Phosphorylation of Ca2+/calmodulin-dependent protein kinase type ii and the α-amino-3-hydroxy-5-methyl-4-isoxazole propionate (ampa) receptor in response to a threonine-devoid diet

Sharp, James W.; Ross, Catherine M.; Koehnle, Thomas J.; Gietzen, Dorothy W.

doi:10.1016/j.neuroscience.2004.03.066

Cited by 15 publications

(25 citation statements)

References 44 publications

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“…This may suggest that increased phosphorylation levels of GluR1 at serine 831 were likely mediated by CaMKII signaling pathway. This is consistent with in vitro report in which GluR1 at serine 831 was phosphorylated by CaMKII [15,16]. Our results confirm previous studies that phosphorylation of serine 831 of GluR1 modulates redistribution of GluR1 [12,13].…”

Section: Distinct Changes Of Glur1 and Pglur1s831 In Lesioned Striatumsupporting

confidence: 94%

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Changes in Subcellular Distribution and Phosphorylation of GluR1 in Lesioned Striatum of 6-Hydroxydopamine-Lesioned and l-dopa-Treated Rats

Kong

Yang

et al. 2006

Neurochem Res

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Recent evidence has linked striatal amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA) receptor function to the adverse effects of long-term dopaminergic treatment in Parkinson's disease. The phosphorylation of AMPA subunit, GluR1, reflects AMPA receptor activity. To determine whether serine phosphorylation of GluR1 subunit by activation of Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) contributes to the process, we examined the effects of unilateral nigrostriatal depletion with 6-hydroxydopamine and subsequent L: -dopa treatment on motor responses and phosphorylation states. Three weeks of L: -dopa administration to rats shortened the duration of the rotational response. We found a significant reduction in the abundance of both phosphorylated GluR1 at serine-831 site (pGluR1S831) and GluR1 in the cell plasma membrane of lesioned striatum. Chronic treatment of lesioned rats with L: -dopa markedly upregulated the phosphorylation of GluR1 in lesioned striatum with a concomitant normalization of the plasma membrane GluR1 abundance, which lasted at least 1 day after withdrawal of chronic L: -dopa treatment. Our immunostaining data showed that these changes were confined to parvalbumin-positive neurons where GluR1 subunits are exclusively expressed. Both the altered motor response duration and the degree of pGluR1S831 were attenuated by the intrastriatal administration of CaMKII inhibitor KN-93. These findings suggest that activation of CaMKII contributes to both development and maintenance of motor response duration alterations, through a mechanism that involves an increase in pGluR1S831 within parvalbumin-positive neurons.

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Section: Distinct Changes Of Glur1 and Pglur1s831 In Lesioned Striatumsupporting

confidence: 94%

“…CaMKII is a protein kinase that is highly concentrated in the brain and crucial for synaptic plasticity. Activation of CaM-KII is directly involved in the phosphorylation of AMPA receptor GluR1 subunit serine 831 [15,16]. CaMKII has also been linked to the pathogenesis of motor complications [17].…”

Section: Introductionmentioning

confidence: 99%

Changes in Subcellular Distribution and Phosphorylation of GluR1 in Lesioned Striatum of 6-Hydroxydopamine-Lesioned and l-dopa-Treated Rats

Kong

Yang

et al. 2006

Neurochem Res

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“…Thoroughly documented models are available for "conditioned taste aversion" (24, 28, 29, 32-34, 40, 111) and "long-term potentiation" (28, 86), for the learned aversions and memory for place, respectively. Here we address the mechanisms that provide sensing of the IAA deficiency (36, 41, 48, 80) and activation of the neurons in the APC (36, [97][98][99][100].…”

Section: Rejection Of Iaa-deficient Foodmentioning

confidence: 99%

Mechanisms of Food Intake Repression in Indispensable Amino Acid Deficiency

2007

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Animals reject diets that lead to indispensable amino acid (IAA) depletion or deficiency. This behavior is adaptive, as continued IAA depletion is incompatible with maintenance of protein synthesis and survival. Following rejection of the diet, animals begin foraging for a better IAA source and develop conditioned aversions to cues associated with the deficient diet. These responses require a sensory system to detect the IAA depletion and alert the appropriate neural circuitry for the behavior. The chemosensor for IAA deprivation is in the highly excitable anterior piriform cortex (APC) of the brain. Recently, the well-conserved general AA control non-derepressing system of yeast was discovered to be activated by IAA deprivation via uncharged tRNA in mammalian APC. This system provides the sensory limb of the mechanism for recognition of IAA depletion that leads to activation of the APC, diet rejection, and subsequent adaptive strategies.

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“…[26] and calcineurin (CaN) is shown in brain ischemia [31]. CaN is dependent on CaM, which is clearly seen in layer II of the APC [32], reviewed in Sharp et al [13]; CaM makes up 1% of total forebrain protein [33]. CaN (PP2B) is the only known protein serine/threonine phosphatase that is reported to be directly regulated by Ca 2+ /CaM [34]; importantly CaN is the only Ca 2+ -regulated phosphatase in brain [35].…”

Section: Discussionmentioning

confidence: 99%

“…There is increased Ca 2+ in APC slices in vitro [12] upon repletion after the slices had been deprived of an IAA for 2-6 h. Phosphorylated-CaMKII (P-CaMKII), an accepted indicator both of increased intracellular Ca 2+ [Ca 2+ ] i and activated calmodulin (CaM), was increased in the APC of rats 20 min after introduction of an IAA deficient diet [13]. Moreover, Ca 2+ is required for sensing AAs (but not exclusively IAA) by a Ca 2+ receptor [14].…”

Section: Several Lines Of Evidence Suggest That Camentioning

confidence: 99%

Calcium-Dependent Eukaryotic Initiation Factor 2ÃŽÂ± Phosphatase Restores Control to Anterior Piriform Cortex Neural Circuitry after Activation by Essential Amino Acid Deficiency

2016

JNB

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Essential (dietary-indispensable) amino acids (IAA)s are vital precursors for protein synthesis; they cannot be synthesized in metazoans but must be obtained from food to survive. In sensing a reduction of an IAA, the mammalian anterior piriform cortex (APC) is rapidly activated. The initial behavioral response is an abrupt end to an IAA deficient meal about 20 min after meal onset. IAA depletion in the APC activates the conserved eukaryotic initiation factor 2α (eIF2α) kinase, GCN2, via uncharged tRNA. GCN2 kinase activity increases phosphorylation of eIF2α (P-eIF2α), which blocks global protein synthesis. The result is that APC inhibitory elements with short half-lives cannot be replaced. Without their inhibition in this highly sensitive brain area, activation of the glutamatergic output cells ensues. Following APC activation, P-eIF2α must be reduced to release the blockade on protein synthesis and allow recovery of inhibition in the circuit. This completes the homeostatic response, restoring control in the APC. A role for calcium (Ca 2+ ) in regulating P-eIF2α was explored here using Ca 2+ blockers, immunoblotting and electrophysiology in APC brain slices. The responses to IAA depletion in the APC were Ca 2+ dependent, showing a role for Ca 2+ in the system. Yet, the kinase activity of GCN2 was unaffected by intracellular Ca 2+ chelation. Thus, control must be accomplished by phosphatase activity. We suggest that regulation of P-eIF2α, and neuronal stability in the APC, require the activity of protein phosphatase1, a Ca 2+ -dependent subunit of the phosphatase acting on P-eIF2α. This implicates the Ca2+/ calmodulin-dependent calcineurin (Protein Phosphatase 2B/PP2B) as acting with the constitutive repressor of eIF2 phosphorylation (PPP1R15B/CReP) after GCN2 activation in the brain.

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Phosphorylation of Ca2+/calmodulin-dependent protein kinase type ii and the α-amino-3-hydroxy-5-methyl-4-isoxazole propionate (ampa) receptor in response to a threonine-devoid diet

Cited by 15 publications

References 44 publications

Changes in Subcellular Distribution and Phosphorylation of GluR1 in Lesioned Striatum of 6-Hydroxydopamine-Lesioned and l-dopa-Treated Rats

Changes in Subcellular Distribution and Phosphorylation of GluR1 in Lesioned Striatum of 6-Hydroxydopamine-Lesioned and l-dopa-Treated Rats

Mechanisms of Food Intake Repression in Indispensable Amino Acid Deficiency

Calcium-Dependent Eukaryotic Initiation Factor 2ÃŽÂ± Phosphatase Restores Control to Anterior Piriform Cortex Neural Circuitry after Activation by Essential Amino Acid Deficiency

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