Tyrosine kinase inhibitors alter composition of nicotinic receptors on neurons

Haselbeck, Rosalind C.; Berg, Daniela

doi:10.1002/(sici)1097-4695(199612)31:4<404::aid-neu2>3.0.co;2-d

Cited by 6 publications

(7 citation statements)

References 55 publications

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“…In addition, the serine (Ser-530) that is immediately carboxyl-terminal to the A529T polymorphism [DQ (T/A) S*PCK] may be a substrate for the cdc2 family of kinases that includes Cdk5. Phosphorylation of neuronal nAChRs has been shown to influence receptor desensitization or recovery from desensitization (Downing and Role, 1987;Khiroug et al, 1998;Nishizaki and Sumikawa, 1998;Paradiso and Brehm, 1998;Fenster et al, 1999) and may affect receptor trafficking (Haselbeck and Berg, 1996). Therefore, the differences in receptor function observed between the A529T variants of the ␣4 subunit might be explained by differential phosphorylation at or near the site of the polymorphism.…”

Section: Chrna4 Polymorphism Influences Nachr Function In Mice 339mentioning

confidence: 99%

A Polymorphism in the Mouse Neuronal α4 Nicotinic Receptor Subunit Results in An Alteration in Receptor Function

Dobelis

Marks²,

Whiteaker³

et al. 2002

Mol Pharmacol

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Nicotine-stimulated 86 Rb ϩ efflux and [ 3 H]cytisine binding, both of which seem to measure the nicotinic acetylcholine receptor, composed of ␣4 and ␤2 subunits, were assessed in eight brain regions obtained from 14 inbred mouse strains. The potential role of a single nucleotide polymorphism (SNP) in the nicotinic receptor ␣4 subunit gene (Chrna4) on nicotinic receptor binding and function in mice was also evaluated. This SNP leads to an alanine-to-threonine variation at amino acid position 529 of the nascent ␣4 subunit polypeptide. Both nicotine-stimulated 86 Rb ϩ efflux and [ 3 H]cytisine binding were found to vary across brain regions and among mouse strains. Variability in nicotinestimulated 86 Rb ϩ efflux was positively correlated (r Ͼ 0.9) within each strain with the number of [ 3 H]cytisine binding sites.

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Section: Chrna4 Polymorphism Influences Nachr Function In Mice 339mentioning

confidence: 99%

A Polymorphism in the Mouse Neuronal α4 Nicotinic Receptor Subunit Results in An Alteration in Receptor Function

Dobelis

Marks²,

Whiteaker³

et al. 2002

Mol Pharmacol

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“…Protein tyrosine kinase (PTK) inhibitors specifically reduce ␣3-nAChR surface expression in CG neurons, without changing their intracellular levels or ␣7-nAChRs levels (Haselbeck and Berg, 1996). A Ca 2ϩ /calmodulindependent protein kinase (CaM kinase) pathway upregulates ␣7-nAChR expression, but not ␣3-nAChRs in rat SCG neurons in vitro (De Koninck and Cooper, 1995).…”

Section: Molecular Mechanisms That Regulate Neuronal Nachr Expressionmentioning

confidence: 99%

Regulatory mechanisms that govern nicotinic synapse formation in neurons

et al. 2002

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Individual cholinoceptive neurons express high levels of different neuronal nicotinic acetylcholine receptor (nAChR) subtypes, and target them to the appropriate synaptic regions for proper function. This review focuses on the intercellular and intracellular processes that regulate nAChR expression in vertebrate peripheral nervous system (PNS) and central nervous system (CNS) neurons. Specifically, we discuss the cellular and molecular mechanisms that govern the induction and maintenance of nAChR expression-innervation, target tissue interactions, soluble factors, and activity. We define the regulatory principles of interneuronal nicotinic synapse differentiation that have emerged from these studies. We also discuss the molecular players that target nAChRs to the surface membrane and the interneuronal synapse.

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“…Less is known about the effects of tyrosine phosphorylation on neuronal-type nAChRs. Inhibition of protein tyrosine kinases (PTKs) in chick ciliary ganglion neurons causes a slow downregulation in the number of ␣3 subunitcontaining receptors but has little effect on ␣7 nAChRs (De Koninck and Cooper, 1995;Haselbeck and Berg, 1996). Conversely, long-term treatment of hippocampal neurons with neuregulin, which activates receptor PTKs, produces a robust increase in the number of ␣-bungarotoxin (␣BTX)-binding sites and a concomitant increase in ␣7 receptor-mediated currents (Liu et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

Rapid Upregulation of α7 Nicotinic Acetylcholine Receptors by Tyrosine Dephosphorylation

Cho

Song²,

Leitzell³

et al. 2005

J. Neurosci.

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␣7 nicotinic acetylcholine receptors (nAChRs) modulate network activity in the CNS. Thus, functional regulation of ␣7 nAChRs could influence the flow of information through various brain nuclei. It is hypothesized here that these receptors are amenable to modulation by tyrosine phosphorylation. In both Xenopus oocytes and rat hippocampal interneurons, brief exposure to a broad-spectrum protein tyrosine kinase inhibitor, genistein, specifically and reversibly potentiated ␣7 nAChR-mediated responses, whereas a protein tyrosine phosphatase inhibitor, pervanadate, caused depression. Potentiation was associated with an increased expression of surface ␣7 subunits and was not accompanied by detectable changes in receptor open probability, implying that the increased function results from an increased number of ␣7 nAChRs. Soluble N-ethylmaleimide-sensitive factor attachment protein receptor-mediated exocytosis was shown to be a plausible mechanism for the rapid delivery of additional ␣7 nAChRs to the plasma membrane. Direct phosphorylation/ dephosphorylation of ␣7 subunits was unlikely because mutation of all three cytoplasmic tyrosine residues did not prevent the genisteinmediated facilitation. Overall, these data are consistent with the hypothesis that the number of functional cell surface ␣7 nAChRs is controlled indirectly via processes involving tyrosine phosphorylation.

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Tyrosine kinase inhibitors alter composition of nicotinic receptors on neurons

Cited by 6 publications

References 55 publications

A Polymorphism in the Mouse Neuronal α4 Nicotinic Receptor Subunit Results in An Alteration in Receptor Function

A Polymorphism in the Mouse Neuronal α4 Nicotinic Receptor Subunit Results in An Alteration in Receptor Function

Regulatory mechanisms that govern nicotinic synapse formation in neurons

Rapid Upregulation of α7 Nicotinic Acetylcholine Receptors by Tyrosine Dephosphorylation

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