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  • 1
    Electronic Resource
    Electronic Resource
    Phosphorylation of the Nicotinic Acetylcholine Receptor by Protein Tyrosine Kinases (1995)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 757 (1995), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1995.tb17476.x
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  • 2
    Electronic Resource
    Electronic Resource
    Regulation of distinct AMPA receptor phosphorylation sites during bidirectional synaptic plasticity (2000)
    [s.l.] : Macmillian Magazines Ltd.
    Nature 405 (2000), S. 955-959 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Bidirectional changes in the efficacy of neuronal synaptic transmission, such as hippocampal long-term potentiation (LTP) and long-term depression (LTD), are thought to be mechanisms for information storage in the brain. LTP and LTD may be mediated by the modulation of AMPA ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/35016089
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  • 3
    Electronic Resource
    Electronic Resource
    Phosphorylation of DARPP-32 by Cdk5 modulates dopamine signalling in neurons (1999)
    [s.l.] : Macmillian Magazines Ltd.
    Nature 402 (1999), S. 669-671 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The physiological state of the cell is controlled by signal transduction mechanisms which regulate the balance between protein kinase and protein phosphatase activities. Here we report that a single protein can, depending on which particular amino-acid residue is phosphorylated, function either ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/45251
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  • 4
    Electronic Resource
    Electronic Resource
    GRIP: a synaptic PDZ domain-containing protein that interacts with AMPA receptors (1997)
    [s.l.] : Nature Publishing Group
    Nature 386 (1997), S. 279-284 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The C termini of Shaker-type K+ channels and the NMDA receptor are believed to be involved in their subcellular targeting through their interaction with the synaptic cytoskeletal protein PSD-95/SAP909'10. The structure of PSD-95/SAP9011'12 includes three repeats in the N-terminal region of a newly ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/386279a0
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  • 5
    Electronic Resource
    Electronic Resource
    Electroconvulsive Treatment Induces a Rapid and Transient Increase in Tyrosine Phosphorylatin of a 40-Kilodalton Protein Associated with Microtubule-Associated Protein 2 Kinase Activity (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 56 (1991), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Recent studies have identified protein tyrosine phosphorylation as a major intracellular signaling pathway. However, little is known about regulation of this signaling pathway in neuronal systems. To help identify changes in levels of protein tyrosine phosphorylation in brain, we have utilized specific anti-phosphotyrosine antibodies to detect phosphotyrosine-containing proteins by immunoblotting techniques. We have found that electroconvulsive treatment induces a selective increase in tyrosine phosphorylation of a soluble 40-kDa protein. The rise is rapid and transient, reaching maximal levels at 1–2 min and returning to basal levels by 8 min. The phosphotyrosine-containing 40-kDa protein is most prominent in hippocampus, smaller in neocortex, and not detected in brainstem or cerebellum. A phosphotyrosine-containing 42-kDa protein present in several cell types has recently been identified as a serine/threonine phosphotransferase, referred to as microtubule-associated protein 2 kinase. Comparison of the levels of tyrosine phosphorylation of the 40-kDa protein and microtubule-associated protein 2 kinase activity during column chromatography of hippocampal extracts demonstrates that the phosphotyrosine-containing 40-kDa protein and microtubule-associated protein 2 co-purify. Moreover, the tyrosine phosphorylation of the 40-kDa protein and microtubule-associated protein 2 kinase activity are increased to a similar extent following electroconvulsive treatment. These findings suggest that the phosphotyrosine-containing 40-kDa protein identified in brain is closely related to microtubule-associated protein 2 kinase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1991.tb02574.x
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  • 6
    Electronic Resource
    Electronic Resource
    Tyrosine and Serine Phosphorylation of Dystrophin and the 58-kDa Protein in the Postsynaptic Membrane of Torpedo Electric Organ (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 62 (1994), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Dystrophin associates with a 58-kDa and an 87-kDa protein in the postsynaptic membrane of the Torpedo electric organ. We have previously shown that the 87-kDa protein is a major phosphotyrosine-containing protein in these membranes. Immunoprecipitation of the 87-kDa protein from phosphorylated postsynaptic membranes results in coimmunoprecipitation of additional phosphoproteins. These phosphoproteins are identified as dystrophin and the 58-kDa protein. Monoclonal antibodies to dystrophin and the 58-kDa protein immunoprecipitate phosphorylated forms of these proteins from postsynaptic membranes phosphorylated in vitro. Phosphoamino acid analysis reveals that dystrophin and the 58-kDa protein are phosphorylated on serine and tyrosine residues. In addition, both dystrophin and the 58-kDa protein are shown to be phosphorylated on tyrosine residues in vivo. These results suggest that the synaptic function of dystrophin and its associated proteins, the 58-kDa and 87-kDa proteins, may be modulated by tyrosine and serine protein Phosphorylation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1994.62051947.x
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  • 7
    Electronic Resource
    Electronic Resource
    Generation of Two Forms of the γ-Aminobutyric AcidA Receptor γ-2-Subunit in Mice by Alternative Splicing (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 56 (1991), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: γ-Aminobutyric acidA (GABAA) receptors are multisubunit ligand-gated ion channels which mediate neuronal inhibition by GABA and are composed of at least four subunit types (α, β, γ, and δ). The γ2-subunit appears to be essential for benzodiazepine modulation of GABAA receptor function. In cloning murine γ2-subunits, we isolated cDNAs encoding forms of the subunit that differ by the insertion of eight amino acids, LLRMFSFK, in the major intracellular loop between proposed transmembrane domains M3 and M4. The two forms of the γ2-subunit are generated by alternative splicing, as demonstrated by cloning and partial sequencing of the corresponding gene. The eight-amino-acid insertion encodes a potential consensus serine phosphorylation site for protein kinase C. These results suggest a novel mechanism for the regulation of the GABAA receptor by protein phosphorylation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1991.tb08209.x
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  • 8
    Electronic Resource
    Electronic Resource
    Protein Tyrosine Kinase Activity and Its Endogenous Substrates in Rat Brain: A Subcellular and Regional Survey (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 50 (1988), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The rat CNS contains high levels of tyrosine-specific protein kinases that specifically phosphorylate the tyrosine-containing synthetic peptide poly(Glu80,Tyr20). The phosphorylation of this peptide is rapid and occurs with normal Michaelis-Menten kinetics. Using this peptide to assay for enzyme activity, we have measured the protein tyrosine kinase activity in homogenates from various regions of rat CNS. A marked regional distribution pattern vas observed, with high activity present in cerebellum, hippocampus, olfactory bulb, and pyriform cortex, and low activity in the pons/medulla and spinal cord. The distribution of protein tyrosine kinase activity was examined in various subcellular fractions of rat forebrain. The majority of the activity was associated with the particulate fractions, with enrichment in the crude microsomal (P3) and crude synaptic vesicle (LP2) fractions. Moreover, the subcellular distribution of pp60csrc, a well-characterized protein tyrosine kinase, was examined by immunoblot analysis using an affinity-purified antibody specific for pp60csrc. The subcellular distribution of pp60csrc paralleled the overall protein tyrosine kinase activity. In addition, using an antibody specific for phosphotyrosine, endogenous substrates for protein tyrosine kinases were demonstrated on immunoblots of homogenates from the various regions and the subcellular fractions. The immunoblots revealed numerous phosphotyrosine-containing proteins that were present in many of the CNS regions examined and were associated with specific subcellular fractions. The differences in tyrosine-specific protein kinase activity, and in phosphotyrosine-containing proteins, observed in various regional areas and subcellular fractions may reflect specific functional roles for protein tyrosine kinase activity in mammalian brain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1988.tb03029.x
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  • 9
    Electronic Resource
    Electronic Resource
    Biochemical Characterization and Localization of a Non-N-Methyl-D-Aspartate Glutamate Receptor in Rat Brain (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 58 (1992), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The structure and distribution of non-N-methyl-D-aspartate glutamate receptors in the rat brain were studied using subunit-specific antibodies that recognize the receptor subunit GluRl. The GluRl protein, a 106-kDa glycoprotein, appears predominantly in synaptic plasma membranes, where it is highly enriched in the postsynaptic densities. When synaptic plasma membranes are solubilized with the detergent 3-[(3-cholamidopropyl)dimethylammonio]-l-propanesul-fonate, high-affinity a-amino-3-hydroxy-5-methylisoxazole-4-propionate (AMPA) binding and GluRl immunoreactivity comigrate at a native Mr of 610,000. GluRl is enriched in the hippocampus and cerebellar cortex but is present throughout the CNS. It is found on neuronal cell bodies and processes within most regions of the brain; within the cerebellum, however, it is localized to the Bergmann glia. These data suggest that the GluRl protein is a subunit of multimeric AMPA-preferring glutamate receptors present on neurons and on specialized glia.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1992.tb09370.x
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  • 10
    Electronic Resource
    Electronic Resource
    D1 dopamine receptor stimulation increases GluR1 phosphorylation in postnatal nucleus accumbens cultures (2002)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 81 (2002), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Postsynaptic interactions between dopamine and glutamate receptors in the nucleus accumbens are critical for acute responses to drugs of abuse and for neuroadaptations resulting from their chronic administration. We tested the hypothesis that D1 dopamine receptor stimulation increases phosphorylation of the AMPA receptor subunit GluR1 at the protein kinase A phosphorylation site (Ser845). Nucleus accumbens cell cultures were prepared from postnatal day 1 rats. After 14 days in culture, GluR1 phosphorylation was measured by western blotting using phosphorylation site-specific antibodies. The D1 receptor agonist SKF 81297 increased Ser845 phosphorylation in a concentration- dependent manner, with marked increases occurring within 5 min. This was prevented by the D1 receptor antagonist SCH 23390 and the protein kinase A inhibitor H89, and reproduced by forskolin. The D2 receptor agonist quinpirole attenuated the response to D1 receptor stimulation. Neither D1 nor D2 receptor agonists altered GluR1 phosphorylation at Ser831, the site phosphorylated by protein kinase C and calcium/calmodulin-dependent protein kinase II. In other systems, phosphorylation of GluR1 at Ser845 is associated with enhancement of AMPA receptor currents. Thus, the present results suggest that AMPA receptor transmission in the nucleus accumbens may be augmented by concurrent D1 receptor stimulation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.2002.00877.x
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