activate it. Structures required for agrin signaling in CNS neurons are contained within a 20-kD COOH-terminal fragment of the protein. Agrin signaling is independent of alternative splicing at the z site, but requires sequences that flank it because their deletion results in a 15-kD fragment that acts as an agrin antagonist. Thus, distinct regions within agrin are responsible for receptor binding and activation. Using the minimal agrin fragments as affinity probes, we also studied the expression of the agrin receptor on CNS neurons. Our results show that both agrin and its receptor are concentrated at neuron-neuron synapses. These data support the hypothesis that agrin plays a role in formation and/or function of CNS synapses.
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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.