A5065713713- Neuroscience and Neuropharmacology Research
- Ion channel regulation and function
- Receptor Mechanisms and Signaling
- Photoreceptor and optogenetics research
- Cellular transport and secretion
- Lipid Membrane Structure and Behavior
- Neural dynamics and brain function
- Memory and Neural Mechanisms
- Neuroinflammation and Neurodegeneration Mechanisms
- Genetics and Neurodevelopmental Disorders
- Nicotinic Acetylcholine Receptors Study
- Retinal Development and Disorders
- Protein Kinase Regulation and GTPase Signaling
- Mitochondrial Function and Pathology
- Axon Guidance and Neuronal Signaling
- Neurobiology and Insect Physiology Research
- Neurogenesis and neuroplasticity mechanisms
- Neurotransmitter Receptor Influence on Behavior
- Pain Mechanisms and Treatments
- Alzheimer's disease research and treatments
- Neuroscience and Neural Engineering
- Protein Tyrosine Phosphatases
- RNA regulation and disease
- RNA Research and Splicing
- Ubiquitin and proteasome pathways
Johns Hopkins University
2016-2025
Johns Hopkins Medicine
2016-2025
Discovery Institute
2016-2025
Hospital for Sick Children
2024
California University of Pennsylvania
2024
Rush University Medical Center
2024
Washington University in St. Louis
2024
Cleveland Clinic
2024
Brigham and Women's Hospital
2024
University of Maryland, Baltimore
1992-2022
Both theoretical and experimental work have suggested that central neurons compensate for changes in excitatory synaptic input order to maintain a relatively constant output. We report here inhibition of transmission cultured spinal leads an increase mEPSC amplitudes, accompanied by equivalent the accumulation AMPA receptors at synapses. Conversely, increasing activity decrease decline amplitude. The time course this remodeling is slow, similar metabolic half-life neuronal receptors....
Brief bath application of N-methyl-D-aspartate (NMDA) to hippocampal slices produces long-term synaptic depression (LTD) in CA1 that is (1) sensitive postnatal age, (2) saturable, (3) induced postsynaptically, (4) reversible, and (5) not associated with a change paired pulse facilitation. Chemically LTD (Chem-LTD) homosynaptic are mutually occluding, suggesting common expression mechanism. Using phosphorylation site–specific antibodies, we found induction chem-LTD persistent...
Modulation of postsynaptic AMPA receptors in the brain by phosphorylation may play a role expression synaptic plasticity at central excitatory synapses. It is known from biochemical studies that GluR1 receptor subunits can be phosphorylated within their C terminal cAMP-dependent protein kinase A (PKA), which colocalized with phosphatase calcineurin (i.e., 2B). We have examined effect PKA and on time course, peak open probability ( P O,PEAK ), single-channel properties glutamateevoked...
The PSD-95/SAP90 family of proteins has recently been implicated in the organization synaptic structure. Here, we describe isolation a novel Ras-GTPase activating protein, SynGAP, that interacts with PDZ domains PSD-95 and SAP102 vitro vivo. SynGAP is selectively expressed brain highly enriched at excitatory synapses, where it present large macromolecular complex NMDA receptor. stimulates GTPase activity Ras, suggesting negatively regulates Ras synapses. signaling postsynaptic membrane may...
PSD-95, DLG, ZO-1 (PDZ) domain-mediated protein interactions have been shown to play important roles in the regulation of glutamate receptor function at excitatory synapses. Recent studies demonstrating rapid AMPA during synaptic plasticity suggested that interaction with PDZ domain-containing proteins may be dynamically modulated. Here we show PKC phosphorylation GluR2 subunit differentially modulates its GRIP1 and PICK1. The serine residue [serine-880 (Ser880)] C-terminal sequence (IESVKI)...
Synaptic clustering of neurotransmitter receptors is crucial for efficient signal transduction and integration in neurons. PDZ domain–containing proteins such as PSD-95/SAP90 interact with the intracellular C termini a variety are thought to be important targeting anchoring specific synapses. Here, we show that PICK1 (protein interacting kinase), protein, interacts α-amino-3-hydroxy-5-methyl-isoxazole-4-propionic acid (AMPA) vitro vivo. In neurons, specifically colocalizes AMPA at excitatory...