<b>Tyrosine kinases and synaptic transmission</b>

Boxall, Andrew R.; Lancaster, Barrie

doi:10.1046/j.1460-9568.1998.00009.x

Cited by 46 publications

(41 citation statements)

References 70 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…pp60 c-src , a member of nonreceptor PTK that is inactive when phosphorylated in Tyr-527, is activated via a calcium-dependent tyrosine phosphatase. This activity is further increased by PKC-dependent Ser-12 phosphorylation, illustrating some of the synergistic actions between kinases and phosphatases (see [21]). Such complex cross-talk should be taken into account when the role of one particular kinase is investigated through interventions such as pharmacological or genetic manipulations.…”

mentioning

confidence: 95%

Protein kinases: which one is the memory molecule?

Micheau

Riedel

1999

Cellular and Molecular Life Sciences (CMLS)

127

View full text Add to dashboard Cite

Encoding of new experiences is likely to induce activity-dependent modifications in the brain. Studies in organisms far apart on the phylogenetic scale have shown that similar, sometimes identical, signal transduction pathways subserve plasticity in neuronal systems, and they may play pivotal roles in the formation of long-term memories. It has become evident that phosphorylation/dephosphorylation reactions are critical for the initiation of cellular mechanisms that embody, retain and modify information in neural circuits. Although physiological investigations on synaptic plasticity have had a major impact, we have concentrated our review on behavioural studies that provide direct or indirect evidence for a role of kinases in mechanisms underlying memory formation. From these, it appears that the learning event induces activation of a variety of kinases with specific time courses. For instance, the calcium/calmodulin-dependent protein kinase II seems to participate in an early phase of memory formation. Apparently, activation of both protein tyrosine kinases and mitogen-activated protein kinases is required for much longer and may thus have a particular function during transformation from short-term into long-term memory. Quite different time courses appear for protein kinase C (PKC) and protein kinase A (PKA), which may function at two different time points, shortly after training and again much later. This suggests that PKC and PKA might play a role at early and late stages of memory formation. However, we have considered some examples showing that these signalling pathways do not function in isolation but rather interact in an intricate intracellular network. This is indicative of a more complex contribution of each kinase to the fine tuning of encoding and information processing. To decipher this complexity, pharmacological, biochemical and genetic investigations are more than ever necessary to unravel the role of each kinase in the syntax of learning and memory formation.

show abstract

mentioning

confidence: 95%

Protein kinases: which one is the memory molecule?

Micheau

Riedel

1999

Cellular and Molecular Life Sciences (CMLS)

127

View full text Add to dashboard Cite

show abstract

“…Group I mGlu receptor agonist-evoked responses are enhanced in the spinal cord of hyperalgesic animals and are reversed by the administration of NMDA receptor antagonists (Boxall and Lancaster, 1998). NMDA currents in dorsal horn neurons are potentiated by the activation of group I mGlu receptors (Bleakman et al, 1992;Cerne and Randic, 1992;Bond and Lodge, 1995).…”

Section: G Painmentioning

confidence: 99%

Metabotropic Glutamate 1 Receptor: Current Concepts and Perspectives

Ferraguti

Crepaldi

Nicoletti³

2008

Pharmacol Rev

193

205

View full text Add to dashboard Cite

Almost 25 years after the first report that glutamate can activate receptors coupled to heterotrimeric G-proteins, tremendous progress has been made in the field of metabotropic glutamate receptors. Now, eight members of this family of glutamate receptors, encoded by eight different genes that share distinctive structural features have been identified. The first cloned receptor, the metabotropic glutamate ( mGlu) receptor mGlu1 has probably been the most extensively studied mGlu receptor, and in many respects it represents a prototypical subtype for this family of receptors. Its biochemical, anatomical, physiological, and pharmacological characteristics have been intensely investigated. Together with subtype 5, mGlu1 receptors constitute a subgroup of receptors that couple to phospholipase C and mobilize Ca(2+) from intracellular stores. Several alternatively spliced variants of mGlu1 receptors, which differ primarily in the length of their C-terminal domain and anatomical localization, have been reported. Use of a number of genetic approaches and the recent development of selective antagonists have provided a means for clarifying the role played by this receptor in a number of neuronal systems. In this article we discuss recent advancements in the pharmacology and concepts about the intracellular transduction and pathophysiological role of mGlu1 receptors and review earlier data in view of these novel findings. The impact that this new and better understanding of the specific role of these receptors may have on novel treatment strategies for a variety of neurological and psychiatric disorders is considered

show abstract

“…Several studies have reported that protein tyrosine kinases (PTKs) regulate long-term changes of synaptic transmission at glutamatergic synapses (Boxall and Lancaster, 1998). PTK inhibitors such as genistein, herbimycin A, and lavendustin A have been reported to block the induction of hippocampal LTP and cerebellar LTD (O'Dell et al, 1991;Boxall and Lancaster, 1998).…”

Section: Introductionmentioning

confidence: 99%

Tyrosine Phosphorylation and Regulation of the AMPA Receptor by Src Family Tyrosine Kinases

Hayashi

Huganir²

2004

J. Neurosci.

167

178

View full text Add to dashboard Cite

Phosphorylation of AMPA receptors is a major mechanism for the regulation of receptor function and underlies several forms of synaptic plasticity in the CNS. Although serine and threonine phosphorylation of AMPA receptors has been well studied, the potential role of tyrosine phosphorylation of AMPA receptors has not been investigated. Here, we show that the GluR2 subunit of AMPA receptors is tyrosine phosphorylated in vitro and in vivo by Src family tyrosine kinases on tyrosine 876 near its C terminus. In addition, GluR agonist treatment of cultured cortical neurons increased phosphorylation of tyrosine 876. The association with GluR2-interacting molecules GRIP1/2 was decreased by tyrosine phosphorylation of GluR2, whereas PICK1 interaction was not influenced. Moreover, mutation of tyrosine 876 eliminated AMPA-and NMDA-induced internalization of the GluR2 subunit. These data indicate that tyrosine phosphorylation of tyrosine 876 on the GluR2 C terminus by Src family tyrosine kinases is important for the regulation of AMPA receptor function and may be important for synaptic plasticity.

show abstract

Tyrosine kinases and synaptic transmission

Cited by 46 publications

References 70 publications

Protein kinases: which one is the memory molecule?

Protein kinases: which one is the memory molecule?

Metabotropic Glutamate 1 Receptor: Current Concepts and Perspectives

Tyrosine Phosphorylation and Regulation of the AMPA Receptor by Src Family Tyrosine Kinases

Contact Info

Product

Resources

About