Metabotropic glutamate receptor activation causes a rapid redistribution of AMPA receptors

Xiao, Min-Yi; Zhou, Qiang; Nicoll, Roger A.

doi:10.1016/s0028-3908(01)00134-4

Cited by 157 publications

(161 citation statements)

References 23 publications

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“…The potential involvement of p38 MAPK in DHPGinduced loss of surface AMPA receptors was first investigated. In agreement with previous reports (12,13), application of DHPG (50 M) caused a significant reduction in surface expression of AMPA receptors (GluR1: 65.6 Ϯ 6.9% of control slices, n ϭ 5; p Ͻ 0.05) (Fig. 5A).…”

Section: Involvement Of P38 Mapk-stimulated Ampa Receptor Endocytoticsupporting

confidence: 93%

“…It has recently been demonstrated that DHPG-LTD appears to require loss of AMPA receptors from the postsynaptic membrane surface (12,13) and p38 MAPK has been identified to have the ability to accelerate the endocytosis trafficking by stimulating the activity of GDI in extracting Rab5 from endosomal membranes and forming a GDI⅐Rab5 complex (39). This complex is required for ligand sequestration into clathrincoated pits.…”

Section: Involvement Of P38 Mapk-stimulated Ampa Receptor Endocytoticmentioning

confidence: 99%

“…Current studies have reported that the induction of mGluR-dependent LTD does not require extracellular Ca 2ϩ (6), Ca 2ϩ release from intracellular stores (7), activation of Ca 2ϩ /calmodulin-dependent protein kinase II (8), protein kinase A or protein kinase C (7,9), or serine/ threonine protein phosphatases (9). However, this form of LTD requires activation of G q -type G proteins (10), a local translation of dendritic mRNA (5,11), a long-lasting loss of postsynaptic AMPA receptors (12,13), and activation of protein tyrosine phosphatases (14). In addition, more recent studies suggest that p38 MAPK signaling also serves as a signal mediator in the induction of mGluR-dependent LTD (15,16).…”

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confidence: 99%

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Rap1-induced p38 Mitogen-activated Protein Kinase Activation Facilitates AMPA Receptor Trafficking via the GDI·Rab5 Complex

Huang

You

et al. 2004

Journal of Biological Chemistry

166

198

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Recent evidence has emphasized the importance of p38 mitogen-activated protein kinase (MAPK) in the induction of metabotropic glutamate receptor (mGluR)-dependent long term depression (LTD) at hippocampal CA3-CA1 synapses. However, the cascade responsible of mGluR to activate p38 MAPK and the signaling pathway immediately downstream from it to induce synaptic depression is poorly understood. Here, we show that transient activation of group I mGluR with the selective agonist (S)-3,5-dihydroxyphenylglycine (DHPG) activates p38 MAPK through G protein ␤␥-subunit, small GTPase Rap1, and MAPK kinase 3/6 (MKK3/6), thus resulting in mGluR5-dependent LTD. Furthermore, our data clearly show that an accelerating AMPA receptor endocytosis by stimulating the formation of guanyl nucleotide dissociation inhibitor-Rab5 complex is a potential downstream processing of p38 MAPK activation to mediate DHPG-LTD. These results suggest an important role for Rap1-MKK3/6-p38 MAPK pathway in the induction of mGluR-dependent LTD by directly coupling to receptor trafficking machineries to facilitate the loss of synaptic AMPA receptors.Long term depression (LTD) 1 is a persistent activity-dependent decrease of synaptic efficacy that together with the converse process, long term potentiation, has been considered to be crucial for information storage in the brain (1, 2). In the hippocampus, LTD is divided into three categories: homosynaptic, heterosynaptic, and associative LTD (3). The bestcharacterized form of homosynaptic LTD is induced in the CA1 region of the hippocampus by prolonged low frequency synaptic stimulation via a NMDA receptor-dependent rise in postsynaptic [Ca 2ϩ ] i and the activation of serine/threonine protein phosphatases (4). Recent work has shown that mechanistically distinct type of LTD can be induced in the CA1 region by other types of synaptic stimulation or brief pharmacological treatments. For example, a prolonged period of paired-pulse stimulation or a direct application of the selective group I mGluR agonists, such as DHPG, can induce a robust mGluR-dependent form of LTD that is independent of NMDA receptor activation (5). In contrast to the mechanisms of NMDA receptor-dependent LTD, which are fairly well established, the mechanisms of induction and the site of expression of mGluR-dependent LTD are still a matter of some considerable debate. Current studies have reported that the induction of mGluR-dependent LTD does not require extracellular Ca 2ϩ (6), Ca 2ϩ release from intracellular stores (7), activation of Ca 2ϩ /calmodulin-dependent protein kinase II (8), protein kinase A or protein kinase C (7, 9), or serine/ threonine protein phosphatases (9). However, this form of LTD requires activation of G q -type G proteins (10), a local translation of dendritic mRNA (5, 11), a long-lasting loss of postsynaptic AMPA receptors (12, 13), and activation of protein tyrosine phosphatases (14). In addition, more recent studies suggest that p38 MAPK signaling also serves as a signal mediator in the induction of mGluR-depende...

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Section: Involvement Of P38 Mapk-stimulated Ampa Receptor Endocytoticsupporting

confidence: 93%

Section: Involvement Of P38 Mapk-stimulated Ampa Receptor Endocytoticmentioning

confidence: 99%

mentioning

confidence: 99%

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Rap1-induced p38 Mitogen-activated Protein Kinase Activation Facilitates AMPA Receptor Trafficking via the GDI·Rab5 Complex

Huang

You

et al. 2004

Journal of Biological Chemistry

166

198

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“…Moreover, inhibition of caspases and cytochrome c release and overexpression of antiapoptotic proteins of the Bcl-2 family can prolong survival in these models (79,80,84). An overwhelming amount of evidence exists showing that ␣-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid, N-methyl-D-aspartate, and metabotropic (mGlu) glutamate receptors are cleared from the cell surface by endocytosis (85)(86)(87)(88)(89)(90)(91)(92)(93)(94)(95)(96)(97)(98)(99)(100)(101)(102). Rab5 activation is required for the endocytosis of many plasma membrane receptors.…”

Section: Discussionmentioning

confidence: 99%

Alsin Is a Rab5 and Rac1 Guanine Nucleotide Exchange Factor

Topp

Gray

Gerard

et al. 2004

Journal of Biological Chemistry

173

157

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ALS2 is the gene mutated in a recessive juvenile form of amyotrophic lateral sclerosis (ALS2). ALS2 encodes a large protein termed alsin, which contains a number of predicted cell signaling and protein trafficking sequence motifs. To gain insight into the overall function of alsin and to begin to evaluate its role in motor neuron maintenance, we examined the subcellular localization of alsin and the biochemical activities associated with its individual subdomains. We found that the Vps9p domain of alsin has Rab5 guanine nucleotide exchange activity. In addition, alsin interacted specifically with and acted as a guanine nucleotide exchange factor for Rac1. Immunofluorescence and fractionation experiments in both fibroblasts and neurons revealed that alsin is a cytosolic protein, with a significant portion associated with small, punctate membrane structures. Many of these membrane structures also contained Rab5 or Rac1. Upon overexpression of full-length alsin, the overexpressed material was largely cytosolic, indicating that the association with membrane structures could be saturated. We also found that alsin was present in membrane ruffles and lamellipodia. These data suggest that alsin is involved in membrane transport events, potentially linking endocytic processes and actin cytoskeleton remodeling.Amyotrophic lateral sclerosis (ALS) 1 is a heterogeneous neurological disorder characterized by progressive degeneration of motor neurons, usually causing death as a result of respiratory paralysis (1, 2). Although mostly sporadic in nature, a genetic link has been established in 5-10% of ALS cases (3). Chromosomal mapping studies have identified six independent loci associated with the familial forms of ALS (Refs. 4 -10; reviewed in Refs. 11 and 12). Molecular genetic analysis identified two genes that, when mutated, lead to ALS. The first discovered was the gene coding for Cu-Zn superoxide dismutase 1 (SOD1) (10). Initially, mutations in SOD1 were thought to result in defective free radical scavenger activity. However, it is now generally accepted that the alterations in SOD1 that lead to ALS are the result of an unknown, but toxic gain-of-function. The second gene identified is mutated in a juvenile form of ALS, ALS2 (13,14). Mutations in this gene lead to a rare recessive form of ALS that presents early in life and progresses much more slowly than the classical form (6, 15). Two small deletions in ALS2 were originally associated with the disease (13,14). Each is expected to severely truncate the predicted protein product of ALS2. In addition, mutations in ALS2 have recently been associated with two other neurodegenerative disorders, juvenile-onset primary lateral sclerosis (14) and infantile-onset hereditary spastic paralegia (16 -18). Like the original mutations identified, these mutations are predicted to generate prematurely truncated forms of the protein product.The protein encoded by ALS2, alsin, is predicted to contain numerous domains implicating roles in cell signaling, membrane localization, and protein...

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“…In cultured neurons, several stimuli can cause AMPAR internalization, such as the activation of NMDARs Beattie et al, 2000;Ehlers, 2000), AMPARs , mGluRs (Snyder et al, 2001;Xiao et al, 2001) or insulin receptors Man et al, 2000). Receptor internalization may be caused by different signaling pathways, and AMPARs are differentially sorted between recycling and degradative pathways following endocytosis, depending on the endocytic stimulus (Ehlers, 2000;Lin et al, 2000).…”

Section: Vesicular Traffic Synaptic Targeting and Lateral Membrane Dmentioning

confidence: 99%

Regulation of AMPA receptors and synaptic plasticity

et al. 2009

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Metabotropic glutamate receptor activation causes a rapid redistribution of AMPA receptors

Cited by 157 publications

References 23 publications

Rap1-induced p38 Mitogen-activated Protein Kinase Activation Facilitates AMPA Receptor Trafficking via the GDI·Rab5 Complex

Rap1-induced p38 Mitogen-activated Protein Kinase Activation Facilitates AMPA Receptor Trafficking via the GDI·Rab5 Complex

Alsin Is a Rab5 and Rac1 Guanine Nucleotide Exchange Factor

Regulation of AMPA receptors and synaptic plasticity

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